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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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Rab Proteins01:14

Rab Proteins

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Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
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Rab Cascades01:25

Rab Cascades

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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.
2.6K
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

7.2K
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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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: Jul 4, 2025

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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Atypical RhoUV GTPases in development and disease.

Stephanie Woo1,2, Leesa Strasser1,2

  • 1Department of Molecular Cell Biology, University of California, Merced, CA, U.S.A.

Biochemical Society Transactions
|February 5, 2024
PubMed
Summary
This summary is machine-generated.

RhoU and RhoV GTPases are atypical regulators of the cytoskeleton, cell adhesion, and migration. This review explores their specialized functions in embryonic development and disease, including cancer metastasis.

Keywords:
EMTRho GTPasesRhoURhoVcancerembryogenesis

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RhoC GTPase Activation Assay
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Affinity Precipitation of Active Rho-GEFs Using a GST-tagged Mutant Rho Protein GST-RhoAG17A from Epithelial Cell Lysates
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Affinity Precipitation of Active Rho-GEFs Using a GST-tagged Mutant Rho Protein GST-RhoAG17A from Epithelial Cell Lysates

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Related Experiment Videos

Last Updated: Jul 4, 2025

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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Affinity Precipitation of Active Rho-GEFs Using a GST-tagged Mutant Rho Protein GST-RhoAG17A from Epithelial Cell Lysates
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Affinity Precipitation of Active Rho-GEFs Using a GST-tagged Mutant Rho Protein GST-RhoAG17A from Epithelial Cell Lysates

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Developmental Biology

Background:

  • RhoU and RhoV form a distinct subfamily within the Rho GTPase family.
  • These GTPases are atypical due to unique GTP/GDP binding kinetics and terminal modifications.
  • They are implicated in cytoskeletal dynamics, cell adhesion, and migration.

Approach:

  • This review synthesizes current research on RhoU and RhoV functions.
  • It focuses on their roles in embryonic development and organogenesis.
  • The review also examines their involvement in disease processes, particularly cancer metastasis.

Key Points:

  • RhoU and RhoV exhibit distinct expression patterns during embryonic development.
  • Their unique structural features influence subcellular localization and activity.
  • Dysregulation of RhoU and RhoV is linked to developmental abnormalities and cancer progression.

Conclusions:

  • RhoU and RhoV possess specialized functions critical for normal development.
  • Understanding their roles in disease pathogenesis may offer therapeutic targets.
  • Further research is needed to fully elucidate their complex regulatory mechanisms.