A model for Rab GTPase localization. (1st August 2005)

• Record Type: Journal Article
• Authors: Pfeffer, S.
• Is Part Of: Biochemical Society transactions. Volume 33:Number 4(2005)
• Page Start: 627
• Page End: 630
• Publication Date: 2005-08-01
• Subjects: endosome -- GDP dissociation inhibitor (GDI) -- GTPase -- mannose 6-phosphate receptor -- membrane microdomain -- Rab; Biochemistry -- Congresses; 572
• DOI: 10.1042/BST0330627
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : The human genome encodes almost 70 Rab GTPases. These proteins are C-terminally geranylgeranylated and are localized to the surfaces of distinct membrane-bound compartments in eukaryotic cells. This mini review presents a working model for how Rabs achieve and maintain their steady-state localizations. Data from a number of laboratories suggest that Rabs participate in the generation of macromolecular assemblies that generate functional microdomains within a given membrane compartment. Our data suggest that these complex interactions are important for the cellular localization of Rab proteins at steady state.