Synaptic vesicle phosphoproteins and regulation of synaptic function.
Complex brain functions, such as learning and memory, are believed to involve changes in the efficiency of communication between nerve cells. Therefore, the elucidation of the molecular mechanisms that regulate synaptic transmission, the process of intercellular communication, is an essential step toward understanding nervous system function. Several proteins associated with synaptic vesicles, the organelles that store neurotransmitters, are targets for protein phosphorylation and dephosphorylation. One of these phosphoproteins, synapsin I, by means of changes in its state of phosphorylation, appears to control the fraction of synaptic vesicles available for release and thereby to regulate the efficiency of neurotransmitter release. This article describes current understanding of the mechanism by which synapsin I modulates communication between nerve cells and reviews the properties and putative functions of other phosphoproteins associated with synaptic vesicles.
Greengard
P
P
Laboratory of Molecular and Cellular Neuroscience, Rockefeller University, New York, NY 10021.
Valtorta
F
F
Czernik
A J
AJ
Benfenati
F
F
D000818:Animals; D002135:Calcium-Binding Proteins; D006706:Homeostasis; D008562:Membrane Glycoproteins / Q000502:physiology; D008959:Models, Neurological; D009419:Nerve Tissue Proteins / Q000502:physiology*; D010750:Phosphoproteins / Q000378:metabolism*; D011494:Protein Kinases / Q000378:metabolism*; D013569:Synapses / Q000502:physiology* / Q000648:ultrastructure; D016704:Synapsins / Q000502:physiology*; D013572:Synaptic Vesicles / Q000502:physiology* / Q000648:ultrastructure; D050857:Synaptotagmins
D002135:Calcium-Binding Proteins; D008562:Membrane Glycoproteins; D009419:Nerve Tissue Proteins; D010750:Phosphoproteins; D016704:Synapsins; D050857:Synaptotagmins; D011494:Protein Kinases