Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Binding of the complexin N terminus to the SNARE complex potentiates synaptic-vesicle fusogenicity.

Nature structural & molecular biology - 1 May 2010

Xue Mingshan, Craig Timothy K, Xu Junjie, Chao Hsiao-Tuan, Rizo Josep, Rosenmund Christian

Abstract excerpt

Complexins facilitate and inhibit neurotransmitter release through distinct domains, and their function was proposed to be coupled to the Ca(2+) sensor synaptotagmin-1 (Syt1). However, the mechanisms underlying complexin function remain unclear. We now uncover an interaction between the complexin N terminus and the SNARE complex C terminus, and we show that disrupting this interaction abolishes the facilitatory...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adaptor Proteins, Vesicular Transport
Share to Calcium

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Nerve Tissue Proteins

Share to Neurons

Share to Nuclear Magnetic Resonance, Biomolecular

Share to SNARE Proteins

Share to Synaptic Vesicles

Share to Synaptotagmin I

Source

Open in PubMed Open full text

Identifiers

PMID: 20400951
DOI: 10.1038/nsmb.1791
PMCID: PMC3172005

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Binding of the complexin N terminus to the SNARE complex potentiates synaptic-vesicle fusogenicity.PMID 20400951Read ↗

Synaptotagmin oligomerization is essential for calcium control of regulated exocytosis.Semantic proximity Read ↗

Mutations of Single Residues in the Complexin N-terminus Exhibit Distinct Phenotypes in Synaptic Vesicle Fusion.Semantic proximity Read ↗

Molecular origins of synaptotagmin 1 activities on vesicle docking and fusion pore opening.Semantic proximity Read ↗

Synergistic roles of Synaptotagmin-1 and complexin in calcium-regulated neuronal exocytosis.Semantic proximity Read ↗

Complexins living up to their name--new light on their role in exocytosis.Semantic proximity Read ↗

Vesicle docking and fusion pore modulation by the neuronal calcium sensor Synaptotagmin-1.Semantic proximity Read ↗

Fusion pore dynamics are regulated by synaptotagmin*t-SNARE interactions.Semantic proximity Read ↗

Deconstructing complexin function in activating and clamping Ca2+-triggered exocytosis by comparing knockout and knockdown phenotypes.Semantic proximity Read ↗

Vesicle docking and fusion pore modulation by the neuronal calcium sensor Synaptotagmin-1Semantic proximity Read ↗

Synaptotagmin controls and modulates synaptic-vesicle fusion in a Ca(2+)-dependent manner.Semantic proximity Read ↗

Transmembrane tethering of synaptotagmin to synaptic vesicles controls multiple modes of neurotransmitter release.Semantic proximity Read ↗

The C2 domains of synaptotagmin--partners in exocytosis.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.