Cargando…

Snarepins Are Functionally Resistant to Disruption by Nsf and αSNAP

SNARE (SNAP [soluble NSF {N-ethylmaleimide–sensitive fusion protein} attachment protein] receptor) proteins are required for many fusion processes, and recent studies of isolated SNARE proteins reveal that they are inherently capable of fusing lipid bilayers. Cis-SNARE complexes (formed when vesicle...

Descripción completa

Detalles Bibliográficos
Autores principales: Weber, Thomas, Parlati, Francesco, McNew, James A., Johnston, Robert J., Westermann, Benedikt, Söllner, Thomas H., Rothman, James E.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2000
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2174819/
https://www.ncbi.nlm.nih.gov/pubmed/10831610
_version_ 1782145379731505152
author Weber, Thomas
Parlati, Francesco
McNew, James A.
Johnston, Robert J.
Westermann, Benedikt
Söllner, Thomas H.
Rothman, James E.
author_facet Weber, Thomas
Parlati, Francesco
McNew, James A.
Johnston, Robert J.
Westermann, Benedikt
Söllner, Thomas H.
Rothman, James E.
author_sort Weber, Thomas
collection PubMed
description SNARE (SNAP [soluble NSF {N-ethylmaleimide–sensitive fusion protein} attachment protein] receptor) proteins are required for many fusion processes, and recent studies of isolated SNARE proteins reveal that they are inherently capable of fusing lipid bilayers. Cis-SNARE complexes (formed when vesicle SNAREs [v-SNAREs] and target membrane SNAREs [t-SNAREs] combine in the same membrane) are disrupted by the action of the abundant cytoplasmic ATPase NSF, which is necessary to maintain a supply of uncombined v- and t-SNAREs for fusion in cells. Fusion is mediated by these same SNARE proteins, forming trans-SNARE complexes between membranes. This raises an important question: why doesn't NSF disrupt these SNARE complexes as well, preventing fusion from occurring at all? Here, we report several lines of evidence that demonstrate that SNAREpins (trans-SNARE complexes) are in fact functionally resistant to NSF, and they become so at the moment they form and commit to fusion. This elegant design allows fusion to proceed locally in the face of an overall environment that massively favors SNARE disruption.
format Text
id pubmed-2174819
institution National Center for Biotechnology Information
language English
publishDate 2000
publisher The Rockefeller University Press
record_format MEDLINE/PubMed
spelling pubmed-21748192008-05-01 Snarepins Are Functionally Resistant to Disruption by Nsf and αSNAP Weber, Thomas Parlati, Francesco McNew, James A. Johnston, Robert J. Westermann, Benedikt Söllner, Thomas H. Rothman, James E. J Cell Biol Original Article SNARE (SNAP [soluble NSF {N-ethylmaleimide–sensitive fusion protein} attachment protein] receptor) proteins are required for many fusion processes, and recent studies of isolated SNARE proteins reveal that they are inherently capable of fusing lipid bilayers. Cis-SNARE complexes (formed when vesicle SNAREs [v-SNAREs] and target membrane SNAREs [t-SNAREs] combine in the same membrane) are disrupted by the action of the abundant cytoplasmic ATPase NSF, which is necessary to maintain a supply of uncombined v- and t-SNAREs for fusion in cells. Fusion is mediated by these same SNARE proteins, forming trans-SNARE complexes between membranes. This raises an important question: why doesn't NSF disrupt these SNARE complexes as well, preventing fusion from occurring at all? Here, we report several lines of evidence that demonstrate that SNAREpins (trans-SNARE complexes) are in fact functionally resistant to NSF, and they become so at the moment they form and commit to fusion. This elegant design allows fusion to proceed locally in the face of an overall environment that massively favors SNARE disruption. The Rockefeller University Press 2000-05-29 /pmc/articles/PMC2174819/ /pubmed/10831610 Text en © 2000 The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Original Article
Weber, Thomas
Parlati, Francesco
McNew, James A.
Johnston, Robert J.
Westermann, Benedikt
Söllner, Thomas H.
Rothman, James E.
Snarepins Are Functionally Resistant to Disruption by Nsf and αSNAP
title Snarepins Are Functionally Resistant to Disruption by Nsf and αSNAP
title_full Snarepins Are Functionally Resistant to Disruption by Nsf and αSNAP
title_fullStr Snarepins Are Functionally Resistant to Disruption by Nsf and αSNAP
title_full_unstemmed Snarepins Are Functionally Resistant to Disruption by Nsf and αSNAP
title_short Snarepins Are Functionally Resistant to Disruption by Nsf and αSNAP
title_sort snarepins are functionally resistant to disruption by nsf and αsnap
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2174819/
https://www.ncbi.nlm.nih.gov/pubmed/10831610
work_keys_str_mv AT weberthomas snarepinsarefunctionallyresistanttodisruptionbynsfandasnap
AT parlatifrancesco snarepinsarefunctionallyresistanttodisruptionbynsfandasnap
AT mcnewjamesa snarepinsarefunctionallyresistanttodisruptionbynsfandasnap
AT johnstonrobertj snarepinsarefunctionallyresistanttodisruptionbynsfandasnap
AT westermannbenedikt snarepinsarefunctionallyresistanttodisruptionbynsfandasnap
AT sollnerthomash snarepinsarefunctionallyresistanttodisruptionbynsfandasnap
AT rothmanjamese snarepinsarefunctionallyresistanttodisruptionbynsfandasnap