Organization and function of the Rab prenylation and recycling machinery

Alexandrov , Kirill, Wu, Yaowen, Blankenfeldt, Wulf, Waldmann, Herbert and Goody, Roger S. (2011) Organization and function of the Rab prenylation and recycling machinery. The Enzymes, 29 147-162. doi:10.1016/B978-0-12-381339-8.00008-1


Author Alexandrov , Kirill
Wu, Yaowen
Blankenfeldt, Wulf
Waldmann, Herbert
Goody, Roger S.
Title Organization and function of the Rab prenylation and recycling machinery
Journal name The Enzymes   Check publisher's open access policy
ISSN 0423-2607
1874-6047
ISBN 9780123813398
Publication date 2011-01-20
Sub-type Article (original research)
DOI 10.1016/B978-0-12-381339-8.00008-1
Open Access Status
Volume 29
Start page 147
End page 162
Total pages 16
Place of publication San Diego, CA, United States
Publisher Academic Press
Collection year 2012
Language eng
Abstract The Rab proteins form the largest subgroup of the Ras superfamily and control multiple steps of intracellular vesicular transport. Similar to many other small GTPases, Rab proteins are posttranslationally prenylated. Prenylation by Rab Geranylgeranyl transferase increases hydrophobicity of the RabGTPases and enables them to reversibly associate with their target membrane. Due to the vectoriality of vesicular transport, RabGTPases are recycled upon completion of their functional cycle and returned to a cytosolic intermediate. The cytosolic form of Rab proteins is stabilized by the tightly binding chaperon termed GDP dissociation inhibitor (GDI). GDI also plays a central role in loading of prenylated RabGTPases onto the target membranes. In this chapter, we discuss available structural and biochemical data that shed light on the molecular mechanism of Rab prenylation, membrane delivery, and recycling. We discuss the important functional differences between GDI and a structurally related RabGGTase accessory factor termed Rab escort protein. We summarize the available data on the identity of factors mediating dissociation of the Rab:GDI complex prior to membrane loading and provide arguments for the critical role of guanine nucleotide exchange factors in this process.
Keyword RabGTPases
Protein prenylation
Protein prenyltransferases
Guanine nucleotide exchange factor
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ
Additional Notes Protein Prenylation PART A. Chapter 8

Document type: Journal Article
Sub-type: Article (original research)
Collections: Non HERDC
Institute for Molecular Bioscience - Publications
Australian Institute for Bioengineering and Nanotechnology Publications
 
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Created: Thu, 13 Oct 2011, 10:00:09 EST by Professor Kirill Alexandrov on behalf of Institute for Molecular Bioscience