Ypt/rab gtpases: regulators of protein trafficking.
Ypt/Rab guanosine triphosphatases (GTPases) have emerged in the last decade as key regulators of protein transport in all eukaryotic cells. They seem to be involved in all aspects of vesicle trafficking: vesicle formation, motility, and docking, and membrane remodeling and fusion. The functions of Ypt/Rabs are themselves controlled by upstream regulators that stimulate both their nucleotide cycling and their cycling between membranes. Ypt/Rabs transmit signals to downstream effectors in a guanosine triphosphate (GTP)-dependent manner. The identity of upstream regulators and downstream effectors is known for a number of Ypt/Rabs, and models for their mechanisms of action are emerging. In at least two cases, Ypt/Rab upstream regulators and downstream effectors are found together in a single complex. In agreement with the idea that Ypt/Rabs function in all aspects of vesicular transport, their diverse effectors have recently been shown to function in all identified aspects of vesicle transport. Activators and effectors for individual Ypt/Rabs share no similarity, but are conserved between yeast and mammalian cells. Finally, cross talk demonstrated among the various Ypt/Rabs, and between Ypt/Rabs and other signaling factors, suggests possible coordination among secretory steps, as well as between protein transport and other cellular processes.
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Department of Biological Sciences, Laboratory for Molecular Biology, University of Illinois at Chicago, MBRB 4120, 900 South Ashland Avenue, Chicago, IL 60607, USA. nava@uic.edu
D000818:Animals; D022162:Cytoplasmic Vesicles / Q000378:metabolism; D004705:Endocytosis; D005089:Exocytosis; D005656:Fungal Proteins / Q000502:physiology*; D020555:GTP-Binding Protein Regulators / Q000502:physiology; D006801:Humans; D008954:Models, Biological; D021381:Protein Transport; D015398:Signal Transduction; D020691:rab GTP-Binding Proteins / Q000502:physiology*
D005656:Fungal Proteins; D020555:GTP-Binding Protein Regulators; D020691:rab GTP-Binding Proteins