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Journal articles on the topic 'Rho GTPases Signaling'

Author: Grafiati

Published: 7 September 2023

Last updated: 31 July 2025

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1

Mosaddeghzadeh, Niloufar, and Mohammad Reza Ahmadian. "The RHO Family GTPases: Mechanisms of Regulation and Signaling." Cells 10, no. 7 (2021): 1831. http://dx.doi.org/10.3390/cells10071831.

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Much progress has been made toward deciphering Rho GTPase functions, and many studies have convincingly demonstrated that altered signal transduction through Rho GTPases is a recurring theme in the progression of human malignancies. It seems that 20 canonical RHO GTPases are likely regulated by three GDIs, 85 GEFs, and 66 GAPs, and eventually interact with >70 downstream effectors. A recurring theme is the challenge in understanding the molecular determinants of the specificity of these four classes of interacting proteins that, irrespective of their functions, bind to common sites on the s

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Mulloy, James C., Jose A. Cancelas, Marie-Dominique Filippi, Theodosia A. Kalfa, Fukun Guo, and Yi Zheng. "Rho GTPases in hematopoiesis and hemopathies." Blood 115, no. 5 (2010): 936–47. http://dx.doi.org/10.1182/blood-2009-09-198127.

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AbstractRho family GTPases are intracellular signaling proteins regulating multiple pathways involved in cell actomyosin organization, adhesion, and proliferation. Our knowledge of their cellular functions comes mostly from previous biochemical studies that used mutant overexpression approaches in various clonal cell lines. Recent progress in understanding Rho GTPase functions in blood cell development and regulation by gene targeting of individual Rho GTPases in mice has allowed a genetic understanding of their physiologic roles in hematopoietic progenitors and mature lineages. In particular,

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Olayioye, Monilola A., Bettina Noll, and Angelika Hausser. "Spatiotemporal Control of Intracellular Membrane Trafficking by Rho GTPases." Cells 8, no. 12 (2019): 1478. http://dx.doi.org/10.3390/cells8121478.

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As membrane-associated master regulators of cytoskeletal remodeling, Rho GTPases coordinate a wide range of biological processes such as cell adhesion, motility, and polarity. In the last years, Rho GTPases have also been recognized to control intracellular membrane sorting and trafficking steps directly; however, how Rho GTPase signaling is regulated at endomembranes is still poorly understood. In this review, we will specifically address the local Rho GTPase pools coordinating intracellular membrane trafficking with a focus on the endo- and exocytic pathways. We will further highlight the sp

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Voena and Chiarle. "RHO Family GTPases in the Biology of Lymphoma." Cells 8, no. 7 (2019): 646. http://dx.doi.org/10.3390/cells8070646.

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RHO GTPases are a class of small molecules involved in the regulation of several cellular processes that belong to the RAS GTPase superfamily. The RHO family of GTPases includes several members that are further divided into two different groups: typical and atypical. Both typical and atypical RHO GTPases are critical transducers of intracellular signaling and have been linked to human cancer. Significantly, both gain-of-function and loss-of-function mutations have been described in human tumors with contradicting roles depending on the cell context. The RAS family of GTPases that also belong t

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Zubor, Pavol, Zuzana Dankova, Zuzana Kolkova, et al. "Rho GTPases in Gynecologic Cancers: In-Depth Analysis toward the Paradigm Change from Reactive to Predictive, Preventive, and Personalized Medical Approach Benefiting the Patient and Healthcare." Cancers 12, no. 5 (2020): 1292. http://dx.doi.org/10.3390/cancers12051292.

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Rho guanosine triphospatases (GTPases) resemble a conserved family of GTP-binding proteins regulating actin cytoskeleton dynamics and several signaling pathways central for the cell. Rho GTPases create a so-called Ras-superfamily of GTPases subdivided into subgroups comprising at least 20 members. Rho GTPases play a key regulatory role in gene expression, cell cycle control and proliferation, epithelial cell polarity, cell migration, survival, and apoptosis, among others. They also have tissue-related functions including angiogenesis being involved in inflammatory and wound healing processes.

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Fritz, Rafael Dominik, and Olivier Pertz. "The dynamics of spatio-temporal Rho GTPase signaling: formation of signaling patterns." F1000Research 5 (April 26, 2016): 749. http://dx.doi.org/10.12688/f1000research.7370.1.

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Rho GTPases are crucial signaling molecules that regulate a plethora of biological functions. Traditional biochemical, cell biological, and genetic approaches have founded the basis of Rho GTPase biology. The development of biosensors then allowed measuring Rho GTPase activity with unprecedented spatio-temporal resolution. This revealed that Rho GTPase activity fluctuates on time and length scales of tens of seconds and micrometers, respectively. In this review, we describe Rho GTPase activity patterns observed in different cell systems. We then discuss the growing body of evidence that upstre

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Barlow, Haley Rose, and Ondine Cleaver. "Building Blood Vessels—One Rho GTPase at a Time." Cells 8, no. 6 (2019): 545. http://dx.doi.org/10.3390/cells8060545.

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Blood vessels are required for the survival of any organism larger than the oxygen diffusion limit. Blood vessel formation is a tightly regulated event and vessel growth or changes in permeability are linked to a number of diseases. Elucidating the cell biology of endothelial cells (ECs), which are the building blocks of blood vessels, is thus critical to our understanding of vascular biology and to the development of vascular-targeted disease treatments. Small GTPases of the Rho GTPase family are known to regulate several processes critical for EC growth and maintenance. In fact, many of the

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Kjøller, Lars, and Alan Hall. "Signaling to Rho GTPases." Experimental Cell Research 253, no. 1 (1999): 166–79. http://dx.doi.org/10.1006/excr.1999.4674.

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9

Zhang, Zheng, Ming Liu, and Yi Zheng. "Role of Rho GTPases in stem cell regulation." Biochemical Society Transactions 49, no. 6 (2021): 2941–55. http://dx.doi.org/10.1042/bst20211071.

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The future of regenerative medicine relies on our understanding of stem cells which are essential for tissue/organ generation and regeneration to maintain and/or restore tissue homeostasis. Rho family GTPases are known regulators of a wide variety of cellular processes related to cytoskeletal dynamics, polarity and gene transcription. In the last decade, major new advances have been made in understanding the regulatory role and mechanism of Rho GTPases in self-renewal, differentiation, migration, and lineage specification in tissue-specific signaling mechanisms in various stem cell types to re

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Guo, Daji, Xiaoman Yang, and Lei Shi. "Rho GTPase Regulators and Effectors in Autism Spectrum Disorders: Animal Models and Insights for Therapeutics." Cells 9, no. 4 (2020): 835. http://dx.doi.org/10.3390/cells9040835.

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The Rho family GTPases are small G proteins that act as molecular switches shuttling between active and inactive forms. Rho GTPases are regulated by two classes of regulatory proteins, guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs). Rho GTPases transduce the upstream signals to downstream effectors, thus regulating diverse cellular processes, such as growth, migration, adhesion, and differentiation. In particular, Rho GTPases play essential roles in regulating neuronal morphology and function. Recent evidence suggests that dysfunction of Rho GTPase signaling c

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11

Dandamudi, Akhila, Huzoor Akbar, Jose Cancelas, and Yi Zheng. "Rho GTPase Signaling in Platelet Regulation and Implication for Antiplatelet Therapies." International Journal of Molecular Sciences 24, no. 3 (2023): 2519. http://dx.doi.org/10.3390/ijms24032519.

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Platelets play a vital role in regulating hemostasis and thrombosis. Rho GTPases are well known as molecular switches that control various cellular functions via a balanced GTP-binding/GTP-hydrolysis cycle and signaling cascade through downstream effectors. In platelets, Rho GTPases function as critical regulators by mediating signal transduction that drives platelet activation and aggregation. Mostly by gene targeting and pharmacological inhibition approaches, Rho GTPase family members RhoA, Rac1, and Cdc42 have been shown to be indispensable in regulating the actin cytoskeleton dynamics in p

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Bai, Yanyang, Xiaoliang Xiang, Chunmei Liang, and Lei Shi. "Regulating Rac in the Nervous System: Molecular Function and Disease Implication of Rac GEFs and GAPs." BioMed Research International 2015 (2015): 1–17. http://dx.doi.org/10.1155/2015/632450.

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Rho family GTPases, including RhoA, Rac1, and Cdc42 as the most studied members, are master regulators of actin cytoskeletal organization. Rho GTPases control various aspects of the nervous system and are associated with a number of neuropsychiatric and neurodegenerative diseases. The activity of Rho GTPases is controlled by two families of regulators, guanine nucleotide exchange factors (GEFs) as the activators and GTPase-activating proteins (GAPs) as the inhibitors. Through coordinated regulation by GEFs and GAPs, Rho GTPases act as converging signaling molecules that convey different upstre

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Herbrand, Ulrike, and Mohammad Reza Ahmadian. "p190-RhoGAP as an integral component of the Tiam1/Rac1-induced downregulation of Rho." Biological Chemistry 387, no. 3 (2006): 311–17. http://dx.doi.org/10.1515/bc.2006.041.

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Abstract The Rho family of small GTPases plays a central role in intracellular signal transduction, particularly in reorganization of the actin cytoskeleton. Rho activity induces cell contractility, whereas Rac promotes cellular protrusion, which counteracts Rho signaling. In this regard, the reciprocal balance between these GTPases determines cell morphology and migratory behavior. Here we demonstrate that Tiam1/Rac1 signaling is able to antagonize Rho activity directly at the GTPase level in COS-7 cells. p190-RhoGAP plays a central regulatory role in this signaling pathway. Interfering with

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Saliani, Mahsa, Amin Mirzaiebadizi, Niloufar Mosaddeghzadeh, and Mohammad Reza Ahmadian. "RHO GTPase-Related Long Noncoding RNAs in Human Cancers." Cancers 13, no. 21 (2021): 5386. http://dx.doi.org/10.3390/cancers13215386.

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RHO GTPases are critical signal transducers that regulate cell adhesion, polarity, and migration through multiple signaling pathways. While all these cellular processes are crucial for the maintenance of normal cell homeostasis, disturbances in RHO GTPase-associated signaling pathways contribute to different human diseases, including many malignancies. Several members of the RHO GTPase family are frequently upregulated in human tumors. Abnormal gene regulation confirms the pivotal role of lncRNAs as critical gene regulators, and thus, they could potentially act as oncogenes or tumor suppressor

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Navarro-Lérida, Inmaculada, Miguel Sánchez-Álvarez, and Miguel Ángel del Pozo. "Post-Translational Modification and Subcellular Compartmentalization: Emerging Concepts on the Regulation and Physiopathological Relevance of RhoGTPases." Cells 10, no. 8 (2021): 1990. http://dx.doi.org/10.3390/cells10081990.

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Cells and tissues are continuously exposed to both chemical and physical stimuli and dynamically adapt and respond to this variety of external cues to ensure cellular homeostasis, regulated development and tissue-specific differentiation. Alterations of these pathways promote disease progression—a prominent example being cancer. Rho GTPases are key regulators of the remodeling of cytoskeleton and cell membranes and their coordination and integration with different biological processes, including cell polarization and motility, as well as other signaling networks such as growth signaling and pr

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Delaguillaumie, Alix, Cécile Lagaudrière-Gesbert, Michel R. Popoff, and Hélène Conjeaud. "Rho GTPases link cytoskeletal rearrangements and activation processes induced via the tetraspanin CD82 in T lymphocytes." Journal of Cell Science 115, no. 2 (2002): 433–43. http://dx.doi.org/10.1242/jcs.115.2.433.

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Activation of T lymphocytes requires the engagement of the T-cell receptor and costimulation molecules through cell-to-cell contacts. The tetraspanin CD82 has previously been shown to act as a cytoskeleton-dependent costimulation molecule. We show here that CD82 engagement leads to the tyrosine phosphorylation and association of both the Rho GTPases guanosine exchange factor Vav1 and adapter protein SLP76, suggesting that Rho GTPases participate in CD82 signaling. Indeed, broad inactivation of all Rho GTPases, or a specific blockade of RhoA, Rac1 or Cdc42, inhibited the morphological changes l

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Aslan, Joseph E., Sandra M. Baker, Cassandra P. Loren, et al. "The PAK system links Rho GTPase signaling to thrombin-mediated platelet activation." American Journal of Physiology-Cell Physiology 305, no. 5 (2013): C519—C528. http://dx.doi.org/10.1152/ajpcell.00418.2012.

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Regulation of the platelet actin cytoskeleton by the Rho family of small GTPases is essential for the proper maintenance of hemostasis. However, little is known about how intracellular platelet activation from Rho GTPase family members, including Rac, Cdc42, and Rho, translate into changes in platelet actin structures. To better understand how Rho family GTPases coordinate platelet activation, we identified platelet proteins associated with Rac1, a Rho GTPase family member, and actin regulatory protein essential for platelet hemostatic function. Mass spectrometry analysis revealed that upon pl

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Van Aelst, L., and C. D'Souza-Schorey. "Rho GTPases and signaling networks." Genes & Development 11, no. 18 (1997): 2295–322. http://dx.doi.org/10.1101/gad.11.18.2295.

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Dipankar, Pankaj, Puneet Kumar, Shiba Prasad Dash, and Pranita P. Sarangi. "Functional and Therapeutic Relevance of Rho GTPases in Innate Immune Cell Migration and Function during Inflammation: An In Silico Perspective." Mediators of Inflammation 2021 (February 13, 2021): 1–10. http://dx.doi.org/10.1155/2021/6655412.

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Systematic regulation of leukocyte migration to the site of infection is a vital step during immunological responses. Improper migration and localization of immune cells could be associated with disease pathology as seen in systemic inflammation. Rho GTPases act as molecular switches during inflammatory cell migration by cycling between Rho-GDP (inactive) to Rho-GTP (active) forms and play an essential role in the precise regulation of actin cytoskeletal dynamics as well as other immunological functions of leukocytes. Available reports suggest that the dysregulation of Rho GTPase signaling is

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Jung, Haiyoung, Suk Ran Yoon, Jeewon Lim, Hee Jun Cho, and Hee Gu Lee. "Dysregulation of Rho GTPases in Human Cancers." Cancers 12, no. 5 (2020): 1179. http://dx.doi.org/10.3390/cancers12051179.

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Rho GTPases play central roles in numerous cellular processes, including cell motility, cell polarity, and cell cycle progression, by regulating actin cytoskeletal dynamics and cell adhesion. Dysregulation of Rho GTPase signaling is observed in a broad range of human cancers, and is associated with cancer development and malignant phenotypes, including metastasis and chemoresistance. Rho GTPase activity is precisely controlled by guanine nucleotide exchange factors, GTPase-activating proteins, and guanine nucleotide dissociation inhibitors. Recent evidence demonstrates that it is also regulate

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Mosaddeghzadeh, Niloufar, Kazem Nouri, Oliver H. F. Krumbach, Ehsan Amin, Radovan Dvorsky, and Mohammad R. Ahmadian. "Selectivity Determinants of RHO GTPase Binding to IQGAPs." International Journal of Molecular Sciences 22, no. 22 (2021): 12596. http://dx.doi.org/10.3390/ijms222212596.

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IQ motif-containing GTPase-activating proteins (IQGAPs) modulate a wide range of cellular processes by acting as scaffolds and driving protein components into distinct signaling networks. Their functional states have been proposed to be controlled by members of the RHO family of GTPases, among other regulators. In this study, we show that IQGAP1 and IQGAP2 can associate with CDC42 and RAC1-like proteins but not with RIF, RHOD, or RHO-like proteins, including RHOA. This seems to be based on the distribution of charged surface residues, which varies significantly among RHO GTPases despite their

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Arrazola Sastre, Alazne, Miriam Luque Montoro, Patricia Gálvez-Martín, et al. "Small GTPases of the Ras and Rho Families Switch on/off Signaling Pathways in Neurodegenerative Diseases." International Journal of Molecular Sciences 21, no. 17 (2020): 6312. http://dx.doi.org/10.3390/ijms21176312.

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Small guanosine triphosphatases (GTPases) of the Ras superfamily are key regulators of many key cellular events such as proliferation, differentiation, cell cycle regulation, migration, or apoptosis. To control these biological responses, GTPases activity is regulated by guanine nucleotide exchange factors (GEFs), GTPase activating proteins (GAPs), and in some small GTPases also guanine nucleotide dissociation inhibitors (GDIs). Moreover, small GTPases transduce signals by their downstream effector molecules. Many studies demonstrate that small GTPases of the Ras family are involved in neurode

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Herrmann, Andrea, Britta A. M. Tillmann, Janine Schürmann, Michael Bölker, and Paul Tudzynski. "Small-GTPase-Associated Signaling by the Guanine Nucleotide Exchange Factors CpDock180 and CpCdc24, the GTPase Effector CpSte20, and the Scaffold Protein CpBem1 in Claviceps purpurea." Eukaryotic Cell 13, no. 4 (2014): 470–82. http://dx.doi.org/10.1128/ec.00332-13.

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ABSTRACTMonomeric GTPases of the Rho subfamily are important mediators of polar growth and NADPH (Nox) signaling in a variety of organisms. These pathways influence the ability ofClaviceps purpureato infect host plants. GTPase regulators contribute to the nucleotide loading cycle that is essential for proper functionality of the GTPases. Scaffold proteins gather GTPase complexes to facilitate proper function. The guanine nucleotide exchange factors (GEFs) CpCdc24 and CpDock180 activate GTPase signaling by triggering nucleotide exchange of the GTPases. Here we show that CpCdc24 harbors nucleoti

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Simon, Cory M., Emily M. Vaughan, William M. Bement, and Leah Edelstein-Keshet. "Pattern formation of Rho GTPases in single cell wound healing." Molecular Biology of the Cell 24, no. 3 (2013): 421–32. http://dx.doi.org/10.1091/mbc.e12-08-0634.

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The Rho GTPases—Rho, Rac, and Cdc42—control an enormous variety of processes, many of which reflect activation of these GTPases in spatially confined and mutually exclusive zones. By using mathematical models and experimental results to establish model parameters, we analyze the formation and segregation of Rho and Cdc42 zones during Xenopus oocyte wound repair and the role played by Abr, a dual guanine nucleotide exchange factor–GTPase-activating protein, in this process. The Rho and Cdc42 zones are found to be best represented as manifestations of spatially modulated bistability, and local p

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DerMardirossian, Céline, Gabriel Rocklin, Ji-Yeon Seo, and Gary M. Bokoch. "Phosphorylation of RhoGDI by Src Regulates Rho GTPase Binding and Cytosol-Membrane Cycling." Molecular Biology of the Cell 17, no. 11 (2006): 4760–68. http://dx.doi.org/10.1091/mbc.e06-06-0533.

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Rho GTPases (Rac, Rho, and Cdc42) play important roles in regulating cell function through their ability to coordinate the actin cytoskeleton, modulate the formation of signaling reactive oxidant species, and control gene transcription. Activation of Rho GTPase signaling pathways requires the regulated release of Rho GTPases from RhoGDI complexes, followed by their reuptake after membrane cycling. We show here that Src kinase binds and phosphorylates RhoGDI both in vitro and in vivo at Tyr156. Analysis of Rho GTPase–RhoGDI complexes using in vitro assays of complexation and in vivo by coimmuno

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Dahmene, Manel, Laura Quirion, and Mélanie Laurin. "High Throughput strategies Aimed at Closing the GAP in Our Knowledge of Rho GTPase Signaling." Cells 9, no. 6 (2020): 1430. http://dx.doi.org/10.3390/cells9061430.

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Since their discovery, Rho GTPases have emerged as key regulators of cytoskeletal dynamics. In humans, there are 20 Rho GTPases and more than 150 regulators that belong to the RhoGEF, RhoGAP, and RhoGDI families. Throughout development, Rho GTPases choregraph a plethora of cellular processes essential for cellular migration, cell–cell junctions, and cell polarity assembly. Rho GTPases are also significant mediators of cancer cell invasion. Nevertheless, to date only a few molecules from these intricate signaling networks have been studied in depth, which has prevented appreciation for the full

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Schlessinger, K., A. Hall, and N. Tolwinski. "Wnt signaling pathways meet Rho GTPases." Genes & Development 23, no. 3 (2009): 265–77. http://dx.doi.org/10.1101/gad.1760809.

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Schmitz, Arndt A. P., Eve-Ellen Govek, Benjamin Böttner, and Linda Van Aelst. "Rho GTPases: Signaling, Migration, and Invasion." Experimental Cell Research 261, no. 1 (2000): 1–12. http://dx.doi.org/10.1006/excr.2000.5049.

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Li, Xiaoyu, Xia Bu, Binfeng Lu, Hava Avraham, Richard A. Flavell, and Bing Lim. "The Hematopoiesis-Specific GTP-Binding Protein RhoH Is GTPase Deficient and Modulates Activities of Other Rho GTPases by an Inhibitory Function." Molecular and Cellular Biology 22, no. 4 (2002): 1158–71. http://dx.doi.org/10.1128/mcb.22.4.1158-1171.2002.

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ABSTRACT The Rho subfamily of small GTP-binding proteins mediates many fundamental cellular functions. The commonly studied members (Rho, Rac, and CDC42) regulate actin reorganization, affecting diverse cellular responses, including adhesion, cytokinesis, and motility. Another major function of the Rho GTPases is their role in regulating transcriptional factors and nuclear signaling. RhoH is encoded by a hematopoiesis-specific Rho-related gene recently identified in a fusion transcript with bcl6 in lymphoma cell lines. Significantly, translocations and a high frequency of RhoH mutation have be

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Platre, Matthieu Pierre, Vincent Bayle, Laia Armengot, et al. "Developmental control of plant Rho GTPase nano-organization by the lipid phosphatidylserine." Science 364, no. 6435 (2019): 57–62. http://dx.doi.org/10.1126/science.aav9959.

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Rho guanosine triphosphatases (GTPases) are master regulators of cell signaling, but how they are regulated depending on the cellular context is unclear. We found that the phospholipid phosphatidylserine acts as a developmentally controlled lipid rheostat that tunes Rho GTPase signaling in Arabidopsis. Live superresolution single-molecule imaging revealed that the protein Rho of Plants 6 (ROP6) is stabilized by phosphatidylserine into plasma membrane nanodomains, which are required for auxin signaling. Our experiments also revealed that the plasma membrane phosphatidylserine content varies dur

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Park, Gyeongah, Zhen Jin, Hui Lu, and Jianyang Du. "Clearing Amyloid-Beta by Astrocytes: The Role of Rho GTPases Signaling Pathways as Potential Therapeutic Targets." Brain Sciences 14, no. 12 (2024): 1239. https://doi.org/10.3390/brainsci14121239.

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Astrocytes, vital support cells in the central nervous system (CNS), are crucial for maintaining neuronal health. In neurodegenerative diseases such as Alzheimer’s disease (AD), astrocytes play a key role in clearing toxic amyloid-β (Aβ) peptides. Aβ, a potent neuroinflammatory trigger, stimulates astrocytes to release excessive glutamate and inflammatory factors, exacerbating neuronal dysfunction and death. Recent studies underscore the role of Rho GTPases—particularly RhoA, Rac1, and Cdc42—in regulating Aβ clearance and neuroinflammation. These key regulators of cytoskeletal dynamics and int

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Annan, Robert B., Cunle Wu, Daniel D. Waller, Malcolm Whiteway, and David Y. Thomas. "Rho5p Is Involved in Mediating the Osmotic Stress Response in Saccharomyces cerevisiae, and Its Activity Is Regulated via Msi1p and Npr1p by Phosphorylation and Ubiquitination." Eukaryotic Cell 7, no. 9 (2008): 1441–49. http://dx.doi.org/10.1128/ec.00120-08.

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ABSTRACT Small GTPases of the Rho family act as molecular switches, and modulation of the GTP-bound state of Rho proteins is a well-characterized means of regulating their signaling activity in vivo. In contrast, the regulation of Rho-type GTPases by posttranslational modifications is poorly understood. Here, we present evidence of the control of the Saccharomyces cerevisiae Rho-type GTPase Rho5p by phosphorylation and ubiquitination. Rho5p binds to Ste50p, and the expression of the activated RHO5(Q91H) allele in an Δste50 strain is lethal under conditions of osmotic stress. An overexpression

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Reyes, Steve B., Anjana S. Narayanan, Hye Shin Lee та ін. "αvβ8 integrin interacts with RhoGDI1 to regulate Rac1 and Cdc42 activation and drive glioblastoma cell invasion". Molecular Biology of the Cell 24, № 4 (2013): 474–82. http://dx.doi.org/10.1091/mbc.e12-07-0521.

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The malignant brain cancer glioblastoma multiforme (GBM) displays invasive growth behaviors that are regulated by extracellular cues within the neural microenvironment. The adhesion and signaling pathways that drive GBM cell invasion remain largely uncharacterized. Here we use human GBM cell lines, primary patient samples, and preclinical mouse models to demonstrate that integrin αvβ8 is a major driver of GBM cell invasion. β8 integrin is overexpressed in many human GBM cells, with higher integrin expression correlating with increased invasion and diminished patient survival. Silencing β8 inte

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Brakebusch, Cord. "Rho GTPase Signaling in Health and Disease: A Complex Signaling Network." Cells 10, no. 2 (2021): 401. http://dx.doi.org/10.3390/cells10020401.

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Zhang, Bo, Guohua Yang, Yu Chen, et al. "C-terminal domain (CTD) phosphatase links Rho GTPase signaling to Pol II CTD phosphorylation in Arabidopsis and yeast." Proceedings of the National Academy of Sciences 113, no. 50 (2016): E8197—E8206. http://dx.doi.org/10.1073/pnas.1605871113.

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Rho GTPases, including the Rho, Cdc42, Rac, and ROP subfamilies, act as pivotal signaling switches in various growth and developmental processes. Compared with the well-defined role of cytoskeletal organization in Rho signaling, much less is known regarding transcriptional regulation. In a mutant screen for phenotypic enhancers of transgenic Arabidopsis plants expressing a constitutively active form of ROP2 (designated CA1-1), we identified RNA polymerase II (Pol II) C-terminal domain (CTD) phosphatase-like 1 (CPL1) as a transcriptional regulator of ROP2 signaling. We show that ROP2 activation

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Lawson, Campbell D., and Anne J. Ridley. "Rho GTPase signaling complexes in cell migration and invasion." Journal of Cell Biology 217, no. 2 (2017): 447–57. http://dx.doi.org/10.1083/jcb.201612069.

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Cell migration is dependent on the dynamic formation and disassembly of actin filament–based structures, including lamellipodia, filopodia, invadopodia, and membrane blebs, as well as on cell–cell and cell–extracellular matrix adhesions. These processes all involve Rho family small guanosine triphosphatases (GTPases), which are regulated by the opposing actions of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs). Rho GTPase activity needs to be precisely tuned at distinct cellular locations to enable cells to move in response to different environments and stimul

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Danley, D. E., T. H. Chuang, and G. M. Bokoch. "Defective Rho GTPase regulation by IL-1 beta-converting enzyme-mediated cleavage of D4 GDP dissociation inhibitor." Journal of Immunology 157, no. 2 (1996): 500–503. http://dx.doi.org/10.4049/jimmunol.157.2.500.

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Abstract GTPases of the Rho family regulate many aspects of inflammatory cell activity, including motility, formation of toxic oxygen metabolites, and generation of proinflammatory cytokines. Defective regulation of such signaling pathways leads to a variety of acute and chronic inflammatory disorders, although the mechanisms by which this occurs have not been well defined. We describe in this work specific proteolytic cleavage of D4 GDI, a critical regulator of Rho GTPase activity in inflammatory leukocytes, by IL-1 beta-converting enzyme (ICE). Cleavage of D4 GDI by ICE occurs at Asp55, lead

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Dautt-Castro, Mitzuko, Montserrat Rosendo-Vargas, and Sergio Casas-Flores. "The Small GTPases in Fungal Signaling Conservation and Function." Cells 10, no. 5 (2021): 1039. http://dx.doi.org/10.3390/cells10051039.

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Monomeric GTPases, which belong to the Ras superfamily, are small proteins involved in many biological processes. They are fine-tuned regulated by guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs). Several families have been identified in organisms from different kingdoms. Overall, the most studied families are Ras, Rho, Rab, Ran, Arf, and Miro. Recently, a new family named Big Ras GTPases was reported. As a general rule, the proteins of all families have five characteristic motifs (G1–G5), and some specific features for each family have been described. Here, we

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Zuo, Yan, Wonkyung Oh, Arzu Ulu, and Jeffrey A. Frost. "Minireview: Mouse Models of Rho GTPase Function in Mammary Gland Development, Tumorigenesis, and Metastasis." Molecular Endocrinology 30, no. 3 (2016): 278–89. http://dx.doi.org/10.1210/me.2015-1294.

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Abstract Ras homolog (Rho) family small GTPases are critical regulators of actin cytoskeletal organization, cell motility, proliferation, and survival. Surprisingly, the large majority of the studies underlying our knowledge of Rho protein function have been carried out in cultured cells, and it is only recently that researchers have begun to assess Rho GTPase regulation and function in vivo. The purpose of this review is to evaluate our current knowledge of Rho GTPase function in mouse mammary gland development, tumorigenesis and metastasis. Although our knowledge is still incomplete, these s

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Fusco, Ludovico, Riwal Lefort, Kevin Smith, et al. "Computer vision profiling of neurite outgrowth dynamics reveals spatiotemporal modularity of Rho GTPase signaling." Journal of Cell Biology 212, no. 1 (2016): 91–111. http://dx.doi.org/10.1083/jcb.201506018.

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Rho guanosine triphosphatases (GTPases) control the cytoskeletal dynamics that power neurite outgrowth. This process consists of dynamic neurite initiation, elongation, retraction, and branching cycles that are likely to be regulated by specific spatiotemporal signaling networks, which cannot be resolved with static, steady-state assays. We present NeuriteTracker, a computer-vision approach to automatically segment and track neuronal morphodynamics in time-lapse datasets. Feature extraction then quantifies dynamic neurite outgrowth phenotypes. We identify a set of stereotypic neurite outgrowth

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Bokoch, Gary M., and Becky A. Diebold. "Current molecular models for NADPH oxidase regulation by Rac GTPase." Blood 100, no. 8 (2002): 2692–95. http://dx.doi.org/10.1182/blood-2002-04-1149.

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Reactive oxygen species (ROS) have been increasingly recognized as important components of cell signaling in addition to their well-established roles in host defense. The formation of ROS in phagocytic and nonphagocytic cells involves membrane-localized and Rac guanosine triphosphatase (GTPase)–regulated reduced nicotinamide adenine dinucleotide phosphate (NADPH) oxidase(s). We discuss here the current molecular models for Rac GTPase action in the control of the phagocytic leukocyte NADPH oxidase. As a mechanistically detailed example of Rac GTPase signaling, the NADPH oxidase provides a poten

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Essler, Markus, Stefan Linder, Barbara Schell, et al. "Cytotoxic Necrotizing Factor 1 of Escherichia coli Stimulates Rho/Rho-Kinase-Dependent Myosin Light-Chain Phosphorylation without Inactivating Myosin Light-Chain Phosphatase in Endothelial Cells." Infection and Immunity 71, no. 9 (2003): 5188–93. http://dx.doi.org/10.1128/iai.71.9.5188-5193.2003.

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ABSTRACT Cytotoxic necrotizing factor 1 (CNF-1) is an exotoxin of Escherichia coli that constitutively activates the GTPases Rho, Rac, and CDC42. Stimulation of Rho was shown to enhance myosin light-chain (MLC) phosphorylation via Rho kinase-mediated inhibition of MLC phosphatase in endothelial cells. Here we report that 3 h after CNF stimulation of endothelial cells, RhoA was activated and MLC phosphorylation was increased in a Rho/Rho-kinase-dependent manner, but no decrease in MLC phosphatase activity could be detected. Despite continuous RhoA activation, MLC phosphatase activity was double

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Puetz, Sandra, Lubomir T. Lubomirov, and Gabriele Pfitzer. "Regulation of Smooth Muscle Contraction by Small GTPases." Physiology 24, no. 6 (2009): 342–56. http://dx.doi.org/10.1152/physiol.00023.2009.

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Next to changes in cytosolic [Ca2+], members of the Rho subfamily of small GTPases, in particular Rho and its effector Rho kinase, also known as ROK or ROCK, emerged as key regulators of smooth muscle function in health and disease. In this review, we will focus on the regulation of the contractile machinery by Rho/ROK signaling and its interaction with PKC and cyclic nucleotide signaling. We will briefly discuss the emerging evidence that remodeling of cortical actin is necessary for contraction.

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Eroumé, K., A. Vasilevich, S. Vermeulen, J. de Boer, and A. Carlier. "On the influence of cell shape on dynamic reaction-diffusion polarization patterns." PLOS ONE 16, no. 3 (2021): e0248293. http://dx.doi.org/10.1371/journal.pone.0248293.

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The distribution of signaling molecules following mechanical or chemical stimulation of a cell defines cell polarization, with regions of high active Cdc42 at the front and low active Cdc42 at the rear. As reaction-diffusion phenomena between signaling molecules, such as Rho GTPases, define the gradient dynamics, we hypothesize that the cell shape influences the maintenance of the “front-to-back” cell polarization patterns. We investigated the influence of cell shape on the Cdc42 patterns using an established computational polarization model. Our simulation results showed that not only cell sh

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Engelhardt, Stefan, Adriana Trutzenberg, and Ralph Hückelhoven. "Regulation and Functions of ROP GTPases in Plant–Microbe Interactions." Cells 9, no. 9 (2020): 2016. http://dx.doi.org/10.3390/cells9092016.

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Rho proteins of plants (ROPs) form a specific clade of Rho GTPases, which are involved in either plant immunity or susceptibility to diseases. They are intensively studied in grass host plants, in which ROPs are signaling hubs downstream of both cell surface immune receptor kinases and intracellular nucleotide-binding leucine-rich repeat receptors, which activate major branches of plant immune signaling. Additionally, invasive fungal pathogens may co-opt the function of ROPs for manipulation of the cytoskeleton, cell invasion and host cell developmental reprogramming, which promote pathogenic

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Clark, Edwin A., Warren G. King, Joan S. Brugge, Marc Symons, and Richard O. Hynes. "Integrin-mediated Signals Regulated by Members of the Rho Family of GTPases." Journal of Cell Biology 142, no. 2 (1998): 573–86. http://dx.doi.org/10.1083/jcb.142.2.573.

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The organization of the actin cytoskeleton can be regulated by soluble factors that trigger signal transduction events involving the Rho family of GTPases. Since adhesive interactions are also capable of organizing the actin-based cytoskeleton, we examined the role of Cdc42-, Rac-, and Rho-dependent signaling pathways in regulating the cytoskeleton during integrin-mediated adhesion and cell spreading using dominant-inhibitory mutants of these GTPases. When Rat1 cells initially adhere to the extracellular matrix protein fibronectin, punctate focal complexes form at the cell periphery. Concomita

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Ueyama, Takehiko. "Rho-Family Small GTPases: From Highly Polarized Sensory Neurons to Cancer Cells." Cells 8, no. 2 (2019): 92. http://dx.doi.org/10.3390/cells8020092.

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The small GTPases of the Rho-family (Rho-family GTPases) have various physiological functions, including cytoskeletal regulation, cell polarity establishment, cell proliferation and motility, transcription, reactive oxygen species (ROS) production, and tumorigenesis. A relatively large number of downstream targets of Rho-family GTPases have been reported for in vitro studies. However, only a small number of signal pathways have been established at the in vivo level. Cumulative evidence for the functions of Rho-family GTPases has been reported for in vivo studies using genetically engineered mo

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El Baba, Nada, Mohammad Farran, Elie Abi Khalil, Leila Jaafar, Isabelle Fakhoury, and Mirvat El-Sibai. "The Role of Rho GTPases in VEGF Signaling in Cancer Cells." Analytical Cellular Pathology 2020 (April 16, 2020): 1–11. http://dx.doi.org/10.1155/2020/2097214.

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Vascular endothelial growth factors (VEGFs) consist of five molecules (VEGFA through D as well as placental growth factor) which are crucial for regulating key cellular and tissue functions. The role of VEGF and its intracellular signaling and downstream molecular pathways have been thoroughly studied. Activation of VEGF signal transduction can be initiated by the molecules’ binding to two classes of transmembrane receptors: (1) the VEGF tyrosine kinase receptors (VEGF receptors 1 through 3) and (2) the neuropilins (NRP1 and 2). The involvement of Rho GTPases in modulating VEGFA signaling in b

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Killoran, Ryan C., and Matthew J. Smith. "Conformational resolution of nucleotide cycling and effector interactions for multiple small GTPases determined in parallel." Journal of Biological Chemistry 294, no. 25 (2019): 9937–48. http://dx.doi.org/10.1074/jbc.ra119.008653.

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Small GTPases alternatively bind GDP/GTP guanine nucleotides to gate signaling pathways that direct most cellular processes. Numerous GTPases are implicated in oncogenesis, particularly the three RAS isoforms HRAS, KRAS, and NRAS and the RHO family GTPase RAC1. Signaling networks comprising small GTPases are highly connected, and there is some evidence of direct biochemical cross-talk between their functional G-domains. The activation potential of a given GTPase is contingent on a codependent interaction with the nucleotide and a Mg2+ ion, which bind to individual variants with distinct affini

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Zhang, Bo, Xuelin Zhong, Moira Sauane, Yihong Zhao, and Zhi-Liang Zheng. "Modulation of the Pol II CTD Phosphorylation Code by Rac1 and Cdc42 Small GTPases in Cultured Human Cancer Cells and Its Implication for Developing a Synthetic-Lethal Cancer Therapy." Cells 9, no. 3 (2020): 621. http://dx.doi.org/10.3390/cells9030621.

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Rho GTPases, including Rho, Cdc42, Rac and ROP subfamilies, are key signaling molecules in RNA polymerase II (Pol II) transcriptional control. Our prior work has shown that plant ROP and yeast Cdc42 GTPases similarly modulate Ser2 and Ser5 phosphorylation status of the C-terminal domain (CTD) of the Pol II largest subunit by regulating CTD phosphatase degradation. Here, we present genetic and pharmacological evidence showing that Cdc42 and Rac1 GTPase signaling modulates a similar CTD Ser2 and Ser5 phosphorylation code in cultured human cancer cells. While siRNA knockdown of Cdc42 and Rac1, re

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