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PMID: 16882731 Published · ppublish English Journal Article Review

Rabs and their effectors: achieving specificity in membrane traffic.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 103 ·No. 32 ·2006-08-08 ·Pages 11821-7

Grosshans BL, Ortiz D, Novick P

Abstract

Rab proteins constitute the largest branch of the Ras GTPase superfamily. Rabs use the guanine nucleotide-dependent switch mechanism common to the superfamily to regulate each of the four major steps in membrane traffic: vesicle budding, vesicle delivery, vesicle tethering, and fusion of the vesicle membrane with that of the target compartment. These different tasks are carried out by a diverse collection of effector molecules that bind to specific Rabs in their GTP-bound state. Recent advances have not only greatly extended the number of known Rab effectors, but have also begun to define the mechanisms underlying their distinct functions. By binding to the guanine nucleotide exchange proteins that activate the Rabs certain effectors act to establish positive feedback loops that help to define and maintain tightly localized domains of activated Rab proteins, which then serve to recruit other effector molecules. Additionally, Rab cascades and Rab conversions appear to confer directionality to membrane traffic and couple each stage of traffic with the next along the pathway.

MeSH Terms
Biological Transport Cell Membrane/metabolism Endoplasmic Reticulum/metabolism Fungal Proteins/chemistry,physiology Golgi Apparatus/metabolism Membrane Proteins/chemistry Models, Biological Protein Structure, Tertiary rab GTP-Binding Proteins/physiology
Chemicals
Fungal Proteins Membrane Proteins rab GTP-Binding Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Grosshans Bianka L
Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06520, USA.
Ortiz Darinel
Novick Peter
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.0601617103
Published
2006-08-08
Epub
2006-00-01
Pages
11821-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC1567661
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.0601617103 PMC Full Text View journal details
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