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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Detalles Bibliográficos
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
Descripción
Sumario: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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