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Rab13 Traffics on Vesicles Independent of Prenylation.

Maria S Ioannou1, Martine Girard1, Peter S McPherson2

  • 1From the Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada.

The Journal of Biological Chemistry
|March 13, 2016
PubMed
Summary

Inactive Rab13 associates with vesicles via protein interactions, not prenylation. Upon activation, Rab13 binds the plasma membrane, challenging the canonical model of Rab GTPase membrane trafficking.

Keywords:
DENN domainDENND2BGDIGDP dissociation inhibitorRabTI-VAMPendosomeguanine nucleotide exchange factor (GEF)protein isoprenylationvesicles

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Membrane Trafficking

Background:

  • Rab GTPases regulate intracellular membrane trafficking.
  • Typically, inactive GDP-bound Rabs are soluble, and active GTP-bound Rabs are membrane-associated via C-terminal prenylation.

Purpose of the Study:

  • To investigate the membrane association mechanism of Rab13.
  • To determine if C-terminal prenylation is essential for Rab13 vesicle association and trafficking.

Main Methods:

  • Investigated Rab13's interaction with vesicles and plasma membrane.
  • Analyzed the role of C-terminal prenylation in Rab13 localization and function.

Main Results:

  • Rab13 associates with vesicles in its inactive state independently of C-terminal prenylation.
  • Inactive Rab13 utilizes protein-protein interactions for vesicle association.
  • Activation leads to Rab13 association with the plasma membrane, likely involving prenyl group insertion.

Conclusions:

  • C-terminal prenylation is not required for Rab13 vesicle association.
  • Rab13 employs a distinct mechanism for membrane trafficking compared to the canonical Rab GTPase model.
  • Protein-protein interactions mediate inactive Rab13's association with vesicles.