Journal articles: 'Proteins Cellular signal transduction'

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Watt, F. M., and R. Sever. "Signal transduction." Journal of Cell Science 114, no. 7 (April 1, 2001): 1247–48. http://dx.doi.org/10.1242/jcs.114.7.1247.

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We are pleased to announce the appointment of John Heath as an Editor of Journal of Cell Science. John has a background in developmental biology and has for many years been a leading figure in the field of growth factor and cytokine signalling. Our desire to appoint a new Editor is in part due to the continuing increase in the number of submissions? a consequence of our rising impact factor and author-friendly policies? and in part to our need for another expert in the field of signal transduction among the Editors. On behalf of all the Editors, we would like to welcome John to JCS; we look forward to working with him. The appointment of John Heath coincides with the start of a series of Commentaries focusing on Signal Transduction and Cellular Organization, which will be a feature of JCS throughout 2001. This series is intended to reflect our increasing understanding of the organization of signalling networks, which are no longer viewed merely as linear pathways but instead as complex webs in which scaffold-organized multiprotein complexes and subcellular localization of signalling molecules play key roles. Morgan Sheng's summary of the scaffold functions of PSD-95 in the post-synaptic density (see Cell Science at a Glance) underlines this complexity: PSD-95 is part of an extensive network of proteins that links together different classes of glutamate receptor and couples them to intracellular signalling pathways. In the first Commentary of this series (p. 1253), Bruce Mayer examines the roles of SH3 domains in signalling and discusses the overall logic governing signalling networks. On p. 1265, Graeme Milligan develops the theme by reviewing the evidence for regulation of G-protein-coupled receptor signalling through receptor oligomerization. Future articles in the series examine the importance of subcellular localization of signalling molecules such as Ca(2+), inositol phosphates and Ras, scaffold proteins such as STE5, KSR and AKAPs, and proteins such as p300/CBP and WASP that play central roles integrating signalling to produce biological output (see over). Finally, we would like to emphasize our interest in primary articles relating to this topic and take this opportunity to encourage all those working in the field of signal transduction to submit their best articles to the journal.?

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Ortegón Salas, Clara, Katharina Schneider, Christopher Horst Lillig, and Manuela Gellert. "Signal-regulated oxidation of proteins via MICAL." Biochemical Society Transactions 48, no. 2 (March 27, 2020): 613–20. http://dx.doi.org/10.1042/bst20190866.

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Processing of and responding to various signals is an essential cellular function that influences survival, homeostasis, development, and cell death. Extra- or intracellular signals are perceived via specific receptors and transduced in a particular signalling pathway that results in a precise response. Reversible post-translational redox modifications of cysteinyl and methionyl residues have been characterised in countless signal transduction pathways. Due to the low reactivity of most sulfur-containing amino acid side chains with hydrogen peroxide, for instance, and also to ensure specificity, redox signalling requires catalysis, just like phosphorylation signalling requires kinases and phosphatases. While reducing enzymes of both cysteinyl- and methionyl-derivates have been characterised in great detail before, the discovery and characterisation of MICAL proteins evinced the first examples of specific oxidases in signal transduction. This article provides an overview of the functions of MICAL proteins in the redox regulation of cellular functions.

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Bonventre, J. V. "Phospholipase A2 and signal transduction." Journal of the American Society of Nephrology 3, no. 2 (August 1992): 128–50. http://dx.doi.org/10.1681/asn.v32128.

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Phospholipases A2 (PLA2) comprise a family of enzymes that hydrolyze the acyl bond at the sn-2 position of phospholipids to generate free fatty acids and lysophospholipids. Different forms of PLA2 are involved in digestion, inflammation, and intercellular and intracellular signal transduction. The sn-2 position of phospholipids in mammalian cells is enriched in arachidonic acid, the precursor of eicosanoids, which have diverse physiologic and pathophysiologic effects on the kidney and other organs. Thus, the regulation of PLA2 activity has important implications for kidney function. PLA2 regulation involves: calcium, pH, protein kinases, GTP-binding proteins, inhibitory and activating proteins, metabolic product inhibition, and transcriptional control. The various roles of arachidonic acid and cyclooxygenase, lipoxygenase, and cytochrome P450 mono-oxygenase products of arachidonic acid metabolism, as intracellular messengers, in the regulation of membrane channel activities, intracellular enzyme activities, cellular calcium homeostasis, mitogenesis, differentiation, cytokine and early response gene expression are discussed.

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Finley, Rebecca S. "New Directions in the Treatment of Cancer: Inhibition of Signal Transduction." Journal of Pharmacy Practice 15, no. 1 (February 2002): 5–16. http://dx.doi.org/10.1106/cj0v-jb04-vbd4-v65d.

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In recent years, it has become increasingly apparent that proteins regulated by activated oncogenes or mutated tumor suppressor genes are responsible for the transformation of normal cells to malignant cells as well as for malignant characteristics such as uncontrolled cellular proliferation and the development of metastases. These proteins may be soluble factors, receptors on cell surfaces, or intracellular enzymes that produce signals that stimulate cellular development or proliferation. This process is called signal transduction .In many cases, increased amounts of these proteins have been demonstrated in cancer cells (over normal cells) and have been found to carry prognostic significance. New approaches in cancer treatment are being designed to block such proteins; this approach is termed signal transduction inhibition. !Specific protein targets that anticancer therapies have been developed to inhibit include epidermal growth factor receptors, tyrosine kinase, farnesyl transferase, and various promoters of angiogenesis.

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Hou, Shangwei, Mark F. Reynolds, Frank T. Horrigan, Stefan H. Heinemann, and Toshinori Hoshi. "Reversible Binding of Heme to Proteins in Cellular Signal Transduction." Accounts of Chemical Research 39, no. 12 (December 2006): 918–24. http://dx.doi.org/10.1021/ar040020w.

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Stacey, D. W., M. H. Tsai, C. L. Yu, and J. K. Smith. "Critical Role of Cellular ras Proteins in Proliferative Signal Transduction." Cold Spring Harbor Symposia on Quantitative Biology 53 (January 1, 1988): 871–81. http://dx.doi.org/10.1101/sqb.1988.053.01.100.

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Slemmon, J. Randall, Bingbing Feng, and Joseph A. Erhardt. "Small Proteins that Modulate Calmodulin-Dependent Signal Transduction." Molecular Neurobiology 22, no. 1-3 (2000): 099–114. http://dx.doi.org/10.1385/mn:22:1-3:099.

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Lee, Bok-Soo, Sun-Hwa Lee, Pinghui Feng, Heesoon Chang, Nam-Hyuk Cho, and Jae U. Jung. "Characterization of the Kaposi's Sarcoma-Associated Herpesvirus K1 Signalosome." Journal of Virology 79, no. 19 (October 1, 2005): 12173–84. http://dx.doi.org/10.1128/jvi.79.19.12173-12184.2005.

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ABSTRACT Kaposi's sarcoma (KS) is a multifocal angiogenic tumor and appears to be a hyperplastic disorder caused, in part, by local production of inflammatory cytokines. The K1 lymphocyte receptor-like protein of KS-associated herpesvirus (KSHV) efficiently transduces extracellular signals to elicit cellular activation events through its cytoplasmic immunoreceptor tyrosine-based activation motif (ITAM). To further delineate K1-mediated signal transduction, we purified K1 signaling complexes and identified its cellular components. Upon stimulation, the K1 ITAM was efficiently tyrosine phosphorylated and subsequently interacted with cellular Src homology 2 (SH2)-containing signaling proteins Lyn, Syk, p85, PLCγ2, RasGAP, Vav, SH2 domain-containing protein tyrosine phosphatase 1/2, and Grab2 through its phosphorylated tyrosine residues. Mutational analysis demonstrated that each tyrosine residue of K1 ITAM contributed to the interactions with cellular signaling proteins in distinctive ways. Consequently, these interactions led to the marked augmentation of cellular signal transduction activity, evidenced by the increase of cellular tyrosine phosphorylation and intracellular calcium mobilization, the activation of NF-AT and AP-1 transcription factor activities, and the production of inflammatory cytokines. These results demonstrate that KSHV K1 effectively recruits a set of cellular SH2-containing signaling molecules to form the K1 signalosome, which elicits downstream signal transduction and induces inflammatory cytokine production.

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Periyasamy, C. Periyasamy. "Analysis of Regulated Kinase Signal Network through Feedback Loops in Extra-Cellular Signal." Indonesian Journal of Electrical Engineering and Computer Science 8, no. 2 (November 1, 2017): 549. http://dx.doi.org/10.11591/ijeecs.v8.i2.pp549-551.

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<p>Signal network assumes a vital part in directing the principal cell capacities, for example, cell expansion, survival, separation and motility. Improvement and investigation of scientific model can help us gain a profound comprehension of the unpredictable conduct of ERK flag transduction organizes. This paper exhibits a computational model that offers an incorporated quantitative and dynamic reproduction of ERK flag transduction arranges, actuated by epidermal development figure. The mathematic demonstrate contains the enactment energy of the pathway, a huge number of input circles and association of platform proteins. The model gives knowledge into flag reaction connections between the authoritative of EGF to its receptor at the phone surface and actuation of downstream proteins in the flagging course. The diverse impact of positive and negative input circles of the ERK flag transduction pathway were for the most part examined, showing that criticism circles were the primary affecting variable to the swaying of ERK flag transduction pathway. The forecasts of this wavering of ERK enactment concur well with the writing. It can prompt flag floods of the downstream substrates and instigate relating natural practices.</p>

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Kramer, Markus M., Levin Lataster, Wilfried Weber, and Gerald Radziwill. "Optogenetic Approaches for the Spatiotemporal Control of Signal Transduction Pathways." International Journal of Molecular Sciences 22, no. 10 (May 18, 2021): 5300. http://dx.doi.org/10.3390/ijms22105300.

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Biological signals are sensed by their respective receptors and are transduced and processed by a sophisticated intracellular signaling network leading to a signal-specific cellular response. Thereby, the response to the signal depends on the strength, the frequency, and the duration of the stimulus as well as on the subcellular signal progression. Optogenetic tools are based on genetically encoded light-sensing proteins facilitating the precise spatiotemporal control of signal transduction pathways and cell fate decisions in the absence of natural ligands. In this review, we provide an overview of optogenetic approaches connecting light-regulated protein-protein interaction or caging/uncaging events with steering the function of signaling proteins. We briefly discuss the most common optogenetic switches and their mode of action. The main part deals with the engineering and application of optogenetic tools for the control of transmembrane receptors including receptor tyrosine kinases, the T cell receptor and integrins, and their effector proteins. We also address the hallmarks of optogenetics, the spatial and temporal control of signaling events.

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Prado, M. A., B. Evans-Bain, S. L. Santi, and I. M. Dickerson. "The Role of Cgrp-Receptor Component Protein (Rcp) in Cgrp-Mediated Signal Transduction." Scientific World JOURNAL 1 (2001): 12. http://dx.doi.org/10.1100/tsw.2001.435.

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The calcitonin gene-related peptide (CGRP)-receptor component protein (RCP) is a 17-kDa intracellular peripheral membrane protein required for signal transduction at CGRP receptors. To determine the role of RCP in CGRP-mediated signal transduction, RCP was depleted from NIH3T3 cells using antisense strategy. Loss of RCP protein correlated with loss of cAMP production by CGRP in the antisense cells. In contrast, loss of RCP had no effect on CGRP-mediated binding; therefore RCP is not acting as a chaperone for the CGRP receptor. Instead, RCP is a novel signal transduction molecule that couples the CGRP receptor to the cellular signal transduction machinery. RCP thus represents a prototype for a new class of signal transduction proteins that are required for regulation of G protein-coupled receptors.

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KHOLODENKO, Boris N., Guy C. BROWN, and Jan B. HOEK. "Diffusion control of protein phosphorylation in signal transduction pathways." Biochemical Journal 350, no. 3 (September 8, 2000): 901–7. http://dx.doi.org/10.1042/bj3500901.

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Multiple signalling proteins are phosphorylated and dephosphorylated at separate cellular locations, which potentially causes spatial gradients of phospho-proteins within the cell. We have derived relationships that enable us to estimate the extent to which a protein kinase, a phosphatase and the diffusion of signalling proteins control the protein phosphorylation flux and the phospho-protein gradient. Two different cellular geometries were analysed: (1) the kinase is located on one planar membrane and the phosphatase on a second parallel planar membrane, and (2) the kinase is located on the plasma membrane of a spherical cell and the phosphatase is distributed homogeneously in the cytoplasm. We demonstrate that the control contribution of protein diffusion is potentially significant, given the measured rates for protein kinases, phosphatases and diffusion. If the distance between the membranes is 1µm or greater, the control by diffusion can reach 33% or more, with the rest of the control (67%) shared by the kinase and the phosphatase. At distances of less than 0.1µm, diffusion does not limit protein phosphorylation. For a spherical cell of radius 10µm, a protein diffusion coefficient of 10-8cm2·s-1 and rate constants for the kinase and the phosphatase of approx. 1s-1, control over the phosphorylation flux resides mainly with the phosphatase and protein diffusion, with approximately equal contributions of each of these. The ratio of phospho-protein concentrations at the cell membrane and the cell centre (the dynamic compartmentation of the phospho-protein) is shown to be controlled by the rates of the protein phosphatase and of diffusion. The kinase can contribute significantly to the control of the absolute value of the phospho-protein gradient.

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Mooibroek, Marilyn J., and Jerry H. Wang. "Integration of signal-transduction processes." Biochemistry and Cell Biology 66, no. 6 (June 1, 1988): 557–66. http://dx.doi.org/10.1139/o88-066.

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The adenylate cyclase – cAMP, phospholipase C – IP3 (inositol 1,4,5-triphosphate), and DAG (diacylglycerol) signal transduction systems are used to illustrate general principles underlying the process of information transfer during cell stimulation. Both systems consist of reaction cascades that convert the external signal to an intracellular messenger, translate the messenger to regulatory activities, and then modulate the activities of appropriate cellular proteins to result in specific cell responses. Almost all of these reactions are under second-messenger-dependent regulation, with many being regulated by multiple messengers. Such complex regulation provides ample opportunities for the fine-tuning of the signal cascades and for coordination between cascades during cell stimulation. Specific examples are used to illustrate how the cell uses different intrasystem and intersystem regulatory reactions to achieve specific responses.

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Bachrach, Uriel, Yong-Chun Wang, and Amalia Tabib. "Polyamines: New Cues in Cellular Signal Transduction." Physiology 16, no. 3 (June 2001): 106–9. http://dx.doi.org/10.1152/physiologyonline.2001.16.3.106.

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The naturally occurring polyamines putrescine, spermidine, and spermine are involved in signal transduction. This has been demonstrated by using inhibitors for polyamine biosynthesis (such as α-difluoromethylornithine) or adding polyamines to cultured cells. Different polyamines, preferentially activated protein kinases (tyrosine kinases and MAP kinases), stimulated the expression of nuclear protooncogenes (myc, jun, and fos).

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Radchenko, Martha, and Mike Merrick. "The role of effector molecules in signal transduction by PII proteins." Biochemical Society Transactions 39, no. 1 (January 19, 2011): 189–94. http://dx.doi.org/10.1042/bst0390189.

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PII proteins are one of the most widely distributed signal transduction proteins in Nature, being ubiquitous in bacteria, archaea and plants. They act by protein–protein interaction to control the activities of a wide range of enzymes, transcription factors and transport proteins, the great majority of which are involved in cellular nitrogen metabolism. The regulatory activities of PII proteins are mediated through their ability to bind the key effector metabolites 2-OG (2-oxoglutarate), ATP and ADP. However, the molecular basis of these regulatory effects remains unclear. Recent advances in the solution of the crystal structures of PII proteins complexed with some of their target proteins, as well as the identification of the ATP/ADP- and 2-OG-binding sites, have improved our understanding of their mode of action. In all of the complex structures solved to date, the flexible T-loops of PII facilitate interaction with the target protein. The effector molecules appear to play a key role in modulating the conformation of the T-loops and thereby regulating the interactions between PII and its targets.

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Henn, V., E. Stefan, G. S. Baillie, M. D. Houslay, W. Rosenthal, and E. Klussmann. "Compartmentalized cAMP signalling regulates vasopressin-mediated water reabsorption by controlling aquaporin-2." Biochemical Society Transactions 33, no. 6 (October 26, 2005): 1316–18. http://dx.doi.org/10.1042/bst0331316.

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The cAMP/PKA (protein kinase A) signalling pathway is activated by a plethora of stimuli. To facilitate the specificity of a cellular response, signal transduction complexes are formed and segregated to discrete sites (compartmentalization). cAMP/PKA signalling compartments are maintained by AKAPs (A-kinase anchoring proteins) which bind PKA and other signalling proteins, and by PDEs (phosphodiesterases). The latter hydrolyse cAMP and thus limit its diffusion and terminate PKA activity. An example of a cAMP-dependent process requiring compartmentalization of cAMP/PKA signals is arginine-vasopressin-regulated water reabsorption in renal principal cells. A detailed understanding of the protein interactions within a signal transduction complex offers the possibility to design agents influencing PKA binding to a specific AKAP, the targeting of an AKAP or the interactions of AKAPs with other signalling molecules. The ability to specifically modulate selected branches of a signal transduction pathway would greatly advance basic research, and may lead to new drugs suitable for the treatment of diseases caused by dysregulation of anchored PKA signalling (e.g. renal and cardiovascular diseases).

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Ciambrone, Gary J., Vivian F. Liu, Deborah C. Lin, Ryan P. McGuinness, Gordon K. Leung, and Simon Pitchford. "Cellular Dielectric Spectroscopy: A Powerful New Approach to Label-Free Cellular Analysis." Journal of Biomolecular Screening 9, no. 6 (September 2004): 467–80. http://dx.doi.org/10.1177/1087057104267788.

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The past decade has seen a number of significant changes in identifying higher quality lead compounds earlier in the drug discovery process. Cell-based assay technologies yielding high-content information have emerged to achieve this goal. Although most of these systems are based on fluorescence detection, this article describes the development and application of an innovative cellular assay technology based on radio frequency spectrometry and bioimpedance measurements. Using this technique, the authors have discovered a link between cellular bioimpedance changes and receptor-mediated signal transduction events. By performing dielectric spectroscopy of cells across as pectrum of frequencies (1 KHz to 110 MHz), a series of receptor-specific, frequency-dependent impedance patterns is collected. These raw data patterns are used to determine the identity of the cellular receptor-signaling pathway being tested and to quantify stimulation endpoints and kinetics. The authors describe the application of this technology to the analysis of ligand-induced cellular responses mediated by the 3 major classes of G-protein-coupled receptors (GPCRs) and protein tyrosine kinase receptors. This single assay platform can be used with ease to monitor Gs, Gi, and Gq GPCRs without the need for chimeric or promiscuous G-proteins, fluorophors, or tagged proteins. In contrast to other methods of monitoring cellular signal transduction, this approach provides high information content in a simplified, noninvasive, and biologically relevant fashion.

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Jethmalani, Yogita, and Erin M. Green. "Using Yeast to Define the Regulatory Role of Protein Lysine Methylation." Current Protein & Peptide Science 21, no. 7 (September 23, 2020): 690–98. http://dx.doi.org/10.2174/1389203720666191023150727.

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The post-translational modifications (PTM) of proteins are crucial for cells to survive under diverse environmental conditions and to respond to stimuli. PTMs are known to govern a broad array of cellular processes including signal transduction and chromatin regulation. The PTM lysine methylation has been extensively studied within the context of chromatin and the epigenetic regulation of the genome. However, it has also emerged as a critical regulator of non-histone proteins important for signal transduction pathways. While the number of known non-histone protein methylation events is increasing, the molecular functions of many of these modifications are not yet known. Proteomic studies of the model system Saccharomyces cerevisiae suggest lysine methylation may regulate a diversity of pathways including transcription, RNA processing, translation, and signal transduction cascades. However, there has still been relatively little investigation of lysine methylation as a broad cellular regulator beyond chromatin and transcription. Here, we outline our current state of understanding of non-histone protein methylation in yeast and propose ways in which the yeast system can be leveraged to develop a much more complete picture of molecular mechanisms through which lysine methylation regulates cellular functions.

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Das, Tanuza, Eun Joo Song, and Eunice EunKyeong Kim. "The Multifaceted Roles of USP15 in Signal Transduction." International Journal of Molecular Sciences 22, no. 9 (April 29, 2021): 4728. http://dx.doi.org/10.3390/ijms22094728.

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Ubiquitination and deubiquitination are protein post-translational modification processes that have been recognized as crucial mediators of many complex cellular networks, including maintaining ubiquitin homeostasis, controlling protein stability, and regulating several signaling pathways. Therefore, some of the enzymes involved in ubiquitination and deubiquitination, particularly E3 ligases and deubiquitinases, have attracted attention for drug discovery. Here, we review recent findings on USP15, one of the deubiquitinases, which regulates diverse signaling pathways by deubiquitinating vital target proteins. Even though several basic previous studies have uncovered the versatile roles of USP15 in different signaling networks, those have not yet been systematically and specifically reviewed, which can provide important information about possible disease markers and clinical applications. This review will provide a comprehensive overview of our current understanding of the regulatory mechanisms of USP15 on different signaling pathways for which dynamic reverse ubiquitination is a key regulator.

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Lee, Sun-Hwa, Young-Hwa Chung, Nam-Hyuk Cho, Yousang Gwack, Pinghui Feng, and Jae U. Jung. "Modulation of T-Cell Receptor Signal Transduction by Herpesvirus Signaling Adaptor Protein." Molecular and Cellular Biology 24, no. 12 (June 15, 2004): 5369–82. http://dx.doi.org/10.1128/mcb.24.12.5369-5382.2004.

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ABSTRACT Because of its central regulatory role, T-cell receptor (TCR) signal transduction is a common target of viruses. We report here the identification of a small signaling protein, ORF5, of the T-lymphotropic tumor virus herpesvirus saimiri (HVS). ORF5 is predicted to contain 89 to 91 amino acids with an amino-terminal myristoylation site and six SH2 binding motifs, showing structural similarity to cellular LAT (linker for activation of T cells). Sequence analysis showed that, despite extensive sequence variation, the myristoylation site and SH2 binding motifs were completely conserved among 13 different ORF5 isolates. Upon TCR stimulation, ORF5 was efficiently tyrosine phosphorylated and subsequently interacted with cellular SH2-containing signaling proteins Lck, Fyn, SLP-76, and p85 through its tyrosine residues. ORF5 expression resulted in the marked augmentation of TCR signal transduction activity, evidenced by increased cellular tyrosine phosphorylation, intracellular calcium mobilization, CD69 surface expression, interleukin-2 production, and activation of the NF-AT, NF-κB, and AP-1 transcription factors. Despite its structural similarity to cellular LAT, however, ORF5 could only partially substitute for LAT function in TCR signal transduction. These results demonstrate that HVS utilizes a novel signaling protein, ORF5, to activate TCR signal transduction. This activation probably facilitates viral gene expression and, thereby, persistent infection.

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Sugiura, Reiko, Ryosuke Satoh, Shunji Ishiwata, Nanae Umeda, and Ayako Kita. "Role of RNA-Binding Proteins in MAPK Signal Transduction Pathway." Journal of Signal Transduction 2011 (April 5, 2011): 1–8. http://dx.doi.org/10.1155/2011/109746.

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Mitogen-activated protein kinases (MAPKs), which are found in all eukaryotes, are signal transducing enzymes playing a central role in diverse biological processes, such as cell proliferation, sexual differentiation, and apoptosis. The MAPK signaling pathway plays a key role in the regulation of gene expression through the phosphorylation of transcription factors. Recent studies have identified several RNA-binding proteins (RBPs) as regulators of MAPK signaling because these RBPs bind to the mRNAs encoding the components of the MAPK pathway and regulate the stability of their transcripts. Moreover, RBPs also serve as targets of MAPKs because MAPK phosphorylate and regulate the ability of RBPs to bind and stabilize target mRNAs, thus controlling various cellular functions. In this review, we present evidence for the significance of the MAPK signaling in the regulation of RBPs and their target mRNAs, which provides additional information about the regulatory mechanism underlying gene expression. We further present evidence for the clinical importance of the posttranscriptional regulation of mRNA stability and its implications for drug discovery.

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Coxon, Patricia Y., James T. Summersgill, Julio A. Ramirez, and Richard D. Miller. "Signal Transduction during Legionella pneumophila Entry into Human Monocytes." Infection and Immunity 66, no. 6 (June 1, 1998): 2905–13. http://dx.doi.org/10.1128/iai.66.6.2905-2913.1998.

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ABSTRACT Legionella pneumophila causes Legionnaires’ disease by replication in alveolar macrophages and monocytes. The bacteria are internalized most efficiently by opsonin-dependent, CR3-mediated phagocytosis. This investigation focused on determining the role of actin polymerization and phosphorylation signals in this uptake mechanism. Uptake inhibition assays and confocal microscopic analysis indicated that entry of L. pneumophila activated tyrosine kinase (TK) and protein kinase C (PKC) and induced actin polymerization at the site of bacterial entry. Upon L. pneumophila entry, six major cellular proteins (75, 71, 59, 56, 53, and 52 kDa) were TK phosphorylated in soluble fractions of monocytes, and three of these proteins (52, 53, and 56 kDa) were consistently found in insoluble (i.e., cytoskeletal) fractions of monocytes as well. Tyrosine phosphorylation was suppressed when cells were pretreated with the kinase inhibitor genistein, tyrphostin, or staurosporine. A similar tyrosine-phosphorylated protein pattern was observed with CR3-mediated entry of avirulent L. pneumophila, Escherichia coli, or zymosan into monocytes. This study has shown that PKC and TK signals which activate actin polymerization during the process of phagocytosis are induced upon L. pneumophila entry. In addition, CR3 receptor-mediated phagocytosis into monocytes may involve tyrosine phosphorylation of similar proteins, regardless of the particle being phagocytosed. Therefore, the tyrosine-induced phosphorylation observed during opsonized L. pneumophilaentry is not a virulence-associated event.

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Fraser, Paul E., Gang Yu, Lyne Lévesque, Masaki Nishimura, Dun-Sheng Yang, Howard T. J. Mount, David Westaway, and Peter H. St George-Hyslop. "Presenilin function: connections to Alzheimer's disease and signal transduction." Biochemical Society Symposia 67 (February 1, 2001): 89–100. http://dx.doi.org/10.1042/bss0670089.

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Missense mutations in presenilin 1 (PS1) and presenilin 2 (PS2) are associated with early-onset familial Alzheimer's disease which displays an accelerated deposition of amyloid plaques and neurofibrillary tangles. Presenilins are multi-spanning transmembrane proteins which localize primarily to the endoplasmic reticulum and the Golgi compartments. We have previously demonstrated that PS1 exists as a high-molecular-mass complex that is likely to contain several functional ligands. Potential binding proteins were screened by the yeast two-hybrid system using the cytoplasmically orientated PS1 loop domain which was shown to interact strongly with members of the armadillo family of proteins, including ϐ-catenin, p0071 and a novel neuron-specific plakophilin-related armadillo protein (NPRAP). Armadillo proteins can have dual functions that encompass the stabilization of cellular junctions/synapses and the mediation of signal transduction pathways. Our observations suggest that PS1 may contribute to both aspects of armadillo-related pathways involving neurite outgrowth and nuclear translocation of ϐ-catenin upon activation of the wingless (Wnt) pathway. Alzheimer's disease (AD)-related presenilin mutations exhibit a dominant gain of aberrant function resulting in the prevention of ϐ-catenin translocation following Wnt signalling. These findings indicate a functional role for PS1 in signalling and suggest that mistrafficking of selected presenilin ligands may be a potential mechanism in the genesis of AD.

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Jacob, C., J. R. Lancaster, and G. I. Giles. "Reactive sulphur species in oxidative signal transduction." Biochemical Society Transactions 32, no. 6 (October 26, 2004): 1015–17. http://dx.doi.org/10.1042/bst0321015.

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Intense interest has been generated by the discovery that reactive oxygen species can function as intracellular second messengers. Reactive oxygen species have been implicated in diverse cellular processes, including growth factor signal transduction, gene expression and apoptosis. Additionally, there is evidence for proteins that are regulated by redox environment through the reversible oxidation of their cysteine residues. However, the direct reaction of reactive oxygen species with cysteine at physiological concentrations is generally a slow process, suggesting that intermediates are required to convey efficiently the oxidative stimulus. Here, we discuss the evidence that DSOs (disulphide-S-oxides) are formed from glutathione under oxidizing conditions and specifically modulate the redox status of thiols, indicating the existence of specialized cellular oxidative pathways. DSO inactivated glyceraldehyde 3-phosphate and alcohol dehydrogenases and released zinc from metallothionein and a zinc finger domain. In contrast, equivalent concentrations of H2O2 showed minimal effect. The antioxidants ascorbate, NADH, trolox and melatonin were unable to quench DSO-induced oxidation. These findings support the paradigm of oxidative signal transduction and provide a general pathway whereby reactive oxygen species can convert thiols into disulphides.

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Scott, John D., and Tony Pawson. "Cell Signaling in Space and Time: Where Proteins Come Together and When They’re Apart." Science 326, no. 5957 (November 26, 2009): 1220–24. http://dx.doi.org/10.1126/science.1175668.

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Signal transduction can be defined as the coordinated relay of messages derived from extracellular cues to intracellular effectors. More simply put, information received on the cell surface is processed across the plasma membrane and transmitted to intracellular targets. This requires that the activators, effectors, enzymes, and substrates that respond to cellular signals come together when they need to.

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Zaidi, M., A. Patchell, H. K. Datta, and I. MacIntyre. "UNCOUPLING OF RECEPTOR-MEDIATED CELLULAR RESPONSES BY IONIC LITHIUM." Journal of Endocrinology 123, no. 2 (November 1989): R5—R7. http://dx.doi.org/10.1677/joe.0.123r005.

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ABSTRACT The propensity of ionic lithium to interfere with the coupling of receptors to guanine nucleotide binding proteins (G-proteins) has only recently been investigated using rat cortical membranes. In the present study we have used intact isolated osteoclasts to investigate lithium-induced uncoupling of the receptor-mediated actions of calcitonin. All actions of calcitonin on the osteoclast were abolished by ionic lithium. We believe that the cation prevents signal transduction by inhibiting G protein-receptor interaction, the first step in intracellular signalling.

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Stulnig, T. M., M. Berger, H. Stockinger, V. Horejsí, and W. Waldhǎusl. "Lowering cellular cholesterol inhibits signal transduction via glycosyl phosphatidyl-inositol(GPI)-anchored proteins." Immunology Letters 56 (May 1997): 64. http://dx.doi.org/10.1016/s0165-2478(97)85243-1.

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Stulnig, T. "Lowering cellular cholesterol inhibits signal transduction via glycosyl phosphatidyl-inositol(GPI)-anchored proteins." Immunology Letters 56, no. 1-3 (May 1997): 64. http://dx.doi.org/10.1016/s0165-2478(97)87081-2.

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DiMaio, Daniel, Char-Chang Lai, and Ophir Klein. "VIROCRINE TRANSFORMATION: The Intersection Between Viral Transforming Proteins and Cellular Signal Transduction Pathways." Annual Review of Microbiology 52, no. 1 (October 1998): 397–421. http://dx.doi.org/10.1146/annurev.micro.52.1.397.

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Kahler, Charlene. "Transcriptional repressors." Microbiology Australia 27, no. 3 (2006): 105. http://dx.doi.org/10.1071/ma06105.

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Prokaryotes regulate cellular functions in response to environmental cues via signal transduction pathways. In principal, there are two thematic organisations of signal transduction proteins: ? One-component proteins, in which the input and output domains are physically linked. These are commonly called activators (see article by Schubert & Shearwin) and repressors (reviewed in this article). ? Two-component systems consisting of histidine kinases and response regulators (see article by Cheung & Rood). A recent survey of 145 prokaryotic genomes has revealed the predominance of one-component systems in this domain of life and has provided the first indication of the diversity inherent in these signal transduction pathways.

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Ibitayo, Adenike I., Jeanette Sladick, Sony Tuteja, Otto Louis-Jacques, Hirotaka Yamada, Guy Groblewski, Michael Welsh, and Khalil N. Bitar. "HSP27 in signal transduction and association with contractile proteins in smooth muscle cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 277, no. 2 (August 1, 1999): G445—G454. http://dx.doi.org/10.1152/ajpgi.1999.277.2.g445.

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Sustained smooth muscle contraction is mediated by protein kinase C (PKC) through a signal transduction cascade leading to contraction. Heat-shock protein 27 (HSP27) appears to be the link between these two major events, i.e., signal transduction and sustained smooth muscle contraction. We have investigated the involvement of HSP27 in signal transduction and HSP27 association with contractile proteins (e.g., actin, myosin, tropomyosin, and caldesmon) resulting in sustained smooth muscle contraction. We have carried out confocal microscopy to investigate the cellular reorganization and colocalization of proteins and immunoprecipitation of HSP27 with actin, myosin, tropomyosin, and caldesmon as detected by sequential immunoblotting. Our results indicate that 1) translocation of Raf-1 to the membrane when stimulated with ceramide is inhibited by vasoactive intestinal peptide (VIP), a relaxant neuropeptide; 2) PKC-α and mitogen-activated protein kinase translocate and colocalize on the membrane in response to ceramide, and PKC-α translocation is inhibited by VIP; 3) HSP27 colocalizes with actin when contraction occurs; and 4) HSP27 immunoprecipitates with actin and with the contractile proteins myosin, tropomyosin, and caldesmon. We propose a model in which HSP27 is involved in sustained smooth muscle contraction and modulates the interaction of actin, myosin, tropomyosin, and caldesmon.

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Liu, S., D. A. Calderwood, and M. H. Ginsberg. "Integrin cytoplasmic domain-binding proteins." Journal of Cell Science 113, no. 20 (October 15, 2000): 3563–71. http://dx.doi.org/10.1242/jcs.113.20.3563.

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Integrins are a large family of cell surface receptors that mediate cell adhesion and influence migration, signal transduction, and gene expression. The cytoplasmic domains of integrins play a pivotal role in these integrin-mediated cellular functions. Through interaction with the cytoskeleton, signaling molecules, and other cellular proteins, integrin cytoplasmic domains transduce signals from both the outside and inside of the cell and regulate integrin-mediated biological functions. Identification and functional analyses of integrin cytoplasmic domain-binding proteins have been pursued intensively. In recent years, more cellular proteins have been reported to directly interact with integrin cytoplasmic domains and some of these interactions may play important roles in integrin-mediated biological responses. Integrin (β) chains, for example, interact with actin-binding proteins (e.g. talin and filamin), which form mechanical links to the cytoskeleton. These and other proteins (e.g. FAK, ILK and novel proteins such as TAP20) might also link integrins to signaling mechanisms and, in some cases (e.g. JAB1) mediate integrin-dependent gene regulation.

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Langland, Jeffrey O., John C. Kash, Victoria Carter, Matthew J. Thomas, Michael G. Katze, and Bertram L. Jacobs. "Suppression of Proinflammatory Signal Transduction and Gene Expression by the DualNucleic Acid Binding Domains of the Vaccinia Virus E3L Proteins." Journal of Virology 80, no. 20 (October 15, 2006): 10083–95. http://dx.doi.org/10.1128/jvi.00607-06.

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ABSTRACT Cells have evolved elaborate mechanisms to counteract the onslaught of viral infections. To activate these defenses, the viral threat must be recognized. Danger signals, or pathogen-associated molecular patterns, that are induced by pathogens include double-stranded RNA (dsRNA), viral single-stranded RNA, glycolipids, and CpG DNA. Understanding the signal transduction pathways activated and host gene expression induced by these danger signals is vital to understanding virus-host interactions. The vaccinia virus E3L protein is involved in blocking the host antiviral response and increasing pathogenesis, functions that map to separate C-terminal dsRNA- and N-terminal Z-DNA-binding domains. Viruses containing mutations in these domains allow modeling of the role of dsRNA and Z-form nucleic acid in the host response to virus infection. Deletions in the Z-DNA- or dsRNA-binding domains led to activation of signal transduction cascades and up-regulation of host gene expression, with many genes involved in the inflammatory response. These data suggest that poxviruses actively inhibit cellular recognition of viral danger signals and the subsequent cellular response to the viral threat.

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Palazzo, Luca, and Ivan Ahel. "PARPs in genome stability and signal transduction: implications for cancer therapy." Biochemical Society Transactions 46, no. 6 (November 12, 2018): 1681–95. http://dx.doi.org/10.1042/bst20180418.

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The poly(ADP-ribose) polymerase (PARP) superfamily of enzymes catalyses the ADP-ribosylation (ADPr) of target proteins by using nicotinamide adenine dinucleotide (NAD+) as a donor. ADPr reactions occur either in the form of attachment of a single ADP-ribose nucleotide unit on target proteins or in the form of ADP-ribose chains, with the latter called poly(ADP-ribosyl)ation. PARPs regulate many cellular processes, including the maintenance of genome stability and signal transduction. In this review, we focus on the PARP family members that possess the ability to modify proteins by poly(ADP-ribosyl)ation, namely PARP1, PARP2, Tankyrase-1, and Tankyrase-2. Here, we detail the cellular functions of PARP1 and PARP2 in the regulation of DNA damage response and describe the function of Tankyrases in Wnt-mediated signal transduction. Furthermore, we discuss how the understanding of these pathways has provided some major breakthroughs in the treatment of human cancer.

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Benekli, Mustafa, Maria R. Baer, Heinz Baumann, and Meir Wetzler. "Signal transducer and activator of transcription proteins in leukemias." Blood 101, no. 8 (April 15, 2003): 2940–54. http://dx.doi.org/10.1182/blood-2002-04-1204.

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Abstract Signal transducer and activator of transcription (STAT) proteins are a 7-member family of cytoplasmic transcription factors that contribute to signal transduction by cytokines, hormones, and growth factors. STAT proteins control fundamental cellular processes, including survival, proliferation, and differentiation. Given the critical roles of STAT proteins, it was hypothesized that inappropriate or aberrant activation of STATs might contribute to cellular transformation and, in particular, leukemogenesis. Constitutive activation of mutated STAT3 has in fact been demonstrated to result in transformation. STAT activation has been extensively studied in leukemias, and mechanisms of STAT activation and the potential role of STAT signaling in leukemogenesis are the focus of this review. A better understanding of mechanisms of dysregulation of STAT signaling pathways may serve as a basis for designing novel therapeutic strategies that target these pathways in leukemia cells.

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Vanderbeld, Barbara, and Gregory M. Kelly. "New thoughts on the role of the βγ subunit in G protein signal transduction." Biochemistry and Cell Biology 78, no. 5 (October 1, 2000): 537–50. http://dx.doi.org/10.1139/o00-075.

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Heterotrimeric G proteins are involved in numerous biological processes, where they mediate signal transduction from agonist-bound G-protein-coupled receptors to a variety of intracellular effector molecules and ion channels. G proteins consist of two signaling moieties: a GTP-bound α subunit and a βγ heterodimer. The βγ dimer, recently credited as a significant modulator of G-protein-mediated cellular responses, is postulated to be a major determinant of signaling fidelity between G-protein-coupled receptors and downstream effectors. In this review we have focused on the role of βγ signaling and have included examples to demonstrate the heterogeneity in the heterodimer composition and its implications in signaling fidelity. We also present an overview of some of the effectors regulated by βγ and draw attention to the fact that, although G proteins and their associated receptors play an instrumental role in development, there is rather limited information on βγ signaling in embryogenesis.Key words: G protein, βγ subunit, G-protein-coupled receptor, signal transduction, adenylyl cyclase.

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Prado, M. A., B. Evans-Bain, and I. M. Dickerson. "Receptor component protein (RCP): a member of a multi-protein complex required for G-protein-coupled signal transduction." Biochemical Society Transactions 30, no. 4 (August 1, 2002): 460–64. http://dx.doi.org/10.1042/bst0300460.

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The calcitonin-gene-related peptide (CGRP) receptor component protein (RCP) is a 148-amino-acid intracellular protein that is required for G-protein-coupled signal transduction at receptors for the neuropeptide CGRP. RCP works in conjunction with two other proteins to constitute a functional CGRP receptor: calcitonin-receptor-like receptor (CRLR) and receptor-activity-modifying protein 1 (RAMP1).CRLR has the stereotypical seven-transmembrane topology of a G-protein-coupled receptor; it requires RAMP1 for trafficking to the cell surface and for ligand specificity, and requires RCP for coupling to the cellular signal transduction pathway. We have made cell lines that expressed an antisense construct of RCP and determined that CGRP-mediated signal transduction was reduced, while CGRP binding was unaffected. Furthermore, signalling at two other endogenous G-protein-coupled receptors was unaffected, suggesting that RCP was specific for a limited subset of receptors.

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Wesselborg, Sebastian, and Björn Stork. "Autophagy signal transduction by ATG proteins: from hierarchies to networks." Cellular and Molecular Life Sciences 72, no. 24 (September 21, 2015): 4721–57. http://dx.doi.org/10.1007/s00018-015-2034-8.

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Abouzari, Abouzar, and Barat Ali Fakheri. "Reactive oxygen species: Generation, Oxidative Damage, and Signal Transduction." International Journal of Life Sciences 9, no. 5 (June 14, 2015): 3–17. http://dx.doi.org/10.3126/ijls.v9i5.12699.

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Reactive oxygen species (ROS) are a by-product of normal cell metabolism in plants; however, the balance between production and elimination is disturbed under stress conditions. Several reactive oxygen species are continuously produced in plants as secondary products of aerobic metabolism. Depending on the source of the ROS species, some of them are highly toxic. Plants cellular rapidly use various enzymatic and nonenzymatic mechanisms For detoxify ROS species. Enhanced level of ROS and absence of detoxify systems, can cause damage to biomolecules such as lipids, proteins and DNA and eventually cause to cell death. Despite their destructive activity, they are second messengers in a variety of cellular processes, including conferment of tolerance to various environmental stresses. This review paper describes the Variety of Reactive oxygen species, sources and roles of ROS in plants.DOI: http://dx.doi.org/10.3126/ijls.v9i5.12699

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Mazzoni, I. E., H. C. Ledebur, Jr., E. Paramithiotis, and N. Cashman. "Lymphoid signal transduction mechanisms linked to cellular prion protein." Biochemistry and Cell Biology 83, no. 5 (October 1, 2005): 644–53. http://dx.doi.org/10.1139/o05-058.

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The normal cellular isoform of the prion protein (PrPC) is a glycosylphosphatidylinositol-anchored cell surface protein that is expressed widely, including in lymphoid cells. We compared lectin-induced mitogenesis and selected cell signaling pathways in splenocytes from wild-type BALB/c mice and Zrch Prnp0/0(PrP0/0) mice bred on a BALB/c background for more than 10 generations.3H-thymidine incorporation induced by concanavalin A (Con A) or phytohemagglutinin (PHA) was significantly reduced in PrP0/0splenocytes, most prominently early in activation (24 and 48 h). Con A activation in PrP0/0splenocytes was associated with differences in the phosphorylation (P) patterns of protein kinase C (PKC α/β, but not δ) and the PKC downstream effectors p44/42MAPK (mitogen-activated protein kinase). P-PKC and P-MAPK profiles were similar in wild-type and PrP0/0splenocytes following PMA treatment, indicating that the ability of these 2 enzymes to be phosphorylated is not impaired in the absence of PrPC. Con A-induced calcium fluxes, monitored by indo-1 fluorescence, were equivalent in PrP0/0and PrP+/+splenocytes, suggesting that calcium-dependent mechanisms are not directly implicated in the differential phosphorylation patterns or mitotic responses. Our data indicate that PrP0/0splenocytes display defects in upstream or downstream mechanism(s) that modulate PKCα/β phosphorylation, which in turn affects its capacity to regulate splenocyte mitosis, consistent with a role for PrPCin immune function.Key words: PKC, MAPK, mitosis, bovine spongiform encephalopathy, Creutzfeldt-Jacob disease.

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Pahl, Heike L. "Signal Transduction From the Endoplasmic Reticulum to the Cell Nucleus." Physiological Reviews 79, no. 3 (July 1, 1999): 683–701. http://dx.doi.org/10.1152/physrev.1999.79.3.683.

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The endoplasmic reticulum (ER) serves several important functions. Cholesterol, an essential component of cellular membranes, is synthesized on the ER surface. Inside the organelle, proteins destined for secretion or transport to the cell surface are folded and become glycosylated. Because these processes are essential for cell viability, a disturbance in ER function presents significant stress to the cell. In response to ER stress, three distinct signal transduction pathways can be activated. Two of these, the unfolded protein response and the ER-overload response, respond to disturbances in protein processing. The third, the sterol regulatory cascade, is activated by depletion of cholesterol. This review summarizes the recent advances in our understanding of these ER-nuclear signal transduction pathways. In addition, it points to novel regulatory mechanisms discovered in these pathways, which may be widely used in other systems.

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Resh, Marilyn D. "Regulation of cellular signalling by fatty acid acylation and prenylation of signal transduction proteins." Cellular Signalling 8, no. 6 (September 1996): 403–12. http://dx.doi.org/10.1016/s0898-6568(96)00088-5.

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Rovedo, Mark, and Richard Longnecker. "Epstein-Barr Virus Latent Membrane Protein 2B (LMP2B) Modulates LMP2A Activity." Journal of Virology 81, no. 1 (October 11, 2006): 84–94. http://dx.doi.org/10.1128/jvi.01302-06.

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ABSTRACT Latent membrane protein 2A (LMP2A) and LMP2B are viral proteins expressed during Epstein-Barr virus (EBV) latency in EBV-infected B cells both in cell culture and in vivo. LMP2A has important roles in modulating B-cell receptor (BCR) signal transduction by associating with the cellular tyrosine kinases Lyn and Syk via specific phosphotyrosine motifs found within the LMP2A N-terminal tail domain. LMP2A has been shown to alter normal BCR signal transduction in B cells by reducing levels of Lyn and by blocking tyrosine phosphorylation and calcium mobilization following BCR cross-linking. Although little is currently known about the function of LMP2B in B cells, the similarity in structure between LMP2A and LMP2B suggests that they may localize to the same cellular compartments. To investigate the function of LMP2B, B-cell lines expressing LMP2A, LMP2B, LMP2A/LMP2B, and the relevant vector controls were analyzed. As was previously shown, cells expressing LMP2A had a dramatic block in normal BCR signal transduction as measured by calcium mobilization and tyrosine phosphorylation. There was no effect on BCR signal transduction in cells expressing LMP2B. Interestingly, when LMP2B was expressed in conjunction with LMP2A, there was a restoration of normal BCR signal transduction upon BCR cross-linking. The expression of LMP2B did not alter the cellular localization of LMP2A but did bind to and prevent the phosphorylation of LMP2A. A restoration of Lyn levels, but not a change in LMP2A levels, was also observed in cells coexpressing LMP2B with LMP2A. From these results, we conclude that LMP2B modulates LMP2A activity.

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Jones, Eleanor Livingston, Maria C. Demaria, and Mark D. Wright. "Tetraspanins in cellular immunity." Biochemical Society Transactions 39, no. 2 (March 22, 2011): 506–11. http://dx.doi.org/10.1042/bst0390506.

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Tetraspanins are a superfamily of integral membrane proteins involved in the organization of microdomains that consist of both cell membrane proteins and cytoplasmic signalling molecules. These microdomains are important in regulating molecular recognition at the cell surface and subsequent signal transduction processes central to the generation of an efficient immune response. Tetraspanins, both immune-cell-specific, such as CD37, and ubiquitously expressed, such as CD81, have been shown to be imp-ortant in both innate and adaptive cellular immunity. This is via their molecular interaction with important immune cell-surface molecules such as antigen-presenting MHC proteins, T-cell co-receptors CD4 and CD8, as well as cytoplasmic molecules such as Lck and PKC (protein kinase C). Moreover, the generation of tetraspanin-deficient mice has enabled the study of these proteins in immunity. A variety of tetraspanins have a role in the regulation of pattern recognition, antigen presentation and T-cell proliferation. Recent studies have also begun to elucidate roles for tetraspanins in macrophages, NK cells (natural killer cells) and granulocytes.

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ZHU, LING, TIMON CHENG-YI LIU, MIN WU, JIAN-QIN YUAN, and TONG-SHENG CHEN. "EXTRAOCULAR CELLULAR PHOTOTRANSDUCTION." Journal of Innovative Optical Health Sciences 02, no. 01 (January 2009): 93–100. http://dx.doi.org/10.1142/s1793545809000358.

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Photobiomodulation (PBM) is a modulation of monochromatic light or laser irradiation (LI) on biosystems. It is reviewed from the viewpoint of extraocular phototransduction in this paper. It was found that LI can induce extraocular phototransduction, and there may be an exact correspondence relationship of LI at different wavelengths and in different dose zones, and cellular signal transduction pathways. The signal transduction pathways can be classified into two types so that the Gs protein-mediated pathways belong to pathway 1, and the other pathways such as protein kinase Cs -mediated pathways and mitogen-activated protein kinase-mediated pathways belong to pathway 2. Almost all the present pathways found to mediate PBM belong to pathway 2, but there should be a pathway 1-mediated PBM. The previous studies were rather preliminary, and therefore further work should be done.

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Scheler, Gabriele. "Self-organization of signal transduction." F1000Research 2 (April 23, 2013): 116. http://dx.doi.org/10.12688/f1000research.2-116.v1.

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We propose a model of parameter learning for signal transduction, where the objective function is defined by signal transmission efficiency. We apply this to learn kinetic rates as a form of evolutionary learning, and look for parameters which satisfy the objective. This is a novel approach compared to the usual technique of adjusting parameters only on the basis of experimental data. The resulting model is self-organizing, i.e. perturbations in protein concentrations or changes in extracellular signaling will automatically lead to adaptation. We systematically perturb protein concentrations and observe the response of the system. We find compensatory or co-regulation of protein expression levels. In a novel experiment, we alter the distribution of extracellular signaling, and observe adaptation based on optimizing signal transmission. We also discuss the relationship between signaling with and without transients. Signaling by transients may involve maximization of signal transmission efficiency for the peak response, but a minimization in steady-state responses. With an appropriate objective function, this can also be achieved by concentration adjustment. Self-organizing systems may be predictive of unwanted drug interference effects, since they aim to mimic complex cellular adaptation in a unified way.

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Bihn, Elizabeth A., and Robert J. Ferl. "Subcellular Localization of 14-3-3 Regulatory Proteins in Arabidopsis thaliana." HortScience 31, no. 4 (August 1996): 614e—614. http://dx.doi.org/10.21273/hortsci.31.4.614e.

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The 14-3-3 proteins were originally characterized in mammalian brains and were thought to be specifically involved in neurotransmitter production. Subsequent research has revealed that this family of proteins is ubiquitous in eucaryotic cells and is involved in a wide range of regulatory and signal transduction pathways. For instance, some 14-3-3 proteins have been associated with the signal transduction in response to fungal pathogen attack and to other environmental factors that affect transcription. In Arabidopsis, 10 isoforms of 14-3-3 have been isolated, raising the possibility that diversity of function may be governed by cellular and subcellular specificities of expression and localization. We have investigated the localization of certain 14-3-3 isoforms through transgenic expression of epitope-tagged 14-3-3s.

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Silva, Marta A., and Carlos A. Salgueiro. "Multistep Signaling in Nature: A Close-Up of Geobacter Chemotaxis Sensing." International Journal of Molecular Sciences 22, no. 16 (August 21, 2021): 9034. http://dx.doi.org/10.3390/ijms22169034.

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Environmental changes trigger the continuous adaptation of bacteria to ensure their survival. This is possible through a variety of signal transduction pathways involving chemoreceptors known as methyl-accepting chemotaxis proteins (MCP) that allow the microorganisms to redirect their mobility towards favorable environments. MCP are two-component regulatory (or signal transduction) systems (TCS) formed by a sensor and a response regulator domain. These domains synchronize transient protein phosphorylation and dephosphorylation events to convert the stimuli into an appropriate cellular response. In this review, the variability of TCS domains and the most common signaling mechanisms are highlighted. This is followed by the description of the overall cellular topology, classification and mechanisms of MCP. Finally, the structural and functional properties of a new family of MCP found in Geobacter sulfurreducens are revisited. This bacterium has a diverse repertoire of chemosensory systems, which represents a striking example of a survival mechanism in challenging environments. Two G. sulfurreducens MCP—GSU0582 and GSU0935—are members of a new family of chemotaxis sensor proteins containing a periplasmic PAS-like sensor domain with a c-type heme. Interestingly, the cellular location of this domain opens new routes to the understanding of the redox potential sensing signaling transduction pathways.

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McGinnis, James F., Brian Matsumoto, James P. Whelan, and Wei Cao. "Cytoskeleton participation in subcellular trafficking of signal transduction proteins in rod photoreceptor cells." Journal of Neuroscience Research 67, no. 3 (January 23, 2002): 290–97. http://dx.doi.org/10.1002/jnr.10120.

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Hadwiger, Jeffrey A., and Hoai-Nghia Nguyen. "MAPKs in development: insights from Dictyostelium signaling pathways." BioMolecular Concepts 2, no. 1-2 (April 1, 2011): 39–46. http://dx.doi.org/10.1515/bmc.2011.004.

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AbstractMitogen activated protein kinases (MAPKs) play important roles in the development of eukaryotic organisms through the regulation of signal transduction pathways stimulated by external signals. MAPK signaling pathways have been associated with the regulation of cell growth, differentiation, and chemotaxis, indicating that MAPKs contribute to a diverse set of developmental processes. In most eukaryotes, the diversity of external signals is likely to far exceed the diversity of MAPKs, suggesting that multiple signaling pathways might share MAPKs. Do different signaling pathways converge before MAPK function or can MAPKs maintain signaling specificity through interactions with specific proteins? The genetic and biochemical analysis of MAPK pathways in simple eukaryotes such as Dictyostelium offers opportunities to investigate functional specificity of MAPKs in G-protein-mediated signal transduction pathways. This review considers the regulation and specificity of MAPK function in pathways that control Dictyostelium growth and development.

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Journal articles on the topic 'Proteins Cellular signal transduction'

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