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Review
. 2010 Aug;22(4):461-70.
doi: 10.1016/j.ceb.2010.04.007. Epub 2010 May 11.

Rab GEFs and GAPs

Francis Barr  1 , David G Lambright
Affiliations
Review

Rab GEFs and GAPs

Francis Barr et al. Curr Opin Cell Biol. 2010 Aug.

Abstract

Rabs are GTP-binding proteins with conserved functions in membrane trafficking. They are regulated by a diverse group of structurally unrelated GDP-GTP exchange factors (GEFs), and a family of GTP-hydrolysis activating proteins (GAPs) containing the conserved TBC domain. Recent structural and cell biological studies shed new light on the mechanisms of Rab GEF and GAP action, and the cellular trafficking pathways they act in.

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Figures

Figure 1
Figure 1. Comparison of GEF complexes with the nucleotide free intermediates of Rab GTPases
The nucleotide binding site is marked by GTP and Mg2+ from the structure of Rab5A after superposition. Images were rendered with PyMOL (www.pymol.org) using coordinates from crystal structures with the following PDB ID codes: 2OT3 (Rabex-5/Rab21), 2FU5 (Mss4/Rab8), 2OCY (Sec2/Sec4), 3CUE (TRAPP/Ypt1), and 3JZA (SidM/DrrA). See text for citations and discussion.
Figure 2
Figure 2. Comparison of the nucleotide sites of GAP-GTPase complexes with GDP and either the transition state mimic AlF3/AlF4 or the ground state mimic BeF3
Images were rendered with PyMOL (www.pymol.org) using coordinates from crystal structures with the following PDB ID codes: 2G77 (Gyp1p/Rab33), 1WQ1 (RasGAP/Ras), 1TAD (Gtα), and 3BRW (RapGAP/Rap). See text for citations and discussion.
See this image and copyright information in PMC

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