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

Fabio Benfenati, Flavia Valtorta, James L. Rubenstein, Fred S. Gorelick, Paul Greengard, Andrew J. Czernik

Research output: Contribution to journalArticle

224 Citations (Scopus)

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 phosphorylates 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+/calmodulin-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.

Original languageEnglish
Pages (from-to)417-420
Number of pages4
JournalNature
Volume359
Issue number6394
Publication statusPublished - Oct 1 1992

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Synapsins
Calcium-Calmodulin-Dependent Protein Kinase Type 2
Synaptic Vesicles
Carrier Proteins
Neurotransmitter Agents
Phosphoproteins
Phospholipids
Phosphotransferases
Membranes
Enzymes

ASJC Scopus subject areas

  • General

Cite this

Benfenati, F., Valtorta, F., Rubenstein, J. L., Gorelick, F. S., Greengard, P., & Czernik, A. J. (1992). Synaptic vesicle-associated Ca2+/calmodulin-dependent protein kinase II is a binding protein for synapsin I. Nature, 359(6394), 417-420.

Synaptic vesicle-associated Ca2+/calmodulin-dependent protein kinase II is a binding protein for synapsin I. / Benfenati, Fabio; Valtorta, Flavia; Rubenstein, James L.; Gorelick, Fred S.; Greengard, Paul; Czernik, Andrew J.

In: Nature, Vol. 359, No. 6394, 01.10.1992, p. 417-420.

Research output: Contribution to journalArticle

Benfenati, F, Valtorta, F, Rubenstein, JL, Gorelick, FS, Greengard, P & Czernik, AJ 1992, 'Synaptic vesicle-associated Ca2+/calmodulin-dependent protein kinase II is a binding protein for synapsin I', Nature, vol. 359, no. 6394, pp. 417-420.
Benfenati F, Valtorta F, Rubenstein JL, Gorelick FS, Greengard P, Czernik AJ. Synaptic vesicle-associated Ca2+/calmodulin-dependent protein kinase II is a binding protein for synapsin I. Nature. 1992 Oct 1;359(6394):417-420.
Benfenati, Fabio ; Valtorta, Flavia ; Rubenstein, James L. ; Gorelick, Fred S. ; Greengard, Paul ; Czernik, Andrew J. / Synaptic vesicle-associated Ca2+/calmodulin-dependent protein kinase II is a binding protein for synapsin I. In: Nature. 1992 ; Vol. 359, No. 6394. pp. 417-420.
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AB - SYNAPSIN I is a synaptic vesicle-associated phosphoprotein that is involved in the modulation of neurotransmitter release1. Ca2+/calmodulin-dependent protein kinase II, which phosphorylates 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+/calmodulin-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.

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