The effects of SNAP/SNARE complexes on the ATPase of NSF

Elena Matveeva; Sidney W. Whiteheart

doi:10.1016/S0014-5793(98)01071-0

The effects of SNAP/SNARE complexes on the ATPase of NSF

Elena Matveeva
, Sidney W. Whiteheart

Molecular and Cellular Biochemistry

Producción científica: Article › revisión exhaustiva

27 Citas (Scopus)

Resumen

The ATPase of the N-ethylmaleimide sensitive factor (NSF) appears to be central to the events that culminate in vesicle-target membrane fusion. Complexes containing different combinations of NSF, α-SNAP, Vamp-2 (synaptobrevin 2), syntaxin 1, and SNAP-25 were reconstituted and then tested for their effect on the ATPase of NSF. While NSF interacts with all α-SNAP-containing complexes, only the α-SNAP/t-SNARE complex significantly stimulated ATPase activity. This stimulation was dependent on increasing SNAP/t-SNARE complex and was saturable. The apparent stimulation of ATPase activity is due to a 10-fold increase in initial hydrolysis rate. Complex containing both v- and t-SNAREs bound significantly more α-SNAP but did not stimulate the ATPase of NSF. Copyright (C) 1998 Federation of European Biochemical Societies.

Idioma original	English
Páginas (desde-hasta)	211-214
Número de páginas	4
Publicación	FEBS Letters
Volumen	435
N.º	2-3
DOI	https://doi.org/10.1016/S0014-5793(98)01071-0
Estado	Published - sept 18 1998

Nota bibliográfica

Funding Information:
We thank Dr. Susan A. Buhrow and Dr. Sergey V. Matveev for critical reading of the manuscript, Mr. Jim Smith for his excellent photographic assistance, and the members of the Whiteheart laboratory for their invaluable discussion. We would also like to thank Dr. Phyllis Hanson for the generous gift of the synaptobrevin-2 (Vamp-2) expression construct. This work was supported by the National Institutes of Health Grant HL56652 (to S.W.W.).

Financiación

We thank Dr. Susan A. Buhrow and Dr. Sergey V. Matveev for critical reading of the manuscript, Mr. Jim Smith for his excellent photographic assistance, and the members of the Whiteheart laboratory for their invaluable discussion. We would also like to thank Dr. Phyllis Hanson for the generous gift of the synaptobrevin-2 (Vamp-2) expression construct. This work was supported by the National Institutes of Health Grant HL56652 (to S.W.W.).

Financiadores	Número del financiador
National Institutes of Health (NIH)
National Heart, Lung, and Blood Institute (NHLBI)	R01HL056652

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/S0014-5793(98)01071-0

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title = "The effects of SNAP/SNARE complexes on the ATPase of NSF",

abstract = "The ATPase of the N-ethylmaleimide sensitive factor (NSF) appears to be central to the events that culminate in vesicle-target membrane fusion. Complexes containing different combinations of NSF, α-SNAP, Vamp-2 (synaptobrevin 2), syntaxin 1, and SNAP-25 were reconstituted and then tested for their effect on the ATPase of NSF. While NSF interacts with all α-SNAP-containing complexes, only the α-SNAP/t-SNARE complex significantly stimulated ATPase activity. This stimulation was dependent on increasing SNAP/t-SNARE complex and was saturable. The apparent stimulation of ATPase activity is due to a 10-fold increase in initial hydrolysis rate. Complex containing both v- and t-SNAREs bound significantly more α-SNAP but did not stimulate the ATPase of NSF. Copyright (C) 1998 Federation of European Biochemical Societies.",

keywords = "AAA ATPase, Membrane fusion, N-Ethylmaleimide sensitive factor, SNAP receptor, Soluble NSF attachment protein, Vesicular traffic",

author = "Elena Matveeva and Whiteheart, \{Sidney W.\}",

note = "Funding Information: We thank Dr. Susan A. Buhrow and Dr. Sergey V. Matveev for critical reading of the manuscript, Mr. Jim Smith for his excellent photographic assistance, and the members of the Whiteheart laboratory for their invaluable discussion. We would also like to thank Dr. Phyllis Hanson for the generous gift of the synaptobrevin-2 (Vamp-2) expression construct. This work was supported by the National Institutes of Health Grant HL56652 (to S.W.W.).",

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doi = "10.1016/S0014-5793(98)01071-0",

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N2 - The ATPase of the N-ethylmaleimide sensitive factor (NSF) appears to be central to the events that culminate in vesicle-target membrane fusion. Complexes containing different combinations of NSF, α-SNAP, Vamp-2 (synaptobrevin 2), syntaxin 1, and SNAP-25 were reconstituted and then tested for their effect on the ATPase of NSF. While NSF interacts with all α-SNAP-containing complexes, only the α-SNAP/t-SNARE complex significantly stimulated ATPase activity. This stimulation was dependent on increasing SNAP/t-SNARE complex and was saturable. The apparent stimulation of ATPase activity is due to a 10-fold increase in initial hydrolysis rate. Complex containing both v- and t-SNAREs bound significantly more α-SNAP but did not stimulate the ATPase of NSF. Copyright (C) 1998 Federation of European Biochemical Societies.

AB - The ATPase of the N-ethylmaleimide sensitive factor (NSF) appears to be central to the events that culminate in vesicle-target membrane fusion. Complexes containing different combinations of NSF, α-SNAP, Vamp-2 (synaptobrevin 2), syntaxin 1, and SNAP-25 were reconstituted and then tested for their effect on the ATPase of NSF. While NSF interacts with all α-SNAP-containing complexes, only the α-SNAP/t-SNARE complex significantly stimulated ATPase activity. This stimulation was dependent on increasing SNAP/t-SNARE complex and was saturable. The apparent stimulation of ATPase activity is due to a 10-fold increase in initial hydrolysis rate. Complex containing both v- and t-SNAREs bound significantly more α-SNAP but did not stimulate the ATPase of NSF. Copyright (C) 1998 Federation of European Biochemical Societies.

KW - AAA ATPase

KW - Membrane fusion

KW - N-Ethylmaleimide sensitive factor

KW - SNAP receptor

KW - Soluble NSF attachment protein

KW - Vesicular traffic

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The effects of SNAP/SNARE complexes on the ATPase of NSF

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Nota bibliográfica

Financiación

ASJC Scopus subject areas

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