Targeting of Rab GTPases to cellular membranes. (1st August 2005)

• Record Type: Journal Article
• Authors: Ali, B.R.; Seabra, M.C.
• Is Part Of: Biochemical Society transactions. Volume 33:Number 4(2005)
• Page Start: 652
• Page End: 656
• Publication Date: 2005-08-01
• Subjects: GTPase -- guanine nucleotide dissociation inhibitor (GDI) -- membrane traffic -- prenylation -- Rab -- Rab escort protein (REP); Biochemistry -- Congresses; 572
• DOI: 10.1042/BST0330652
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : Rab proteins are members of the superfamily of Ras-like small GTPases and are involved in several cellular processes relating to membrane trafficking and organelle mobility throughout the cell. Like other small GTPases, Rab proteins are initially synthesized as soluble proteins and for membrane attachment they require the addition of lipid moiety(ies) to specific residues of their polypeptide chain. Despite their well-documented roles in regulating cellular trafficking, Rab proteins own trafficking is still poorly understood. We still need to elucidate the molecular mechanisms of their recruitment to cellular membranes and the structural determinants for their specific cellular localization. Recent results indicate that Rab cellular targeting might be Rab-dependent, and this paper briefly reviews our current knowledge of this process.