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Science 5 February 1993:
Vol. 259. no. 5096, pp. 780 - 785
DOI: 10.1126/science.8430330
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Articles

Science, Vol 259, Issue 5096, 780-785
Copyright © 1993 by American Association for the Advancement of Science

articles

Synaptic vesicle phosphoproteins and regulation of synaptic function

P Greengard, F Valtorta, AJ Czernik, and F Benfenati

Laboratory of Molecular and Cellular Neuroscience, Rockefeller University, New York, NY 10021.

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.


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F-Actin Is Concentrated in Nonrelease Domains at Frog Neuromuscular Junctions.
A. Dunaevsky and E. A. Connor (2000)
J. Neurosci. 20, 6007-6012
   Abstract »    Full Text »    PDF »
Nonreceptor tyrosine protein kinase pp60c-src in spatial learning: Synapse-specific changes in its gene expression, tyrosine phosphorylation, and protein-protein interactions.
W. Zhao, S. Cavallaro, P. Gusev, and D. L. Alkon (2000)
PNAS 97, 8098-8103
   Abstract »    Full Text »    PDF »
Phosphorylated Syntaxin 1 Is Localized to Discrete Domains Along a Subset of Axons.
D. L. Foletti, R. Lin, M. A. F. Finley, and R. H. Scheller (2000)
J. Neurosci. 20, 4535-4544
   Abstract »    Full Text »    PDF »
Disruption of actin impedes transmitter release in snake motor terminals.
J. C Cole, B. R S Villa, and R. S Wilkinson (2000)
J. Physiol. 525, 579-586
   Abstract »    Full Text »    PDF »
Intracellular Ca2+ and Ca2+/Calmodulin-Dependent Kinase II Mediate Acute Potentiation of Neurotransmitter Release by Neurotrophin-3.
X.-p. He, F. Yang, Z.-p. Xie, and B. Lu (2000)
J. Cell Biol. 149, 783-792
   Abstract »    Full Text »    PDF »
Synapsin III: Developmental Expression, Subcellular Localization, and Role in Axon Formation.
A. Ferreira, H.-T. Kao, J. Feng, M. Rapoport, and P. Greengard (2000)
J. Neurosci. 20, 3736-3744
   Abstract »    Full Text »    PDF »
Synucleins Are Developmentally Expressed, and alpha -Synuclein Regulates the Size of the Presynaptic Vesicular Pool in Primary Hippocampal Neurons.
D. D. Murphy, S. M. Rueter, J. Q. Trojanowski, and V. M.-Y. Lee (2000)
J. Neurosci. 20, 3214-3220
   Abstract »    Full Text »    PDF »
Prostaglandin E2 interaction with AVP: effects on AQP2 phosphorylation and distribution.
M. Zelenina, B. M. Christensen, J. Palmer, A. C. Nairn, S. Nielsen, and A. Aperia (2000)
Am J Physiol Renal Physiol 278, F388-F394
   Abstract »    Full Text »    PDF »
The Presynaptic Calcium Channel Is Part of a Transmembrane Complex Linking a Synaptic Laminin (alpha 4beta 2gamma 1) with Non-Erythroid Spectrin.
W. J. Sunderland, Y.-J. Son, J. H. Miner, J. R. Sanes, and S. S. Carlson (2000)
J. Neurosci. 20, 1009-1019
   Abstract »    Full Text »    PDF »
SNIP, a Novel SNAP-25-interacting Protein Implicated in Regulated Exocytosis.
L.-S. Chin, R. D. Nugent, M. C. Raynor, J. P. Vavalle, and L. Li (2000)
J. Biol. Chem. 275, 1191-1200
   Abstract »    Full Text »    PDF »
All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis.
J Modregger, B Ritter, B Witter, M Paulsson, and M Plomann (2000)
J. Cell Sci. 113, 4511-4521
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Use of phosphosynapsin I-specific antibodies for image analysis of signal transduction in single nerve terminals.
A Menegon, D. Dunlap, F Castano, F Benfenati, A. Czernik, P Greengard, and F Valtorta (2000)
J. Cell Sci. 113, 3573-3582
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The phosphatase inhibitor okadaic acid induces AQP2 translocation independently from AQP2 phosphorylation in renal collecting duct cells.
G Valenti, G Procino, M Carmosino, A Frigeri, R Mannucci, I Nicoletti, and M Svelto (2000)
J. Cell Sci. 113, 1985-1992
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Proteins involved in synaptic vesicle trafficking.
G. J Augustine, M. E Burns, W. M DeBello, S. Hilfiker, J. R Morgan, F. E Schweizer, H. Tokumaru, and K. Umayahara (1999)
J. Physiol. 520, 33-41
   Abstract »    Full Text »    PDF »


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