title: Synaptic vesicle proteins and regulated exocytosis.
abstract: The recent identification of novel proteins associated with the membranes of synaptic vesicles has ignited the field of molecular neurobiology to probe the function of these molecules. Evidence is mounting that the vesicle proteins vamp (synaptobrevin), rab3A, synaptophysin, synaptotagmin (p65) and SV2 play an important role in regulated exocytosis, by regulating neurotransmitter uptake, vesicle targeting and fusion with the presynaptic plasma membrane.
authors.affiliation: Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Stanford University Medical Center, CA 94305.
authors.forename: L A
authors.initials: LA
authors.lastname: Elferink
authors.forename: R H
authors.initials: RH
authors.lastname: Scheller
mesh_terms: D000818:Animals; D002118:Calcium / Q000378:metabolism; D002135:Calcium-Binding Proteins; D016764:Cell Polarity; D005089:Exocytosis / Q000502:physiology*; D019204:GTP-Binding Proteins / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D008959:Models, Neurological; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D050683:R-SNARE Proteins; D013572:Synaptic Vesicles / Q000378:metabolism* / Q000648:ultrastructure; D016708:Synaptophysin / Q000378:metabolism; D050863:Synaptotagmin I; D050857:Synaptotagmins; D020692:rab3 GTP-Binding Proteins
chemical_list: D002135:Calcium-Binding Proteins; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D050683:R-SNARE Proteins; D016708:Synaptophysin; D050863:Synaptotagmin I; D050857:Synaptotagmins; D019204:GTP-Binding Proteins; D020692:rab3 GTP-Binding Proteins; D002118:Calcium