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Article
Nature Neuroscience  1, 29 - 35 (1998)
doi:10.1038/229

Two sites of action for synapsin domain E in regulating neurotransmitter release

Sabine Hilfiker1, 3, Felix E. Schweizer2, 3, Hung-Teh Kao1, Andrew J. Czernik1, Paul Greengard1 & George J. Augustine2, 3

1  Laboratory of Molecular and Cellular Neuroscience, The Rockefeller University, New York, New York 10021, USA

2  Department of Neurobiology, Duke University Medical Center, Durham, North Carolina 27710, USA

3  Marine Biological Laboratory, Woods Hole, Massachusetts 02543, USA

Correspondence should be addressed to Paul Greengard greengd@rockvax.rockefeller.edu
Synapsins, a family of synaptic vesicle proteins, have been shown to regulate neurotransmitter release; the mechanism(s) by which they act are not fully understood. Here we have studied the role of domain E of synapsins in neurotransmitter release at the squid giant synapse. Two squid synapsin isoforms were cloned and found to contain a carboxy (C)-terminal domain homologous to domain E of the vertebrate a-type synapsin isoforms. Presynaptic injection of a peptide fragment of domain E greatly reduced the number of synaptic vesicles in the periphery of the active zone, and increased the rate and extent of synaptic depression, suggesting that domain E is essential for synapsins to regulate a reserve pool of synaptic vesicles. Domain E peptide had no effect on the number of docked synaptic vesicles, yet reversibly inhibited and slowed the kinetics of neurotransmitter release, indicating a second role for synapsins that is more intimately associated with the release process itself. Thus, synapsin domain E is involved in at least two distinct reactions that are crucial for exocytosis in presynaptic terminals.

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Nature Neuroscience
ISSN: 1097-6256
EISSN: 1546-1726
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