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Article

Re-visiting the trans insertion model for complexin clamping.

eLife - 2 Apr 2015

Krishnakumar Shyam S, Li Feng, Coleman Jeff, Schauder Curtis M, Kümmel Daniel, Pincet Frederic, Rothman James E, Reinisch Karin M

Abstract excerpt

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...

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Share to Adaptor Proteins, Vesicular Transport
Share to Calorimetry

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 25831964
DOI: 10.7554/eLife.04463
PMCID: PMC4384536

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Re-visiting the trans insertion model for complexin clamping.PMID 25831964Read ↗

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Rapid and selective binding to the synaptic SNARE complex suggests a modulatory role of complexins in neuroexocytosis.Semantic proximity Read ↗

Genetic analysis of the Complexin trans-clamping model for cross-linking SNARE complexes in vivo.Semantic proximity Read ↗

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Structural organization of the synaptic exocytosis core complex.Semantic proximity Read ↗

Complexin is able to bind to SNARE core complexes in different assembled states with distinct affinity.Semantic proximity Read ↗

Membrane tethering by the atlastin GTPase depends on GTP hydrolysis but not on forming the cross-over configuration.Semantic proximity Read ↗

A highly tilted membrane configuration for the prefusion state of synaptobrevin.Semantic proximity Read ↗

Single-molecule studies of synaptotagmin and complexin binding to the SNARE complex.Semantic proximity Read ↗

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