Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 7-Day Trial for You or Your Team.

Learn More →

Synaptic vesicle-associated Ca2+/calmodulin-dependent protein kinase II is a binding protein for synapsin I

Synaptic vesicle-associated Ca2+/calmodulin-dependent protein kinase II is a binding protein for... SYNAPSIN I is a synaptic vesicle-associated phosphoprotein that is involved in the modulation of neurotransmitter release1. Ca2+/calmodulin-dependent protein kinase II, which phosphory-lates two sites in the carboxy-terminal region of synapsin I, causes synapsin I to dissociate from synaptic vesicles2 and increases nerotransmitter release3,4. Conversely, the dephosphorylated form of synapsin I, but not the form phosphorylated by Ca2+/cal-modulin-dependent protein kinase II, inhibits neurotransmitter release4–6. The amino-terminal region of synapsin I interacts with membrane phospholipids, whereas the C-terminal region binds to a protein component of synaptic vesicles7,8. Here we demonstrate that the binding of the C-terminal region of synapsin I involves the regulatory domain of a synaptic vesicle-associated form of Ca2+/calmodulin-dependent protein kinase II. Our results indicate that this form of the kinase functions both as a binding protein for synapsin I, and as an enzyme that phosphorylates synapsin I and promotes its dissociation from the vesicles. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Springer Journals

Synaptic vesicle-associated Ca2+/calmodulin-dependent protein kinase II is a binding protein for synapsin I

Download PDF
4 pages

Loading next page...
 
/lp/springer-journals/synaptic-vesicle-associated-ca2-calmodulin-dependent-protein-kinase-ii-YObEmMeIH4

References (26)

Publisher
Springer Journals
Copyright
Copyright © 1992 by Nature Publishing Group
Subject
Science, Humanities and Social Sciences, multidisciplinary; Science, Humanities and Social Sciences, multidisciplinary; Science, multidisciplinary
ISSN
0028-0836
eISSN
1476-4687
DOI
10.1038/359417a0
Publisher site
See Article on Publisher Site

Abstract

SYNAPSIN I is a synaptic vesicle-associated phosphoprotein that is involved in the modulation of neurotransmitter release1. Ca2+/calmodulin-dependent protein kinase II, which phosphory-lates two sites in the carboxy-terminal region of synapsin I, causes synapsin I to dissociate from synaptic vesicles2 and increases nerotransmitter release3,4. Conversely, the dephosphorylated form of synapsin I, but not the form phosphorylated by Ca2+/cal-modulin-dependent protein kinase II, inhibits neurotransmitter release4–6. The amino-terminal region of synapsin I interacts with membrane phospholipids, whereas the C-terminal region binds to a protein component of synaptic vesicles7,8. Here we demonstrate that the binding of the C-terminal region of synapsin I involves the regulatory domain of a synaptic vesicle-associated form of Ca2+/calmodulin-dependent protein kinase II. Our results indicate that this form of the kinase functions both as a binding protein for synapsin I, and as an enzyme that phosphorylates synapsin I and promotes its dissociation from the vesicles.

Journal

Nature – Springer Journals

Published: Oct 1, 1992

There are no references for this article.