NMR analysis of the structure of synaptobrevin and of its interaction with syntaxin

James Hazzard; Thomas C. Südhof; Jose Rizo-Rey

doi:10.1023/A:1008382027065

NMR analysis of the structure of synaptobrevin and of its interaction with syntaxin

James Hazzard, Thomas C. Südhof, Jose Rizo-Rey

Research output: Contribution to journal › Article › peer-review

68 Scopus citations

Abstract

Synaptobrevin is a synaptic vesicle protein that has an essential role in exocytosis and forms the SNARE complex with syntaxin and SNAP-25. We have analyzed the structure of isolated synaptobrevin and its binary interaction with syntaxin using NMR spectroscopy. Our results demonstrate that isolated synaptobrevin is largely unfolded in solution. The entire SNARE motif of synaptobrevin is capable of interacting with the isolated C-terminal SNARE motif of syntaxin but only a few residues bind to the full-length cytoplasmic region of syntaxin. This result suggests an interaction between the N- and C-terminal regions of syntaxin that competes with core complex assembly.

Original language	English (US)
Pages (from-to)	203-207
Number of pages	5
Journal	Journal of biomolecular NMR
Volume	14
Issue number	3
DOIs	https://doi.org/10.1023/A:1008382027065
State	Published - 1999

Keywords

Exocytosis
H, N and C assignments
Neurotransmitter release
Synaptic protein
Synaptobrevin
Syntaxin

ASJC Scopus subject areas

Biochemistry
Spectroscopy

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title = "NMR analysis of the structure of synaptobrevin and of its interaction with syntaxin",

abstract = "Synaptobrevin is a synaptic vesicle protein that has an essential role in exocytosis and forms the SNARE complex with syntaxin and SNAP-25. We have analyzed the structure of isolated synaptobrevin and its binary interaction with syntaxin using NMR spectroscopy. Our results demonstrate that isolated synaptobrevin is largely unfolded in solution. The entire SNARE motif of synaptobrevin is capable of interacting with the isolated C-terminal SNARE motif of syntaxin but only a few residues bind to the full-length cytoplasmic region of syntaxin. This result suggests an interaction between the N- and C-terminal regions of syntaxin that competes with core complex assembly.",

keywords = "Exocytosis, H, N and C assignments, Neurotransmitter release, Synaptic protein, Synaptobrevin, Syntaxin",

author = "James Hazzard and S{\"u}dhof, {Thomas C.} and Jose Rizo-Rey",

note = "Funding Information: We thank Lewis Kay for providing pulse sequences. This work was supported by an Established Investigator Grant from the American Heart Association and a grant from the Welch Foundation (to J.R.). Copyright: Copyright 2007 Elsevier B.V., All rights reserved.",

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AU - Hazzard, James

AU - Südhof, Thomas C.

AU - Rizo-Rey, Jose

N1 - Funding Information: We thank Lewis Kay for providing pulse sequences. This work was supported by an Established Investigator Grant from the American Heart Association and a grant from the Welch Foundation (to J.R.). Copyright: Copyright 2007 Elsevier B.V., All rights reserved.

PY - 1999

Y1 - 1999

N2 - Synaptobrevin is a synaptic vesicle protein that has an essential role in exocytosis and forms the SNARE complex with syntaxin and SNAP-25. We have analyzed the structure of isolated synaptobrevin and its binary interaction with syntaxin using NMR spectroscopy. Our results demonstrate that isolated synaptobrevin is largely unfolded in solution. The entire SNARE motif of synaptobrevin is capable of interacting with the isolated C-terminal SNARE motif of syntaxin but only a few residues bind to the full-length cytoplasmic region of syntaxin. This result suggests an interaction between the N- and C-terminal regions of syntaxin that competes with core complex assembly.

AB - Synaptobrevin is a synaptic vesicle protein that has an essential role in exocytosis and forms the SNARE complex with syntaxin and SNAP-25. We have analyzed the structure of isolated synaptobrevin and its binary interaction with syntaxin using NMR spectroscopy. Our results demonstrate that isolated synaptobrevin is largely unfolded in solution. The entire SNARE motif of synaptobrevin is capable of interacting with the isolated C-terminal SNARE motif of syntaxin but only a few residues bind to the full-length cytoplasmic region of syntaxin. This result suggests an interaction between the N- and C-terminal regions of syntaxin that competes with core complex assembly.

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KW - H, N and C assignments

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KW - Syntaxin

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NMR analysis of the structure of synaptobrevin and of its interaction with syntaxin

Abstract

Keywords

ASJC Scopus subject areas

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