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Journal articles on the topic 'GTPasas'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Baldiris-Avila, Rosa, Natali Acosta, Andrea Arzuza-Romero, and Ricardo Vivas-Reyes. "Red de interacción proteína-proteína de fosfatidilinositol 4,5-bifosfato 5-fosfatasa relacionada con el síndrome de Lowe." Revista de la Academia Colombiana de Ciencias Exactas, Físicas y Naturales 40, no. 157 (2016): 559. http://dx.doi.org/10.18257/raccefyn.381.

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<p>El síndrome de Lowe (SL) es una enfermedad transmitida por herencia ligada al sexo, que afecta mayoritariamente a los hombres y muy ocasionalmente a las mujeres. El SL consiste en mutaciones en el gen OCRL1 que afectan el metabolismo del inositol fosfato, produciendo afecciones significativas de los ojos, el sistema nervioso y los riñones. En este estudio se construyó una red de interacción proteína-proteína para la enzima fosfatidilinositol 4,5-bifosfato 5-fosfatasa, en el software Cytoscape versión 3.3.0, a partir de información suministrada por las bases de datos KEGG, PubMed, BioG

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2

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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Nur-E-Kamal, M. S., and H. Maruta. "The role of Gln61 and Glu63 of Ras GTPases in their activation by NF1 and Ras GAP." Molecular Biology of the Cell 3, no. 12 (1992): 1437–42. http://dx.doi.org/10.1091/mbc.3.12.1437.

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Two distinct GAPs of 120 and 235 kDa called GAP1 and NF1 serve as attenuators of Ras, a member of GTP-dependent signal transducers, by stimulating its intrinsic guanosine triphosphatase (GTPase) activity. The GAP1 (also called Ras GAP) is highly specific for Ras and does not stimulate the intrinsic GTPase activity of Rap1 or Rho. Using GAP1C, the C-terminal GTPase activating domain (residues 720-1044) of bovine GAP1, we have shown previously that the GAP1 specificity is determined by the Ras domain (residues 61-65) where Gln61 plays the primary role. The corresponding domain (residues 1175-153

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4

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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5

Kötting, Carsten, and Klaus Gerwert. "What vibrations tell us about GTPases." Biological Chemistry 396, no. 2 (2015): 131–44. http://dx.doi.org/10.1515/hsz-2014-0219.

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Abstract In this review, we discuss how time-resolved Fourier transform infrared (FTIR) spectroscopy is used to understand how GTP hydrolysis is catalyzed by small GTPases and their cognate GTPase-activating proteins (GAPs). By interaction with small GTPases, GAPs regulate important signal transduction pathways and transport mechanisms in cells. The GTPase reaction terminates signaling and controls transport. Dysfunctions of GTP hydrolysis in these proteins are linked to serious diseases including cancer. Using FTIR, we resolved both the intrinsic and GAP-catalyzed GTPase reaction of the small

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Kesseler, Christoph, Julian Kahr, Natalie Waldt, et al. "EXTH-64. SMALL GTPASES IN MENINGIOMAS: PROLIFERATION, MIGRATION, SURVIVAL, POTENTIAL TREATMENT AND INTERACTIONS." Neuro-Oncology 22, Supplement_2 (2020): ii101. http://dx.doi.org/10.1093/neuonc/noaa215.418.

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Abstract PURPOSE To evaluate the role of the small GTPases RhoA, Rac1 and Cdc42 in meningiomas as therapeutic targets and their interactions in meningiomas. EXPERIMENTAL DESIGN We analyzed expression of GTPases in human meningioma samples and meningioma cell lines of various WHO grades. Malignant IOMM-Lee meningioma cells were used to generate shRNA mediated knockdowns of GTPases RhoA, Rac1 or Cdc42 and to study knockdown effects on proliferation and migration, as well as analysis of cell morphology by confocal microscopy. The same tests were used to investigate effects of the two inhibitors F

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7

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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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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Shah, Bhavin, and Andreas W. Püschel. "Regulation of Rap GTPases in mammalian neurons." Biological Chemistry 397, no. 10 (2016): 1055–69. http://dx.doi.org/10.1515/hsz-2016-0165.

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Abstract Small GTPases are central regulators of many cellular processes. The highly conserved Rap GTPases perform essential functions in the mammalian nervous system during development and in mature neurons. During neocortical development, Rap1 is required to regulate cadherin- and integrin-mediated adhesion. In the adult nervous system Rap1 and Rap2 regulate the maturation and plasticity of dendritic spine and synapses. Although genetic studies have revealed important roles of Rap GTPases in neurons, their regulation by guanine nucleotide exchange factors (GEFs) that activate them and GTPase

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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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Anderson, Erik L., and Michael J. Hamann. "Detection of Rho GEF and GAP activity through a sensitive split luciferase assay system." Biochemical Journal 441, no. 3 (2012): 869–80. http://dx.doi.org/10.1042/bj20111111.

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Rho GTPases regulate the assembly of cellular actin structures and are activated by GEFs (guanine-nucleotide-exchange factors) and rendered inactive by GAPs (GTPase-activating proteins). Using the Rho GTPases Cdc42, Rac1 and RhoA, and the GTPase-binding portions of the effector proteins p21-activated kinase and Rhophilin1, we have developed split luciferase assays for detecting both GEF and GAP regulation of these GTPases. The system relies on purifying split luciferase fusion proteins of the GTPases and effectors from bacteria, and our results show that the assays replicate GEF and GAP specif

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Pai, Sung-Yun, Chaekyun Kim, and David A. Williams. "Rac GTPases in Human Diseases." Disease Markers 29, no. 3-4 (2010): 177–87. http://dx.doi.org/10.1155/2010/380291.

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Rho GTPases are members of the Ras superfamily of GTPases that regulate a wide variety of cellular functions. While Rho GTPase pathways have been implicated in various pathological conditions in humans, to date coding mutations in only the hematopoietic specific GTPase,RAC2, have been found to cause a human disease, a severe phagocytic immunodeficiency characterized by life-threatening infections in infancy. Interestingly, the phenotype was predicted by a mouse knock-out ofRAC2and resembles leukocyte adhesion deficiency (LAD). Here we review Rho GTPases with a specific focus on Rac GTPases. In

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Peurois, François, Gérald Peyroche, and Jacqueline Cherfils. "Small GTPase peripheral binding to membranes: molecular determinants and supramolecular organization." Biochemical Society Transactions 47, no. 1 (2018): 13–22. http://dx.doi.org/10.1042/bst20170525.

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AbstractSmall GTPases regulate many aspects of cell logistics by alternating between an inactive, GDP-bound form and an active, GTP-bound form. This nucleotide switch is coupled to a cytosol/membrane cycle, such that GTP-bound small GTPases carry out their functions at the periphery of endomembranes. A global understanding of the molecular determinants of the interaction of small GTPases with membranes and of the resulting supramolecular organization is beginning to emerge from studies of model systems. Recent studies highlighted that small GTPases establish multiple interactions with membrane

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Tsukuba, Takayuki, Yu Yamaguchi, and Tomoko Kadowaki. "Large Rab GTPases: Novel Membrane Trafficking Regulators with a Calcium Sensor and Functional Domains." International Journal of Molecular Sciences 22, no. 14 (2021): 7691. http://dx.doi.org/10.3390/ijms22147691.

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Rab GTPases are major coordinators of intracellular membrane trafficking, including vesicle transport, membrane fission, tethering, docking, and fusion events. Rab GTPases are roughly divided into two groups: conventional “small” Rab GTPases and atypical “large” Rab GTPases that have been recently reported. Some members of large Rab GTPases in mammals include Rab44, Rab45/RASEF, and Rab46. The genes of these large Rab GTPases commonly encode an amino-terminal EF-hand domain, coiled-coil domain, and the carboxyl-terminal Rab GTPase domain. A common feature of large Rab GTPases is that they expr

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Humphries, Brock A., Zhishan Wang, and Chengfeng Yang. "MicroRNA Regulation of the Small Rho GTPase Regulators—Complexities and Opportunities in Targeting Cancer Metastasis." Cancers 12, no. 5 (2020): 1092. http://dx.doi.org/10.3390/cancers12051092.

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The small Rho GTPases regulate important cellular processes that affect cancer metastasis, such as cell survival and proliferation, actin dynamics, adhesion, migration, invasion and transcriptional activation. The Rho GTPases function as molecular switches cycling between an active GTP-bound and inactive guanosine diphosphate (GDP)-bound conformation. It is known that Rho GTPase activities are mainly regulated by guanine nucleotide exchange factors (RhoGEFs), GTPase-activating proteins (RhoGAPs), GDP dissociation inhibitors (RhoGDIs) and guanine nucleotide exchange modifiers (GEMs). These Rho

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Cherfils, Jacqueline, and Mahel Zeghouf. "Regulation of Small GTPases by GEFs, GAPs, and GDIs." Physiological Reviews 93, no. 1 (2013): 269–309. http://dx.doi.org/10.1152/physrev.00003.2012.

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Small GTPases use GDP/GTP alternation to actuate a variety of functional switches that are pivotal for cell dynamics. The GTPase switch is turned on by GEFs, which stimulate dissociation of the tightly bound GDP, and turned off by GAPs, which accelerate the intrinsically sluggish hydrolysis of GTP. For Ras, Rho, and Rab GTPases, this switch incorporates a membrane/cytosol alternation regulated by GDIs and GDI-like proteins. The structures and core mechanisms of representative members of small GTPase regulators from most families have now been elucidated, illuminating their general traits combi

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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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Zhu, Min, and Xiu-qi Wang. "Regulation of mTORC1 by Small GTPases in Response to Nutrients." Journal of Nutrition 150, no. 5 (2020): 1004–11. http://dx.doi.org/10.1093/jn/nxz301.

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ABSTRACT Mechanistic target of rapamycin complex 1 (mTORC1) is a highly evolutionarily conserved serine/threonine kinase that regulates cell growth and metabolism in response to multiple environmental cues, such as nutrients, hormones, energy, and stress. Deregulation of mTORC1 can lead to diseases such as diabetes, obesity, and cancer. A series of small GTPases, including Rag, Ras homolog enriched in brain (Rheb), adenosine diphosphate ribosylation factor 1 (Arf1), Ras-related protein Ral-A, Ras homolog (Rho), and Rab, are involved in regulating mTORC1 in response to nutrients, and mTORC1 is

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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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Jiang, Shu-Ye, and Srinivasan Ramachandran. "Comparative and evolutionary analysis of genes encoding small GTPases and their activating proteins in eukaryotic genomes." Physiological Genomics 24, no. 3 (2006): 235–51. http://dx.doi.org/10.1152/physiolgenomics.00210.2005.

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Both small GTPase and its activating protein (GAP) superfamilies exist in various eukaryotes. The small GTPases regulate a wide variety of cellular processes by cycling between active GTP- and inactive GAP-bound conformations. The GAPs promote GTPase inactivation by stimulating the GTP hydrolysis. In this study, we identified 111 small GTPases and 85 GAPs in rice, 65 GAPs in Arabidopsis, 90 small GTPases in Drosophila melanogaster, and 35 GAPs in Saccharomyces cerevisiaeby genome-wide analysis. We then analyzed and compared a total of 498 small GTPases and 422 GAPs from these four eukaryotic a

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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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deCathelineau, Aimee M., and Gary M. Bokoch. "Inactivation of Rho GTPases by Statins Attenuates Anthrax Lethal Toxin Activity." Infection and Immunity 77, no. 1 (2008): 348–59. http://dx.doi.org/10.1128/iai.01005-08.

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ABSTRACT Anthrax lethal factor (LF), secreted by Bacillus anthracis, interacts with protective antigen to form a bipartite toxin (lethal toxin [LT]) that exerts pleiotropic biological effects resulting in subversion of the innate immune response. Although the mitogen-activated protein kinase kinases (MKKs) are the major intracellular protein targets of LF, the pathology induced by LT is not well understood. The statin family of HMG-coenzyme A reductase inhibitors have potent anti-inflammatory effects independent of their cholesterol-lowering properties, which have been attributed to modulation

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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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Goryachev, Andrew B., and Marcin Leda. "Autoactivation of small GTPases by the GEF–effector positive feedback modules." F1000Research 8 (September 23, 2019): 1676. http://dx.doi.org/10.12688/f1000research.20003.1.

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Small GTPases are organizers of a plethora of cellular processes. The time and place of their activation are tightly controlled by the localization and activation of their regulators, guanine-nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs). Remarkably, in some systems, the upstream regulators of GTPases are also found downstream of their activity. Resulting feedback loops can generate complex spatiotemporal dynamics of GTPases with important functional consequences. Here we discuss the concept of positive autoregulation of small GTPases by the GEF–effector feedback mod

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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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Humphries, Brock, Zhishan Wang, and Chengfeng Yang. "Rho GTPases: Big Players in Breast Cancer Initiation, Metastasis and Therapeutic Responses." Cells 9, no. 10 (2020): 2167. http://dx.doi.org/10.3390/cells9102167.

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Rho GTPases, a family of the Ras GTPase superfamily, are key regulators of the actin cytoskeleton. They were originally thought to primarily affect cell migration and invasion; however, recent advances in our understanding of the biology and function of Rho GTPases have demonstrated their diverse roles within the cell, including membrane trafficking, gene transcription, migration, invasion, adhesion, survival and growth. As these processes are critically involved in cancer initiation, metastasis and therapeutic responses, it is not surprising that studies have demonstrated important roles of R

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Thapliyal, Ashish, Rashmi Verma, and Navin Kumar. "Small G Proteins Dexras1 and RHES and Their Role in Pathophysiological Processes." International Journal of Cell Biology 2014 (2014): 1–10. http://dx.doi.org/10.1155/2014/308535.

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Dexras1 and RHES, monomeric G proteins, are members of small GTPase family that are involved in modulation of pathophysiological processes. Dexras1 and RHES levels are modulated by hormones and Dexras1 expression undergoes circadian fluctuations. Both these GTPases are capable of modulating calcium ion channels which in turn can potentially modulate neurosecretion/hormonal release. These two GTPases have been reported to prevent the aberrant cell growth and induce apoptosis in cell lines. Present review focuses on role of these two monomeric GTPases and summarizes their role in pathophysiologi

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Charest, Pascale G., and Richard A. Firtel. "Big roles for small GTPases in the control of directed cell movement." Biochemical Journal 401, no. 2 (2006): 377–90. http://dx.doi.org/10.1042/bj20061432.

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Small GTPases are involved in the control of diverse cellular behaviours, including cellular growth, differentiation and motility. In addition, recent studies have revealed new roles for small GTPases in the regulation of eukaryotic chemotaxis. Efficient chemotaxis results from co-ordinated chemoattractant gradient sensing, cell polarization and cellular motility, and accumulating data suggest that small GTPase signalling plays a central role in each of these processes as well as in signal relay. The present review summarizes these recent findings, which shed light on the molecular mechanisms

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Peterson, J., Y. Zheng, L. Bender, A. Myers, R. Cerione, and A. Bender. "Interactions between the bud emergence proteins Bem1p and Bem2p and Rho-type GTPases in yeast." Journal of Cell Biology 127, no. 5 (1994): 1395–406. http://dx.doi.org/10.1083/jcb.127.5.1395.

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The SH3 domain-containing protein Bem1p is needed for normal bud emergence and mating projection formation, two processes that require asymmetric reorganizations of the cortical cytoskeleton in Saccharomyces cerevisiae. To identify proteins that functionally and/or physically interact with Bem1p, we screened for mutations that display synthetic lethality with a mutant allele of the BEM1 gene and for genes whose products display two-hybrid interactions with the Bem1 protein. CDC24, which is required for bud emergence and encodes a GEF (guanine-nucleotide exchange factor) for the essential Rho-t

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Bruewer, Matthias, Ann M. Hopkins, Michael E. Hobert, Asma Nusrat, and James L. Madara. "RhoA, Rac1, and Cdc42 exert distinct effects on epithelial barrier via selective structural and biochemical modulation of junctional proteins and F-actin." American Journal of Physiology-Cell Physiology 287, no. 2 (2004): C327—C335. http://dx.doi.org/10.1152/ajpcell.00087.2004.

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Epithelial intercellular junctions regulate cell-cell contact and mucosal barrier function. Both tight junctions (TJs) and adherens junctions (AJs) are regulated in part by their affiliation with the F-actin cytoskeleton. The cytoskeleton in turn is influenced by Rho family small GTPases such as RhoA, Rac1, and Cdc42, all of which constitute eukaryotic targets for several pathogenic organisms. With a tetracycline-repressible system to achieve regulated expression in Madin-Darby canine kidney (MDCK) epithelial cells, we used dominant-negative (DN) and constitutively active (CA) forms of RhoA, R

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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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Kim, MinJung, Tami J. Kingsbury, Wen-Chih Cheng, et al. "RAB14 and RAB5 Gtpases Regulate Human Erythropoiesis, Potentially Via Opposing Roles in Endosomal Recycling." Blood 126, no. 23 (2015): 937. http://dx.doi.org/10.1182/blood.v126.23.937.937.

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Abstract Previously, we reported that the erythroid-expressed miRs, miR-144 and miR-451, target the RAB14 GTPase during human erythropoiesis in the human TF1 erythropoietic model cell line and in primary CD34+ hematopoietic stem-progenitor cells. In response to erythropoietin, endogenous RAB14 levels decreased during erythropoiesis, and RAB14 knockdown increased the numbers of erythroid (CD34- CD71hi CD235ahi) cells, increased b-hemoglobin expression, and decreased ETO2 expression (Kim, BJH, 2015). Taken together, our findings revealed that RAB14 functions as a physiologic inhibitor of human e

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Héraud, Pinault, Lagrée, and Moreau. "p190RhoGAPs, the ARHGAP35- and ARHGAP5-Encoded Proteins, in Health and Disease." Cells 8, no. 4 (2019): 351. http://dx.doi.org/10.3390/cells8040351.

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Small guanosine triphosphatases (GTPases) gathered in the Rat sarcoma (Ras) superfamily represent a large family of proteins involved in several key cellular mechanisms. Within the Ras superfamily, the Ras homolog (Rho) family is specialized in the regulation of actin cytoskeleton-based mechanisms. These proteins switch between an active and an inactive state, resulting in subsequent inhibiting or activating downstream signals, leading finally to regulation of actin-based processes. The On/Off status of Rho GTPases implicates two subsets of regulators: GEFs (guanine nucleotide exchange factors

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Reichman, Melvin, Amanda Schabdach, Meera Kumar, et al. "A High-Throughput Assay for Rho Guanine Nucleotide Exchange Factors Based on the Transcreener GDP Assay." Journal of Biomolecular Screening 20, no. 10 (2015): 1294–99. http://dx.doi.org/10.1177/1087057115596326.

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Ras homologous (Rho) family GTPases act as molecular switches controlling cell growth, movement, and gene expression by cycling between inactive guanosine diphosphate (GDP)- and active guanosine triphosphate (GTP)-bound conformations. Guanine nucleotide exchange factors (GEFs) positively regulate Rho GTPases by accelerating GDP dissociation to allow formation of the active, GTP-bound complex. Rho proteins are directly involved in cancer pathways, especially cell migration and invasion, and inhibiting GEFs holds potential as a therapeutic strategy to diminish Rho-dependent oncogenesis. Methods

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Møller, Lisbeth Liliendal Valbjørn, Amira Klip, and Lykke Sylow. "Rho GTPases—Emerging Regulators of Glucose Homeostasis and Metabolic Health." Cells 8, no. 5 (2019): 434. http://dx.doi.org/10.3390/cells8050434.

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Rho guanosine triphosphatases (GTPases) are key regulators in a number of cellular functions, including actin cytoskeleton remodeling and vesicle traffic. Traditionally, Rho GTPases are studied because of their function in cell migration and cancer, while their roles in metabolism are less documented. However, emerging evidence implicates Rho GTPases as regulators of processes of crucial importance for maintaining metabolic homeostasis. Thus, the time is now ripe for reviewing Rho GTPases in the context of metabolic health. Rho GTPase-mediated key processes include the release of insulin from

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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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Taymans, Jean-Marc. "The GTPase function of LRRK2." Biochemical Society Transactions 40, no. 5 (2012): 1063–69. http://dx.doi.org/10.1042/bst20120133.

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LRRK2 (leucine-rich repeat kinase 2) is a large protein encoding multiple functional domains, including two catalytically active domains, a kinase and a GTPase domain. The LRRK2 GTPase belongs to the Ras-GTPase superfamily of GTPases, more specifically to the ROC (Ras of complex proteins) subfamily. Studies with recombinant LRRK2 protein purified from eukaryotic cells have confirmed that LRRK2 binds guanine nucleotides and catalyses the hydrolysis of GTP to GDP. LRRK2 is linked to PD (Parkinson's disease) and GTPase activity is impaired for several PD mutants located in the ROC and COR (C-term

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Voss, Stephanie, Dennis M. Krüger, Oliver Koch, and Yao-Wen Wu. "Spatiotemporal imaging of small GTPases activity in live cells." Proceedings of the National Academy of Sciences 113, no. 50 (2016): 14348–53. http://dx.doi.org/10.1073/pnas.1613999113.

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Ras-like small GTPases function as molecular switches and regulate diverse cellular events. To examine the dynamics of signaling requires spatiotemporal visualization of their activity in the cell. Current small GTPase sensors rely on specific effector domains that are available for only a small number of GTPases and compete for endogenous regulator/effector binding. Here, we describe versatile conformational sensors for GTPase activity (COSGAs) based on the conserved GTPase fold. Conformational changes upon GDP/GTP exchange were directly observed in solution, on beads, and in live cells by Fö

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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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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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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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Aspenström, Pontus. "The Intrinsic GDP/GTP Exchange Activities of Cdc42 and Rac1 Are Critical Determinants for Their Specific Effects on Mobilization of the Actin Filament System." Cells 8, no. 7 (2019): 759. http://dx.doi.org/10.3390/cells8070759.

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The Rho GTPases comprise a subfamily of the Ras superfamily of small GTPases. Their importance in regulation of cell morphology and cell migration is well characterized. According to the prevailing paradigm, Cdc42 regulates the formation of filopodia, Rac1 regulates the formation of lamellipodia, and RhoA triggers the assembly of focal adhesions. However, this scheme is clearly an oversimplification, as the Rho subfamily encompasses 20 members with diverse effects on a number of vital cellular processes, including cytoskeletal dynamics and cell proliferation, migration, and invasion. This arti

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Pfeffer, Suzanne R. "Rab GTPases: master regulators that establish the secretory and endocytic pathways." Molecular Biology of the Cell 28, no. 6 (2017): 712–15. http://dx.doi.org/10.1091/mbc.e16-10-0737.

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Several of the most important discoveries in the field of membrane traffic have come from studies of Rab GTPases by Marino Zerial and Peter Novick and their colleagues. Zerial was the first to discover that Rab GTPases represent identity markers for different membrane-bound compartments, and each Rab organizes a collection of specific effectors into function-specifying membrane microdomains to carry out receptor trafficking. Novick discovered that the order (and thus polarity) of Rab GTPases along the secretory and endocytic pathways are established by their specific, cognate guanine nucleotid

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Dovas, Athanassios, and John R. Couchman. "RhoGDI: multiple functions in the regulation of Rho family GTPase activities." Biochemical Journal 390, no. 1 (2005): 1–9. http://dx.doi.org/10.1042/bj20050104.

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RhoGDI (Rho GDP-dissociation inhibitor) was identified as a down-regulator of Rho family GTPases typified by its ability to prevent nucleotide exchange and membrane association. Structural studies on GTPase–RhoGDI complexes, in combination with biochemical and cell biological results, have provided insight as to how RhoGDI exerts its effects on nucleotide binding, the membrane association–dissociation cycling of the GTPase and how these activities are controlled. Despite the initial negative roles attributed to RhoGDI, recent evidence has come to suggest that it may also act as a positive regu

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Kumar Srivastava, Vijay, Mintu Chandra, and Sunando Datta. "Crystallization and preliminary X-ray analysis of RabX3, a tandem GTPase fromEntamoeba histolytica." Acta Crystallographica Section F Structural Biology Communications 70, no. 7 (2014): 933–37. http://dx.doi.org/10.1107/s2053230x14011388.

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Ras superfamily GTPases regulate signalling pathways that control multiple biological processes by modulating the GTP/GDP cycle. Various Rab GTPases, which are the key regulators of vesicular trafficking pathways, play a vital role in the survival and virulence of the enteric parasiteEntamoeba histolytica. The Rab GTPases act as binary molecular switches that utilize the conformational changes associated with the GTP/GDP cycle to elicit responses from target proteins and thereby regulate a broad spectrum of cellular processes including cell proliferation, cytoskeletal assembly, nuclear transpo

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Cortes, Claudio, Kimberly A. Rzomp, Amy Tvinnereim, Marci A. Scidmore, and Benjamin Wizel. "Chlamydia pneumoniae Inclusion Membrane Protein Cpn0585 Interacts with Multiple Rab GTPases." Infection and Immunity 75, no. 12 (2007): 5586–96. http://dx.doi.org/10.1128/iai.01020-07.

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ABSTRACT Chlamydiae are intracellular bacteria that develop within a membrane-bound vacuole called an inclusion. To ensure that the inclusion is a safe niche for chlamydial replication, chlamydiae exploit a number of host cell processes, including membrane-trafficking pathways. Recently, several Rab GTPases were found to associate with the inclusions of various chlamydial species. Here we report that Cpn0585, a Chlamydia pneumoniae inclusion membrane protein (Inc), interacts with multiple Rab GTPases. The results from yeast two-hybrid experiments revealed that an amino-terminally truncated for

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Beckers, Cora, Victor van Hinsbergh, and Geerten van Nieuw Amerongen. "Driving Rho GTPase activity in endothelial cells regulates barrier integrity." Thrombosis and Haemostasis 103, no. 01 (2010): 40–55. http://dx.doi.org/10.1160/th09-06-0403.

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SummaryIn the past decade understanding of the role of the Rho GTPases RhoA, Rac1 and Cdc42 has been developed from regulatory proteins that regulate specific actin cytoskeletal structures – stress fibers, lamellipodia and filopodia – to complex integrators of cytoskeletal structures that can exert multiple functions depending on the cellular context. Fundamental to these functions are three-dimensional complexes between the individual Rho GTPases, their specific activators (GEFs) and inhibitors (GDIs and GAPs), which greatly outnumber the Rho GTPases themselves, and additional regulatory prot

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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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Rogg, Manuel, Jasmin I. Maier, Robert Dotzauer, et al. "SRGAP1 Controls Small Rho GTPases To Regulate Podocyte Foot Process Maintenance." Journal of the American Society of Nephrology 32, no. 3 (2021): 563–79. http://dx.doi.org/10.1681/asn.2020081126.

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BackgroundPrevious research demonstrated that small Rho GTPases, modulators of the actin cytoskeleton, are drivers of podocyte foot-process effacement in glomerular diseases, such as FSGS. However, a comprehensive understanding of the regulatory networks of small Rho GTPases in podocytes is lacking.MethodsWe conducted an analysis of podocyte transcriptome and proteome datasets for Rho GTPases; mapped in vivo, podocyte-specific Rho GTPase affinity networks; and examined conditional knockout mice and murine disease models targeting Srgap1. To evaluate podocyte foot-process morphology, we used su

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Blombach, Fabian, Stan J. J. Brouns, and John van der Oost. "Assembling the archaeal ribosome: roles for translation-factor-related GTPases." Biochemical Society Transactions 39, no. 1 (2011): 45–50. http://dx.doi.org/10.1042/bst0390045.

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The assembly of ribosomal subunits from their individual components (rRNA and ribosomal proteins) requires the assistance of a multitude of factors in order to control and increase the efficiency of the assembly process. GTPases of the TRAFAC (translation-factor-related) class constitute a major type of ribosome-assembly factor in Eukaryota and Bacteria. They are thought to aid the stepwise assembly of ribosomal subunits through a ‘molecular switch’ mechanism that involves conformational changes in response to GTP hydrolysis. Most conserved TRAFAC GTPases are involved in ribosome assembly or o

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