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Related Concept Videos

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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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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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 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.
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The Ras Gene02:38

The Ras Gene

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The Ras-gene-encoded proteins are regulators of signaling pathways controlling cell proliferation, differentiation, or cell survival. The Ras-gene family in humans constitutes three primary members—the HRas, NRas, and KRas. These genes code for four functionally distinct yet closely related proteins—the HRas, NRas, KRas4A, and KRas4B. The involvement of mutant Ras genes in human cancer was first discovered in 1982 and is among the most common causes of human tumorigenesis.
Ras is a...
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Related Experiment Video

Updated: Oct 16, 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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Developmentally regulated GTPases: structure, function and roles in disease.

Christian A E Westrip1, Qinqin Zhuang1,2, Charlotte Hall1

  • 1Tumour Oxygenase Group, Institute of Cancer and Genomic Sciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK.

Cellular and Molecular Life Sciences : CMLS
|October 19, 2021
PubMed
Summary
This summary is machine-generated.

Developmentally regulated GTP-binding proteins (DRG1 and DRG2) and their partners (DFRP1 and DFRP2) regulate cell proliferation and translation. This review covers their structure, function, and roles in diseases like cancer.

Keywords:
GTPaseGir2Rbg1Rbg2RibosomeTma46Translation

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Last Updated: Oct 16, 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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Analyzing the Function of Small GTPases by Microinjection of Plasmids into Polarized Epithelial Cells
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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • GTPases are crucial for cellular processes.
  • The DRG subfamily (DRG1, DRG2) and their partners (DFRP1, DFRP2) regulate cell proliferation, translation, and microtubules.
  • Despite their importance, DRGs and DFRPs are poorly characterized.

Purpose of the Study:

  • To provide an overview of the structural biology and biochemistry of DRG GTPases.
  • To discuss the current understanding of DRGs and DFRPs in normal physiology.
  • To explore the emerging roles of DRGs and DFRPs in diseases, particularly cancer.

Main Methods:

  • Literature review
  • Structural biology analysis
  • Biochemical studies
  • Physiological and disease-related research

Main Results:

  • DRG1 and DRG2 interact with DFRP1 and DFRP2, respectively, preventing degradation.
  • These protein families are involved in cell growth control and translation.
  • Emerging evidence links DRGs and DFRPs to cancer development.

Conclusions:

  • DRG GTPases and their regulatory partners play significant roles in fundamental cellular processes.
  • Further research into their structure and function is crucial for understanding their involvement in diseases like cancer.