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Journal articles on the topic 'Cytoskeletal proteins'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Letek, Michal, María Fiuza, Almudena F. Villadangos, Luís M. Mateos, and José A. Gil. "Cytoskeletal Proteins ofActinobacteria." International Journal of Cell Biology 2012 (2012): 1–10. http://dx.doi.org/10.1155/2012/905832.

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Although bacteria are considered the simplest life forms, we are now slowly unraveling their cellular complexity. Surprisingly, not only do bacterial cells have a cytoskeleton but also the building blocks are not very different from the cytoskeleton that our own cells use to grow and divide. Nonetheless, despite important advances in our understanding of the basic physiology of certain bacterial models, little is known aboutActinobacteria, an ancient group of Eubacteria. Here we review current knowledge on the cytoskeletal elements required for bacterial cell growth and cell division, focusing

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2

Albrecht, D. L., and R. J. Noelle. "Membrane Ig-cytoskeletal interactions. I. Flow cytofluorometric and biochemical analysis of membrane IgM-cytoskeletal interactions." Journal of Immunology 141, no. 11 (1988): 3915–22. http://dx.doi.org/10.4049/jimmunol.141.11.3915.

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Abstract Membrane IgM (mIgM) and mIgD are the receptors for Ag on the surface of B lymphocytes, mIg is soluble in detergent; however, when mIg is cross-linked with anti-Ig, the mIg becomes associated with the cytoskeletal matrix and is rendered detergent-insoluble. By a novel flow cytofluorometric assay and by biochemical analysis, it has been shown that anti-isotype-specific antibodies induce mIgM and mIgD to associate with the cytoskeleton of B lymphocytes in an isotype-specific fashion. The detergent solubility of other prominent B lymphocyte surface proteins, such as class I and class II M

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3

Miura, Tetsuji. "Cytoskeletal Proteins." Circulation Journal 74, no. 11 (2010): 2295–96. http://dx.doi.org/10.1253/circj.cj-10-0935.

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4

Dvořáková, Kateřina, Harry D. M. Moore, Nataša Šebková, and Jiří Paleček. "Cytoskeleton localization in the sperm head prior to fertilization." Reproduction 130, no. 1 (2005): 61–69. http://dx.doi.org/10.1530/rep.1.00549.

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Three major cytoskeletal proteins, actin, tubulin and spectrin, are present in the head of mammalian spermatozoa. Although cytoskeletal proteins are implicated in the regulation of capacitation and the acrosome reaction (AR), their exact role remains poorly understood. The aim of this study was to compare the distribution of the sperm head cytoskeleton before and after the AR in spermatozoa representing a range of acrosome size and shape. Spermatozoa from the human and three rodents (rat, hamster and grey squirrel) were fixed before and after the AR in appropriate mediumin vitro. Indirect immu

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Paradžik, Tina, Iva I. Podgorski, Tanja Vojvoda Zeljko, and Mladen Paradžik. "Ancient Origins of Cytoskeletal Crosstalk: Spectraplakin-like Proteins Precede the Emergence of Cortical Microtubule Stabilization Complexes as Crosslinkers." International Journal of Molecular Sciences 23, no. 10 (2022): 5594. http://dx.doi.org/10.3390/ijms23105594.

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Adhesion between cells and the extracellular matrix (ECM) is one of the prerequisites for multicellularity, motility, and tissue specialization. Focal adhesions (FAs) are defined as protein complexes that mediate signals from the ECM to major components of the cytoskeleton (microtubules, actin, and intermediate filaments), and their mutual communication determines a variety of cellular processes. In this study, human cytoskeletal crosstalk proteins were identified by comparing datasets with experimentally determined cytoskeletal proteins. The spectraplakin dystonin was the only protein found i

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Chifflet, Silvia, and Julio A. Hernández. "The Plasma Membrane Potential and the Organization of the Actin Cytoskeleton of Epithelial Cells." International Journal of Cell Biology 2012 (2012): 1–13. http://dx.doi.org/10.1155/2012/121424.

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The establishment and maintenance of the polarized epithelial phenotype require a characteristic organization of the cytoskeletal components. There are many cellular effectors involved in the regulation of the cytoskeleton of epithelial cells. Recently, modifications in the plasma membrane potential (PMP) have been suggested to participate in the modulation of the cytoskeletal organization of epithelia. Here, we review evidence showing that changes in the PMP of diverse epithelial cells promote characteristic modifications in the cytoskeletal organization, with a focus on the actin cytoskeleto

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7

Fox, Joan. "Cytoskeletal Proteins and Platelet Signaling." Thrombosis and Haemostasis 86, no. 07 (2001): 198–213. http://dx.doi.org/10.1055/s-0037-1616218.

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SummaryThe actin filament network fills the cytoplasm of unstimulated platelets and connects with a submembranous latticework of short cross-linked actin filaments, known as the membrane skeleton. One function of the cytoskeleton is to direct the contours of the membrane in the unstimulated platelet and the rapid changes in shape in the activated platelet. Activation-induced changes result from events such as phosphorylation or calpain-induced cleavage of cytoskeletal proteins. The specific reorganizations depend upon the combination of signals to which platelets are exposed. A second function

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Chinthalapudi, Krishna, Erumbi Rangarajan, Dipak Patil, and Tina Izard. "Lipid-directed cytoskeletal protein oligomerization at sites of cell adhesion." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C1833. http://dx.doi.org/10.1107/s2053273314081674.

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Vertebrate cell growth, division, migration, morphogenesis, and development, rely on the dynamic interactions of cells with components the extracellular matrix (ECM) via cell surface complexes. These focal adhesions (FAs) are comprised of integrin receptors, associated signaling molecules, and talin, which is required for "inside-out" signaling that stabilizes contacts of integrin receptors with the ECM by linking FAs to the actin cytoskeleton by binding to vinculin. The highly dynamic interactions with the actin cytoskeleton are also essential for the formation of membrane protrusions (lamell

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9

Ong, Mei Shan, Shuo Deng, Clarissa Esmeralda Halim, et al. "Cytoskeletal Proteins in Cancer and Intracellular Stress: A Therapeutic Perspective." Cancers 12, no. 1 (2020): 238. http://dx.doi.org/10.3390/cancers12010238.

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Cytoskeletal proteins, which consist of different sub-families of proteins including microtubules, actin and intermediate filaments, are essential for survival and cellular processes in both normal as well as cancer cells. However, in cancer cells, these mechanisms can be altered to promote tumour development and progression, whereby the functions of cytoskeletal proteins are co-opted to facilitate increased migrative and invasive capabilities, proliferation, as well as resistance to cellular and environmental stresses. Herein, we discuss the cytoskeletal responses to important intracellular s

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10

Perry, G., D. A. Zelasko, L. M. Sayre, and M. A. Smith. "Oxidative Damage to Axonal Cytoskeletal Proteins." Microscopy and Microanalysis 3, S2 (1997): 43–44. http://dx.doi.org/10.1017/s1431927600007108.

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Proteins of the axonal cytoskeleton, particularly neurofilament and microtubule-associated protein τ, should be particularly sensitive to the effects of oxidative modification due to their high content of lysine, an amino acid that is particularly susceptible to direct oxidization as well as adduction by carbonyls produced from lipid and sugar oxidation. To understand the susceptibility of the cytoskeleton to oxidative modification and whether such modification is related to the physiological function of the cytoskeleton, we undertook a cytological analysis of motor neurons isolated from mouse

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Hutchings, Nathan R., John E. Donelson, and Kent L. Hill. "Trypanin is a cytoskeletal linker protein and is required for cell motility in African trypanosomes." Journal of Cell Biology 156, no. 5 (2002): 867–77. http://dx.doi.org/10.1083/jcb.200201036.

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The cytoskeleton of eukaryotic cells is comprised of a complex network of distinct but interconnected filament systems that function in cell division, cell motility, and subcellular trafficking of proteins and organelles. A gap in our understanding of this dynamic network is the identification of proteins that connect subsets of cytoskeletal structures. We previously discovered a family of cytoskeleton-associated proteins that includes GAS11, a candidate human tumor suppressor upregulated in growth-arrested cells, and trypanin, a component of the flagellar cytoskeleton of African trypanosomes.

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12

Scott, J. D. "A-kinase-anchoring proteins and cytoskeletal signalling events." Biochemical Society Transactions 31, no. 1 (2003): 87–89. http://dx.doi.org/10.1042/bst0310087.

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Targeting of protein kinases and phosphatases to the cytoskeleton enhances the regulation of many signalling events. Cytoskeletal signalling complexes facilitate this process by optimizing the relay of messages from membrane receptors to specific sites on the actin cytoskeleton. These signals influence fundamental cell properties such as shape, movement and division. Targeting of the cAMP-dependent kinase (protein kinase A) and other enzymes to this compartment is achieved through interaction with A-kinase-anchoring proteins (AKAPs). The present paper discusses recent progress on dissecting th

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Muñoz-Lasso, Diana C., Carlos Romá-Mateo, Federico V. Pallardó, and Pilar Gonzalez-Cabo. "Much More Than a Scaffold: Cytoskeletal Proteins in Neurological Disorders." Cells 9, no. 2 (2020): 358. http://dx.doi.org/10.3390/cells9020358.

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Recent observations related to the structure of the cytoskeleton in neurons and novel cytoskeletal abnormalities involved in the pathophysiology of some neurological diseases are changing our view on the function of the cytoskeletal proteins in the nervous system. These efforts allow a better understanding of the molecular mechanisms underlying neurological diseases and allow us to see beyond our current knowledge for the development of new treatments. The neuronal cytoskeleton can be described as an organelle formed by the three-dimensional lattice of the three main families of filaments: act

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14

Zencheck, Wendy D., Hui Xiao, and Louis M. Weiss. "Lysine post-translational modifications and the cytoskeleton." Essays in Biochemistry 52 (May 25, 2012): 135–45. http://dx.doi.org/10.1042/bse0520135.

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PTMs (post-translational modifications) of lysine residues have proven to be major regulators of gene expression, protein–protein interactions, and protein processing and degradation. This is of particular importance in regulating the cytoskeleton, an enormously complex system of proteins responsible for cell motility, intracellular trafficking, and maintenance of cell form and structure. The cytoskeleton is present in all cells, including eukaryotes and prokaryotes, and comprises structures such as flagella, cilia and lamellipodia which play critical roles in intracellular transport and cellu

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Haglund, Cat M., and Matthew D. Welch. "Pathogens and polymers: Microbe–host interactions illuminate the cytoskeleton." Journal of Cell Biology 195, no. 1 (2011): 7–17. http://dx.doi.org/10.1083/jcb.201103148.

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Intracellular pathogens subvert the host cell cytoskeleton to promote their own survival, replication, and dissemination. Study of these microbes has led to many discoveries about host cell biology, including the identification of cytoskeletal proteins, regulatory pathways, and mechanisms of cytoskeletal function. Actin is a common target of bacterial pathogens, but recent work also highlights the use of microtubules, cytoskeletal motors, intermediate filaments, and septins. The study of pathogen interactions with the cytoskeleton has illuminated key cellular processes such as phagocytosis, ma

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Csortos, Csilla, Irina Kolosova, and Alexander D. Verin. "Regulation of vascular endothelial cell barrier function and cytoskeleton structure by protein phosphatases of the PPP family." American Journal of Physiology-Lung Cellular and Molecular Physiology 293, no. 4 (2007): L843—L854. http://dx.doi.org/10.1152/ajplung.00120.2007.

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Reversible phosphorylation of cytoskeletal and cytoskeleton-associated proteins is a significant element of endothelial barrier function regulation. Therefore, understanding the mechanisms of phosphorylation/dephosphorylation of endothelial cell cytoskeletal proteins is vital to the treatment of severe lung disorders such as high permeability pulmonary edema. In vivo, there is a controlled balance between the activities of protein kinases and phosphatases. Due to various external or internal signals, this balance may be shifted. The actual balances at a given time alter the phosphorylation lev

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Kumeta, Masahiro, Shige H. Yoshimura, James Hejna, and Kunio Takeyasu. "Nucleocytoplasmic Shuttling of Cytoskeletal Proteins: Molecular Mechanism and Biological Significance." International Journal of Cell Biology 2012 (2012): 1–12. http://dx.doi.org/10.1155/2012/494902.

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Various nuclear functional complexes contain cytoskeletal proteins as regulatory subunits; for example, nuclear actin participates in transcriptional complexes, and actin-related proteins are integral to chromatin remodeling complexes. Nuclear complexes such as these are involved in both basal and adaptive nuclear functions. In addition to nuclear import via classical nuclear transport pathways or passive diffusion, some large cytoskeletal proteins spontaneously migrate into the nucleus in a karyopherin-independent manner. The balance of nucleocytoplasmic distribution of such proteins can be a

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18

Jackson, Wesley M., Michael J. Jaasma, Raymond Y. Tang, and Tony M. Keaveny. "Mechanical loading by fluid shear is sufficient to alter the cytoskeletal composition of osteoblastic cells." American Journal of Physiology-Cell Physiology 295, no. 4 (2008): C1007—C1015. http://dx.doi.org/10.1152/ajpcell.00509.2007.

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Many structural modifications have been observed as a part of the cellular response to mechanical loading in a variety of cell types. Although changes in morphology and cytoskeletal rearrangement have been widely reported, few studies have investigated the change in cytoskeletal composition. Measuring how the amounts of specific structural proteins in the cytoskeleton change in response to mechanical loading will help to elucidate cellular mechanisms of functional adaptation to the applied forces. Therefore, the overall hypothesis of this study was that osteoblasts would respond to fluid shear

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Mackay, A. M., D. M. Eckley, C. Chue, and W. C. Earnshaw. "Molecular analysis of the INCENPs (inner centromere proteins): separate domains are required for association with microtubules during interphase and with the central spindle during anaphase." Journal of Cell Biology 123, no. 2 (1993): 373–85. http://dx.doi.org/10.1083/jcb.123.2.373.

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It has recently been proposed that mitotic chromosomes transport certain cytoskeletal proteins to the metaphase plate so that these proteins are able to subsequently participate in the assembly of the anaphase spindle and the cleavage furrow. To understand how such proteins accomplish their dual chromosomal: cytoskeletal role, we have begun a molecular and functional analysis of the inner centromere proteins (INCENPs), founder members of the class of "chromosome passenger proteins". cDNA clones encoding the open reading frames of the two chicken INCENPs were recovered. The predicted proteins,

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20

Stolz, D. B., G. Bannish, and B. S. Jacobson. "The role of the cytoskeleton and intercellular junctions in the transcellular membrane protein polarity of bovine aortic endothelial cells in vitro." Journal of Cell Science 103, no. 1 (1992): 53–68. http://dx.doi.org/10.1242/jcs.103.1.53.

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This project examines the transcellular membrane protein polarity of bovine aortic endothelial cell (BAEC) monolayers in vitro with respect to the roles that intercellular junctions (as defined by comparing confluent and subconfluent monolayers) and the submembranous cytoskeleton play in controlling this phenomenon. Plasma membrane (PM) proteins obtained from apical (AP) and basolateral (BL) PM domains of confluent BAEC monolayers were isolated using the cationic colloidal silica technique and resolved by two-dimensional gel electrophoresis (2-D PAGE). To facilitate the identification of domai

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21

Li, Yuqiang, Dan Wang, Heming Ge, Cenap Güngör, Xuejun Gong, and Yongheng Chen. "Cytoskeletal and Cytoskeleton-Associated Proteins: Key Regulators of Cancer Stem Cell Properties." Pharmaceuticals 15, no. 11 (2022): 1369. http://dx.doi.org/10.3390/ph15111369.

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Cancer stem cells (CSCs) are a subpopulation of cancer cells possessing stemness characteristics that are closely associated with tumor proliferation, recurrence and resistance to therapy. Recent studies have shown that different cytoskeletal components and remodeling processes have a profound impact on the behavior of CSCs. In this review, we outline the different cytoskeletal components regulating the properties of CSCs and discuss current and ongoing therapeutic strategies targeting the cytoskeleton. Given the many challenges currently faced in targeted cancer therapy, a deeper comprehensio

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Kingston, DD. "Cytoskeletal and Extracellular Proteins." Biochemical Education 17, no. 4 (1989): 222. http://dx.doi.org/10.1016/0307-4412(89)90173-8.

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23

Riederer, B. M., R. Porchet, R. A. Marugg, and L. I. Binder. "Solubility of cytoskeletal proteins in immunohistochemistry and the influence of fixation." Journal of Histochemistry & Cytochemistry 41, no. 4 (1993): 609–16. http://dx.doi.org/10.1177/41.4.8450200.

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For accurate and quantitative immunohistochemical localization of antigens it is crucial to know the solubility of tissue proteins and their degree of loss during processing. In this study we focused on the solubility of several cytoskeletal proteins in cat brain tissue at various ages and their loss during immunohistochemical procedures. We further examined whether fixation affected either solubility or immunocytochemical detectability of several cytoskeletal proteins. An assay was designed to measure the solubility of cytoskeletal proteins in cryostat sections. Quantity and quality of protei

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Kost, Benedikt, Yi-Qun Bao, and Nam-Hai Chua. "Cytoskeleton and plant organogenesis." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 357, no. 1422 (2002): 777–89. http://dx.doi.org/10.1098/rstb.2002.1090.

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The functions of microtubules and actin filaments during various processes that are essential for the growth, reproduction and survival of single plant cells have been well characterized. A large number of plant structural cytoskeletal or cytoskeleton–associated proteins, as well as genes encoding such proteins, have been identified. Although many of these genes and proteins have been partially characterized with respect to their functions, a coherent picture of how they interact to execute cytoskeletal functions in plant cells has yet to emerge. Cytoskeleton–controlled cellular processes are

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Gillespie, C. S., R. Wilson, A. Davidson, and P. J. Brophy. "Characterization of a cytoskeletal matrix associated with myelin from rat brain." Biochemical Journal 260, no. 3 (1989): 689–96. http://dx.doi.org/10.1042/bj2600689.

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Extraction of rat brain myelin in a buffer containing Triton X-100 yielded a soluble fraction and an insoluble residue that was enriched in cytoskeletal elements. Immunoblot analysis of the detergent-soluble fraction and the insoluble cytoskeletal residue showed that all of the tubulin and more than half of the actin were found within the cytoskeletal fraction. The distribution of myelin-specific proteins was also examined, and revealed that 2′,3′-cyclic nucleotide 3′-phosphohydrolase (CNPase) I and most of the myelin basic proteins (MBPs) were equally distributed between both fractions. By co

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Wickstead, Bill, and Keith Gull. "The evolution of the cytoskeleton." Journal of Cell Biology 194, no. 4 (2011): 513–25. http://dx.doi.org/10.1083/jcb.201102065.

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The cytoskeleton is a system of intracellular filaments crucial for cell shape, division, and function in all three domains of life. The simple cytoskeletons of prokaryotes show surprising plasticity in composition, with none of the core filament-forming proteins conserved in all lineages. In contrast, eukaryotic cytoskeletal function has been hugely elaborated by the addition of accessory proteins and extensive gene duplication and specialization. Much of this complexity evolved before the last common ancestor of eukaryotes. The distribution of cytoskeletal filaments puts constraints on the l

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Knecht, David A. "The effect of cytoskeletal protein mutations on cell motility and morphogenesis." Proceedings, annual meeting, Electron Microscopy Society of America 50, no. 1 (1992): 594–95. http://dx.doi.org/10.1017/s0424820100123374.

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The cortical cytoskeleton of eukaryotic cells is composed of actin filaments and a variety of associated proteins. The polymerization, depolymerization, cross-linking and bundling of these filaments, are presumed to be intimately involved in such processes as cell motility, cell adhesion and cell shape. In developing systems, all of these processes are involved in the morphogenetic mechanisms that shape tissues, organs and organisms.We are investigating the complex interactions among cytoskeletal proteins using the simple eukaryotic amoebae, Dictyostelium discoideum. Our approach is to determi

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Fanning, Alan S., Christina M. Van Itallie, and James M. Anderson. "Zonula occludens-1 and -2 regulate apical cell structure and the zonula adherens cytoskeleton in polarized epithelia." Molecular Biology of the Cell 23, no. 4 (2012): 577–90. http://dx.doi.org/10.1091/mbc.e11-09-0791.

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The structure and function of both adherens (AJ) and tight (TJ) junctions are dependent on the cortical actin cytoskeleton. The zonula occludens (ZO)-1 and -2 proteins have context-dependent interactions with both junction types and bind directly to F-actin and other cytoskeletal proteins, suggesting ZO-1 and -2 might regulate cytoskeletal activity at cell junctions. To address this hypothesis, we generated stable Madin-Darby canine kidney cell lines depleted of both ZO-1 and -2. Both paracellular permeability and the localization of TJ proteins are disrupted in ZO-1/-2–depleted cells. In addi

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Stødkilde, Lene, Johan Palmfeldt, Line Nilsson, et al. "Proteomic identification of early changes in the renal cytoskeleton in obstructive uropathy." American Journal of Physiology-Renal Physiology 306, no. 12 (2014): F1429—F1441. http://dx.doi.org/10.1152/ajprenal.00244.2013.

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Bilateral ureteral obstruction (BUO) is associated with renal damage and impaired ability to concentrate urine and is known to induce alterations in an array of kidney proteins. The aim of this study was to identify acute proteomic alterations induced by BUO. Rats were subjected to BUO for 2, 6, or 24 h. Mass spectrometry-based proteomics was performed on the renal inner medulla, and protein changes in the obstructed group were identified. Significant changes were successfully identified for 109 proteins belonging to different biological classes. Interestingly, proteins belonging to the cytosk

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Toyoda, Hideki, Keiji Nakai, Serdar B. Omay, et al. "Differential Association of Protein Ser/Thr Phosphatase Types 1 and 2A with the Cytoskeleton upon Platelet Activation." Thrombosis and Haemostasis 76, no. 06 (1996): 1053–62. http://dx.doi.org/10.1055/s-0038-1650706.

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SummaryThe association of protein Ser/Thr phosphatase type 1(PP1) and type 2A (PP2A) with the cytoskeleton (Triton X-100 insoluble residue) during human platelet activation was investigated. In unstimulated platelets, 40% of total PPl-like activity was present in the Triton-insoluble cytoskeleton, while only 10% of the total PP2A-like activity was present in this fraction. Stimulation with 1 U/ml thrombin produced a 1.8-fold increase in PPl-like activity and a 7-fold increase in PP2A-like activity, respectively, in the cytoskeletal fraction, under aggregating conditions. Immunoblot analysis re

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Bezanilla, Magdalena, Amy S. Gladfelter, David R. Kovar, and Wei-Lih Lee. "Cytoskeletal dynamics: A view from the membrane." Journal of Cell Biology 209, no. 3 (2015): 329–37. http://dx.doi.org/10.1083/jcb.201502062.

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Many aspects of cytoskeletal assembly and dynamics can be recapitulated in vitro; yet, how the cytoskeleton integrates signals in vivo across cellular membranes is far less understood. Recent work has demonstrated that the membrane alone, or through membrane-associated proteins, can effect dynamic changes to the cytoskeleton, thereby impacting cell physiology. Having identified mechanistic links between membranes and the actin, microtubule, and septin cytoskeletons, these studies highlight the membrane’s central role in coordinating these cytoskeletal systems to carry out essential processes,

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Ramos-León, Félix, and Kumaran S. Ramamurthi. "Cytoskeletal proteins: lessons learned from bacteria." Physical Biology 19, no. 2 (2022): 021005. http://dx.doi.org/10.1088/1478-3975/ac4ef0.

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Abstract Cytoskeletal proteins are classified as a group that is defined functionally, whose members are capable of polymerizing into higher order structures, either dynamically or statically, to perform structural roles during a variety of cellular processes. In eukaryotes, the most well-studied cytoskeletal proteins are actin, tubulin, and intermediate filaments, and are essential for cell shape and movement, chromosome segregation, and intracellular cargo transport. Prokaryotes often harbor homologs of these proteins, but in bacterial cells, these homologs are usually not employed in roles

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Harris, Andrew R., Pamela Jreij, and Daniel A. Fletcher. "Mechanotransduction by the Actin Cytoskeleton: Converting Mechanical Stimuli into Biochemical Signals." Annual Review of Biophysics 47, no. 1 (2018): 617–31. http://dx.doi.org/10.1146/annurev-biophys-070816-033547.

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Force transmission through the actin cytoskeleton plays a central role in cell movements, shape change, and internal organization. Dynamic reorganization of actin filaments by an array of specialized binding proteins creates biochemically and architecturally distinct structures, many of which are finely tuned to exert or resist mechanical loads. The molecular complexity of the actin cytoskeleton continues to be revealed by detailed biochemical assays, and the architectural diversity and dynamics of actin structures are being uncovered by advances in super-resolution fluorescence microscopy and

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Kuznetsov, Andrey V., Sabzali Javadov, Michael Grimm, Raimund Margreiter, Michael J. Ausserlechner, and Judith Hagenbuchner. "Crosstalk between Mitochondria and Cytoskeleton in Cardiac Cells." Cells 9, no. 1 (2020): 222. http://dx.doi.org/10.3390/cells9010222.

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Elucidation of the mitochondrial regulatory mechanisms for the understanding of muscle bioenergetics and the role of mitochondria is a fundamental problem in cellular physiology and pathophysiology. The cytoskeleton (microtubules, intermediate filaments, microfilaments) plays a central role in the maintenance of mitochondrial shape, location, and motility. In addition, numerous interactions between cytoskeletal proteins and mitochondria can actively participate in the regulation of mitochondrial respiration and oxidative phosphorylation. In cardiac and skeletal muscles, mitochondrial positions

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Kriho, V., G. D. Pappas, N. Lieska, C. M. Wu, and H. Y. Yang. "Rat Reactive Astrocyte Marker (IFAP-70/280KD) is Expressed in Rat Spinal Cord Motor Neurons Following Transection of Sciatic Nerve." Microscopy and Microanalysis 3, S2 (1997): 159–60. http://dx.doi.org/10.1017/s1431927600007686.

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Following injury to peripheral nerves, processes involved in regeneration must be activated, restoring the original architecture and synaptic connections of the neuron. This is essential for the efficient operation of the sophisticated communications network of the nervous system. In order to accomplish these tasks, complex changes occur in gene expression. Regenerating neurons shift into a growth mode wherein large amounts of cytoskeletal proteins and other growth-associated proteins are produced. These materials, which are synthesized and produced in the neuronal cell body, are then transfer

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Zhang, Hong, Yuan Liu, Cencen Li та Weiya Zhang. "ITGβ6 Facilitates Skeletal Muscle Development by Maintaining the Properties and Cytoskeleton Stability of Satellite Cells". Life 12, № 7 (2022): 926. http://dx.doi.org/10.3390/life12070926.

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Integrin proteins are important receptors connecting the intracellular skeleton of satellite cells and the extracellular matrix (ECM), playing an important role in the process of skeletal muscle development. In this research, the function of ITGβ6 in regulating the differentiation of satellite cells was studied. Transcriptome and proteome analysis indicated that Itgβ6 is a key node connecting ECM-related proteins to the cytoskeleton, and it is necessary for the integrity of the membrane structure and stability of the cytoskeletal system, which are essential for satellite cell adhesion. Functio

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Tashiro, Tomoko. "Axonal transport of cytoskeletal proteins." SEIBUTSU BUTSURI KAGAKU 30, no. 1 (1986): 37–44. http://dx.doi.org/10.2198/sbk.30.37.

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&NA;. "SKELETAL MUSCLE CYTOSKELETAL PROTEINS 319." Medicine &amp Science in Sports &amp Exercise 28, Supplement (1996): 54. http://dx.doi.org/10.1097/00005768-199605001-00319.

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Biancone, L., P. Vavassori, I. Monteleone, et al. "Cytoskeletal proteins and resident flora." Digestive and Liver Disease 34 (September 2002): S34—S36. http://dx.doi.org/10.1016/s1590-8658(02)80161-x.

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Lippincott-Schwartz, Jennifer. "Cytoskeletal proteins and Golgi dynamics." Current Opinion in Cell Biology 10, no. 1 (1998): 52–59. http://dx.doi.org/10.1016/s0955-0674(98)80086-0.

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Wasserman, Steven. "FH proteins as cytoskeletal organizers." Trends in Cell Biology 8, no. 3 (1998): 111–15. http://dx.doi.org/10.1016/s0962-8924(97)01217-8.

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Horenberg, Allison L., Alisa M. Houghton, Saurav Pandey, Vikram Seshadri, and William H. Guilford. "S‐nitrosylation of cytoskeletal proteins." Cytoskeleton 76, no. 3 (2019): 243–53. http://dx.doi.org/10.1002/cm.21520.

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Fialová, Lenka, A. Bartoš, J. Soukupová, J. Švarcová, P. Ridzoň, and I. Malbohan. "Synergy of Serum and Cerebrospinal Fluid Antibodies Against Axonal Cytoskeletal Proteins in Patients with Different Neurological Diseases." Folia Biologica 55, no. 1 (2009): 23–26. http://dx.doi.org/10.14712/fb2009055010023.

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Autoantibodies against different axonal cytoskeletal proteins [the light (NFL) and medium (NFM) subunit of neurofilament and tubulin (TUB)] in serum and cerebrospinal fluid may be generated in response to the release of cytoskeleton from damaged neurons. We studied the relationships among these autoantibodies. Paired cerebrospinal fluid (CSF) and serum samples were obtained from 47 multiple sclerosis (MS) patients, 14 patients with neurodegenerative diseases, 21 patients with various neurological diseases and 16 normal control subjects. Levels of antibodies against NFL, NFM and TUB were relate

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Aunis, D., and M. F. Bader. "The cytoskeleton as a barrier to exocytosis in secretory cells." Journal of Experimental Biology 139, no. 1 (1988): 253–66. http://dx.doi.org/10.1242/jeb.139.1.253.

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Chromaffin cells of the adrenal medulla synthesize, store and secrete catecholamines. These cells contain numerous electron-dense secretory granules which discharge their contents into the extracellular space by exocytosis. The subplasmalemmal area of the chromaffin cell is characterized by the presence of a highly organized cytoskeletal network. F-Actin seems to be exclusively localized in this area and together with specific actin-binding proteins forms a dense viscoelastic gel; fodrin, vinculin and caldesmon, three actin cross-linking proteins, and gelsolin, an actin-severing protein, are f

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Carpenter, David A., Sohaib A. Khan, and Wallace Ip. "Discrimination of the assembly states of cytoskeletal proteins in cultured cells using confocal microscopy." Proceedings, annual meeting, Electron Microscopy Society of America 51 (August 1, 1993): 270–71. http://dx.doi.org/10.1017/s0424820100147193.

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The cytoskeleton is a three-dimensional network of cytoplasmic filaments that mediates many processes involving motility, and the specification and maintenance of cell form. In recent years, it has become evident that all three major components of the cytoskeleton- microfilaments, microtubules, and intermediate filaments (IF)-are dynamic structures that undergo reversible assembly-disassembly as required by the physiologic needs of the cell. While the assembled form of the cytoskeleton-the filamentous network-is readily visible by conventional immunofluorescence microscopy, it is often difficu

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Costa, Manoel Luís. "Cytoskeleton and Adhesion in Myogenesis." ISRN Developmental Biology 2014 (April 15, 2014): 1–15. http://dx.doi.org/10.1155/2014/713631.

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The function of muscle is to contract, which means to exert force on a substrate. The adaptations required for skeletal muscle differentiation, from a prototypic cell, involve specialization of housekeeping cytoskeletal contracting and supporting systems into crystalline arrays of proteins. Here I discuss the changes that all three cytoskeletal systems (microfilaments, intermediate filaments, and microtubules) undergo through myogenesis. I also discuss their interaction, through the membrane, to extracellular matrix and to other cells, where force will be exerted during contraction. The three

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Guay-Woodford, L. M., O. Platt, and H. W. Harris. "Toad urinary bladder epithelial cells contain an analogue of cytoskeletal protein 4.1." American Journal of Physiology-Cell Physiology 260, no. 6 (1991): C1308—C1314. http://dx.doi.org/10.1152/ajpcell.1991.260.6.c1308.

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Epithelial cell polarity and vectorial transport require cytoskeletal proteins that maintain local cell membrane structure and mediate cytoplasmic vesicle movement. The cytoskeleton of leaky epithelia, such as the intestinal mucosa and renal proximal tubule cells, has been extensively studied. However, cytoskeletal studies in tight epithelia such as the mammalian collecting duct and toad urinary bladder generally have been confined to ultrastructural investigation. Recent research in nonepithelial cell types has identified an interesting family of cytoskeletal proteins. Present in multiple cel

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Nemeth, Laszlo, Udo Rolle, and Prem Puri. "Altered Cytoskeleton in Smooth Muscle of Aganglionic Bowel." Archives of Pathology & Laboratory Medicine 126, no. 6 (2002): 692–96. http://dx.doi.org/10.5858/2002-126-0692-acismo.

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Abstract Context.—Intestinal motility is under the control of smooth muscle cells, enteric plexus, and hormonal factors. In Hirschsprung disease (HD), the aganglionic colon remains spastic or tonically enhanced and unable to relax. The smooth muscle cell's cytoskeleton consists of proteins or structures whose primary function is to link or connect protein filaments to each other or to the anchoring sites. Dystrophin is a subsarcolemmal protein with a double adhesion property, one between the membrane elements and the contractile filaments of the cytoskeleton and the other between the cytoskele

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Li, Jiejie, and Christopher J. Staiger. "Understanding Cytoskeletal Dynamics During the Plant Immune Response." Annual Review of Phytopathology 56, no. 1 (2018): 513–33. http://dx.doi.org/10.1146/annurev-phyto-080516-035632.

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The plant cytoskeleton is a dynamic framework of cytoplasmic filaments that rearranges as the needs of the cell change during growth and development. Incessant turnover mechanisms allow these networks to be rapidly redeployed in defense of host cytoplasm against microbial invaders. Both chemical and mechanical stimuli are recognized as danger signals to the plant, and these are perceived and transduced into cytoskeletal dynamics and architecture changes through a collection of well-recognized, previously characterized players. Recent advances in quantitative cell biology approaches, along with

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Chopard, Angele, Françoise Pons, and Jean-François Marini. "Cytoskeletal protein contents before and after hindlimb suspension in a fast and slow rat skeletal muscle." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 280, no. 2 (2001): R323—R330. http://dx.doi.org/10.1152/ajpregu.2001.280.2.r323.

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Transversal cytoskeletal organization of muscle fibers is well described, although very few data are available concerning protein content. Measurements of desmin, α-actinin, and actin contents in soleus and extensor digitorum longus (EDL) rat skeletal muscles, taken with the results previously reported for several dystrophin-glycoprotein complex (DGC) components, indicate that the contents of most cytoskeletal proteins are higher in slow-type fibers than in fast ones. The effects of hypokinesia and unloading on the cytoskeleton were also investigated, using hindlimb suspension. First, this res

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