UNIT 15.18 Analysis of Rab GTPases

  1. Lars Langemeyer,
  2. Francis A. Barr

Published Online: 1 DEC 2012

DOI: 10.1002/0471143030.cb1518s57

Current Protocols in Cell Biology

Current Protocols in Cell Biology

How to Cite

Langemeyer, L. and Barr, F. A. 2012. Analysis of Rab GTPases. Current Protocols in Cell Biology. 57:15.18:15.18.1–15.18.17.

Author Information

  1. Department of Biochemistry, University of Oxford, Oxford, United Kingdom

Publication History

  1. Published Online: 1 DEC 2012
  2. Published Print: DEC 2012


This unit describes methods to identify proteins interacting with, and regulating, Rab GTPases. Rabs form the largest subgroup of Ras superfamily GTPases, and act as molecular switches controlling the specificity of membrane trafficking. The regulation and the signal readout of Rabs are mediated by four groups of proteins, the GDP-GTP exchange factors (GEFs), GTPase activating proteins (GAPs), Rab chaperones, and effector proteins. Rabs are activated at the membrane surface by specific GEFs that promote the exchange of bound GDP to GTP. Effector proteins then bind to the activated Rab GTPase and mediate the cellular response at this membrane surface. Finally, a Rab-specific GAP-protein inactivates the GTPase by catalyzing the hydrolysis of bound GTP to GDP, thus terminating the cellular response. The methods described here are valuable for characterizing these different types of activity, and assigning which Rab they act on. Curr. Protoc. Cell Biol. 57:15.18.1-15.18.17. © 2012 by John Wiley & Sons, Inc.


  • Rab;
  • GTPase;
  • GEF;
  • GAP;
  • effector-protein