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Related Concept Videos

Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

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Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
Three regulatory proteins control their activity:
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GTPases and their Regulation02:14

GTPases and their Regulation

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Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒  small G-proteins consisting of a single domain and large multi-domain G-proteins.
Large G-proteins,...
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GTPases and their Regulation02:14

GTPases and their Regulation

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Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

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Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high...
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Rab Cascades01:25

Rab Cascades

3.6K
Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
3.6K
Cell Polarization by Rho Proteins01:21

Cell Polarization by Rho Proteins

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Cell polarity is the asymmetric distribution of cellular and membrane components, making one side of the cell different from the other. This polarity is essential to many processes such as embryogenesis, axon migration, glucose transport across epithelial cells, and directional cell migration. A migrating cell responds to intracellular or extracellular signals via molecular cascades that reorganize the actin cytoskeleton to establish this polarity. In these cells, the Rho family proteins Cdc42,...
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Related Experiment Video

Updated: Feb 18, 2026

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells
10:27

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells

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Fast-cycling Rho GTPases.

Pontus Aspenström1

  • 1Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Nobels väg 16 , Box 280, SE, Stockholm, Sweden.

Small Gtpases
|November 22, 2017
PubMed
Summary

Atypical Rho GTPases, unlike classical ones, exhibit unique GDP/GTP exchange kinetics. This review details

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Biochemistry

Background:

  • Rho GTPases are key regulators of cell functions.
  • Traditionally, they were thought to follow a simple GDP/GTP cycle.
  • However, many Rho GTPases exhibit atypical behavior.

Purpose of the Study:

  • To review atypical Rho GTPases with fast-cycling properties.
  • To describe their regulatory mechanisms.
  • To explore their role in human diseases.

Main Methods:

  • Literature review of Rho GTPase research.
  • Analysis of kinetic properties of Rho GTPase subfamily members.
  • Synthesis of findings on atypical Rho GTPase regulation and function.
Keywords:
Atypical Rho GTPasesRhoDRhoUactincell migrationstress fibers

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Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
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Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay

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RhoC GTPase Activation Assay
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RhoC GTPase Activation Assay

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Related Experiment Videos

Last Updated: Feb 18, 2026

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells
10:27

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells

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Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
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Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay

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RhoC GTPase Activation Assay
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Main Results:

  • At least 10 of the 20 Rho GTPases are atypical.
  • Atypical Rho GTPases include those that do not hydrolyze GTP or have enhanced GDP/GTP exchange.
  • This review focuses on the 'fast-cycling' Rho GTPases.

Conclusions:

  • Fast-cycling Rho GTPases represent a distinct functional class.
  • Understanding their regulation is crucial.
  • Dysregulation of atypical Rho GTPases is implicated in human pathologies.