Targeting Rab GTPases to distinct membrane compartments.
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.
Pfeffer
Suzanne
S
Department of Biochemistry, Stanford University School of Medicine, Stanford, California 94305-5307, USA. pfeffer@stanford.edu
Aivazian
Dikran
D
D000818:Animals; D002417:Cattle; D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism*; D003600:Cytosol / Q000378:metabolism; D020558:GTP Phosphohydrolases / Q000378:metabolism; D006153:Guanosine Diphosphate / Q000378:metabolism; D006801:Humans; D008954:Models, Biological; D008958:Models, Molecular; D010766:Phosphorylation; D010802:Phylogeny; D017368:Protein Prenylation; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D020691:rab GTP-Binding Proteins / Q000378:metabolism / Q000502:physiology*
D006153:Guanosine Diphosphate; D020558:GTP Phosphohydrolases; D020691:rab GTP-Binding Proteins