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PMID: 9023371 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Binding of the synaptic vesicle v-SNARE, synaptotagmin, to the plasma membrane t-SNARE, SNAP-25, can explain docked vesicles at neurotoxin-treated synapses.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 94 ·No. 3 ·1997-02-04 ·Pages 997-1001

Schiavo G, Stenbeck G, Rothman JE, Söllner TH

Abstract

Neurotransmitter release requires the specific docking of synaptic vesicles to the presynaptic plasma membrane followed by a calcium-triggered fusion event. Herein we report a previously unsuspected interaction of the synaptic vesicle protein and likely calcium sensor synaptotagmin with the plasma membrane t-SNARE SNAP-25. This interaction appears to resolve the apparent paradox that synaptic vesicles are capable of docking even when VAMP (vesicle-associated membrane protein) or syntaxin is cleaved or deleted and suggests that two species of v-SNAREs (VAMP and synaptotagmin) and two species of t-SNAREs (SNAP-25 and syntaxin) interact to functionally dock synaptic vesicles.

MeSH Terms
Animals Botulinum Toxins/pharmacology Calcium-Binding Proteins Cattle Cell Membrane/metabolism Cerebral Cortex/metabolism Membrane Glycoproteins/genetics,metabolism Membrane Proteins/metabolism Nerve Tissue Proteins/genetics,metabolism Presynaptic Terminals Qa-SNARE Proteins R-SNARE Proteins Recombinant Fusion Proteins/metabolism SNARE Proteins Synaptic Transmission/physiology Synaptic Vesicles/metabolism Synaptosomal-Associated Protein 25 Synaptotagmins Vesicular Transport Proteins
Chemicals
Calcium-Binding Proteins Membrane Glycoproteins Membrane Proteins Nerve Tissue Proteins Qa-SNARE Proteins R-SNARE Proteins Recombinant Fusion Proteins SNARE Proteins Synaptosomal-Associated Protein 25 Vesicular Transport Proteins Synaptotagmins Botulinum Toxins botulinum toxin type E
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Schiavo G
Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.
Stenbeck G
Rothman J E
Söllner T H
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.94.3.997
Published
1997-02-04
Pages
997-1001
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC19628
Subset
IM
Corrections
CommentIn
PMID: 9023331
External Links
PubMed source DOI: 10.1073/pnas.94.3.997 PMC Full Text View journal details
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