Re-visiting the trans insertion model for complexin clamping

We have previously proposed that complexin cross-links multiple pre-fusion SNARE complexes via a trans interaction to function as a clamp on SNARE-mediated neurotransmitter release. A recent NMR study was unable to detect the trans clamping interaction of complexin and therefore questioned the previ...

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Autores principales: Krishnakumar, Shyam S, Li, Feng, Coleman, Jeff, Schauder, Curtis M, Kümmel, Daniel, Pincet, Frederic, Rothman, James E, Reinisch, Karin M
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2015
Materias:
Biochemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4384536/
https://www.ncbi.nlm.nih.gov/pubmed/25831964
http://dx.doi.org/10.7554/eLife.04463
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author Krishnakumar, Shyam S
Li, Feng
Coleman, Jeff
Schauder, Curtis M
Kümmel, Daniel
Pincet, Frederic
Rothman, James E
Reinisch, Karin M
author_facet Krishnakumar, Shyam S
Li, Feng
Coleman, Jeff
Schauder, Curtis M
Kümmel, Daniel
Pincet, Frederic
Rothman, James E
Reinisch, Karin M
author_sort Krishnakumar, Shyam S
collection PubMed
description We have previously proposed that complexin cross-links multiple pre-fusion SNARE complexes via a trans interaction to function as a clamp on SNARE-mediated neurotransmitter release. A recent NMR study was unable to detect the trans clamping interaction of complexin and therefore questioned the previous interpretation of the fluorescence resonance energy transfer and isothermal titration calorimetry data on which the trans clamping model was originally based. Here we present new biochemical data that underscore the validity of our previous interpretation and the continued relevancy of the trans insertion model for complexin clamping. DOI: http://dx.doi.org/10.7554/eLife.04463.001
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spelling pubmed-43845362015-04-07 Re-visiting the trans insertion model for complexin clamping Krishnakumar, Shyam S Li, Feng Coleman, Jeff Schauder, Curtis M Kümmel, Daniel Pincet, Frederic Rothman, James E Reinisch, Karin M eLife Biochemistry We have previously proposed that complexin cross-links multiple pre-fusion SNARE complexes via a trans interaction to function as a clamp on SNARE-mediated neurotransmitter release. A recent NMR study was unable to detect the trans clamping interaction of complexin and therefore questioned the previous interpretation of the fluorescence resonance energy transfer and isothermal titration calorimetry data on which the trans clamping model was originally based. Here we present new biochemical data that underscore the validity of our previous interpretation and the continued relevancy of the trans insertion model for complexin clamping. DOI: http://dx.doi.org/10.7554/eLife.04463.001 eLife Sciences Publications, Ltd 2015-04-02 /pmc/articles/PMC4384536/ /pubmed/25831964 http://dx.doi.org/10.7554/eLife.04463 Text en © 2015, Krishnakumar et al http://creativecommons.org/licenses/by/4.0/ This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited.
spellingShingle Biochemistry
Krishnakumar, Shyam S
Li, Feng
Coleman, Jeff
Schauder, Curtis M
Kümmel, Daniel
Pincet, Frederic
Rothman, James E
Reinisch, Karin M
Re-visiting the trans insertion model for complexin clamping
title Re-visiting the trans insertion model for complexin clamping
title_full Re-visiting the trans insertion model for complexin clamping
title_fullStr Re-visiting the trans insertion model for complexin clamping
title_full_unstemmed Re-visiting the trans insertion model for complexin clamping
title_short Re-visiting the trans insertion model for complexin clamping
title_sort re-visiting the trans insertion model for complexin clamping
topic Biochemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4384536/
https://www.ncbi.nlm.nih.gov/pubmed/25831964
http://dx.doi.org/10.7554/eLife.04463
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