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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

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Rab Cascades01:25

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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 Proteins01:14

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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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The early endosome containing internalized molecules matures through transformations in its location, morphology, intraluminal pH, and membrane protein composition. Together, these changes result in a more acidic late endosome that contains multiple intraluminal vesicles; therefore, the late endosome is also called a multivesicular body (MVB).
Changes in location
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Gap Junctions

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Multicellular organisms employ a variety of ways for cells to communicate with each other. Gap junctions are specialized proteins that form pores between neighboring cells in animals, connecting the cytoplasm between the two, and allowing for the exchange of molecules and ions. They are found in a wide range of invertebrate and vertebrate species, mediate numerous functions including cell differentiation and development, and are associated with numerous human diseases, including cardiac and...
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Related Experiment Video

Updated: Feb 16, 2026

In Vitro Polymerization of F-actin on Early Endosomes
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Vps34 and the Armus/TBC-2 Rab GAPs: Putting the brakes on the endosomal Rab5 and Rab7 GTPases.

Fiona Law1,2, Christian E Rocheleau1,2

  • 1Division of Endocrinology and Metabolism, Department of Medicine and the Department of Anatomy and Cell Biology, McGill University, Montreal, Quebec, Canada.

Cellular Logistics
|January 4, 2018
PubMed
Summary

The phosphoinositide 3-kinase Vps34 inactivates Rab5 and Rab7 GTPases, crucial for endosome maturation. This discovery clarifies Vps34

Keywords:
GTPasesRab5Rab7endosome maturationlysosome fusionmembrane trafficking

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Endocytosis and Lysosome Biology

Background:

  • Rab5 and Rab7 GTPases regulate endosome maturation and fusion with lysosomes.
  • These GTPases activate Vps34, a class III phosphoinositide 3-kinase, to produce phosphatidylinositol-3 phosphate [PI(3)P] on endosomes.
  • PI(3)P and GTP-bound Rabs recruit regulators for endosome maturation and lysosome fusion.

Purpose of the Study:

  • To investigate the counterintuitive observation that Vps34 loss leads to enlarged endosomes.
  • To elucidate the precise role of Vps34 in regulating Rab GTPase activity.
  • To understand the mechanism by which Vps34 influences endosome maturation.

Main Methods:

  • Analysis of endosome morphology in Vps34-deficient cells.
  • Investigating the interaction between Vps34 and Rab GTPase Activating Proteins (GAPs).
  • Studying the recruitment of TBC1D2 family GAPs by Vps34.

Main Results:

  • Loss of Vps34 function results in enlarged endosomes, similar to phenotypes observed with activated Rab GTPases.
  • Vps34 actively recruits TBC1D2 family Rab GTPase Activating Proteins (GAPs).
  • This recruitment by Vps34 serves to inactivate Rab5 and Rab7 GTPases.

Conclusions:

  • Vps34 has a critical function in negatively regulating Rab5 and Rab7 GTPase activity.
  • Vps34 inactivates Rab5 and Rab7 through the recruitment of TBC1D2 family GAPs.
  • This mechanism is essential for proper endosome maturation and lysosome fusion, explaining the enlarged endosome phenotype upon Vps34 loss.