Review
Nature Reviews Molecular Cell Biology 5, 886-896 (November 2004) | doi:10.1038/nrm1500
Targeting Rab GTPases to distinct membrane compartments
Suzanne Pfeffer1 & Dikran Aivazian1 About the authors
Abstract
Rab GTPases are key to membrane-trafficking events in eukaryotic cells, and human cells contain more than 60 Rab proteins that are localized to distinct compartments. The recent determination of the structure of a monoprenylated Rab GTPase bound to GDP-dissociation inhibitor provides new molecular details that are relevant to models of Rab delivery. The further discovery of an integral membrane protein that can dissociate prenylated Rab proteins from GDP-dissociation inhibitor gives new insights into the mechanisms of Rab localization.
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Author affiliations
- Department of Biochemistry, Stanford University School of Medicine, Stanford, California 94305-5307, USA.
Correspondence to: Suzanne Pfeffer1 Email: pfeffer@stanford.edu
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