title: Rab GTPase localization and Rab cascades in Golgi transport.
abstract: Rab GTPases are master regulators of membrane traffic. By binding to distinct sets of effector proteins, Rabs catalyse the formation of function-specifying membrane microdomains. They are delivered to membranes by a protein named GDI (guanine-nucleotide-dissociation inhibitor) and are stabilized there after nucleotide exchange by effector binding. In the present mini-review, I discuss what we know about how Rab GTPases are delivered to the correct membrane-bound compartments and how Rab GTPase cascades order Rabs within the secretory and endocytic pathways. Finally, I describe how Rab cascades may establish the distinct compartments of the Golgi complex to permit ordered processing, sorting and secretion of secretory cargoes.
authors.affiliation: Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307, USA. pfeffer@stanford.edu
authors.forename: Suzanne R
authors.initials: SR
authors.lastname: Pfeffer
mesh_terms: D000818:Animals; D006056:Golgi Apparatus / Q000378:metabolism* / Q000648:ultrastructure; D020730:Guanine Nucleotide Dissociation Inhibitors / Q000378:metabolism / Q000502:physiology; D020662:Guanine Nucleotide Exchange Factors / Q000378:metabolism / Q000502:physiology; D006801:Humans; D011485:Protein Binding; D021381:Protein Transport; D020691:rab GTP-Binding Proteins / Q000378:metabolism*
chemical_list: D020730:Guanine Nucleotide Dissociation Inhibitors; D020662:Guanine Nucleotide Exchange Factors; D020691:rab GTP-Binding Proteins