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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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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.
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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.
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GTPases and their Regulation02:14

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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.
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The Ras Gene02:38

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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.
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Updated: Mar 25, 2026

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells
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Small RAB GTPases Regulate Multiple Steps of Mitosis.

Stéphanie Miserey-Lenkei1, María I Colombo2

  • 1Institut Curie, PSL Research University, Molecular Mechanisms of Intracellular Transport Group, CNRS UMR 144 Paris, France.

Frontiers in Cell and Developmental Biology
|March 1, 2016
PubMed
Summary

RAB GTPases regulate membrane trafficking and mitosis. This review details how endosome-associated RABs function in early mitosis and cytokinesis, and how Golgi-associated RABs act during metaphase/anaphase and cytokinesis.

Keywords:
RABs GTPasesendosomesgolgi complexmitosistrafficking

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Membrane Trafficking

Background:

  • RAB GTPases are crucial regulators of membrane trafficking.
  • Several RAB GTPase family members play roles in cell division (mitosis).

Purpose of the Study:

  • To review the function of RAB GTPases in mitosis.
  • To highlight the roles of endosome-associated and Golgi-associated RAB GTPases in cell division.

Main Methods:

  • Literature review of studies on RAB GTPases and mitosis.
  • Focus on endosomal and Golgi compartments.

Main Results:

  • Endosome-associated RAB GTPases are involved in early mitosis, spindle pole maturation, and cytokinesis.
  • Golgi-associated RAB GTPases are implicated in the metaphase/anaphase transition and cytokinesis.

Conclusions:

  • RAB GTPases are essential for multiple stages of mitosis and cytokinesis.
  • Distinct RAB GTPase populations in endosomes and Golgi contribute to cell division processes.