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

Gβγ inhibits exocytosis via interaction with critical residues on soluble N-ethylmaleimide-sensitive factor attachment protein-25.

Molecular pharmacology - 1 Dec 2012

Wells Christopher A, Zurawski Zack, Betke Katherine M, Yim Yun Young, Hyde Karren, Rodriguez Shelagh, Alford Simon, Hamm Heidi E

Abstract excerpt

Spatial and temporal regulation of neurotransmitter release is a complex process accomplished by the exocytotic machinery working in tandem with numerous regulatory proteins. G-protein βγ dimers regulate the core process of exocytosis by interacting with the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins soluble N-ethylmaleimide-sensitive factor attachment protein-25...

Read the complete abstract on PubMed

Topics

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

Share to Botulinum Toxins
Share to GTP-Binding Protein beta Subunits

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

Share to GTP-Binding Protein gamma Subunits

Share to Sf9 Cells

Share to SNARE Proteins

Share to Synaptosomal-Associated Protein 25

Share to Synaptotagmin I

Share to Syntaxin 1

Source

Open in PubMed Open full text

Identifiers

PMID: 22962332
DOI: 10.1124/mol.112.080507
PMCID: PMC3502621

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

Gβγ inhibits exocytosis via interaction with critical residues on soluble N-ethylmaleimide-sensitive factor attachment protein-25.PMID 22962332Read ↗

Gβγ directly modulates vesicle fusion by competing with synaptotagmin for binding to neuronal SNARE proteins embedded in membranes.Semantic proximity Read ↗

Ca2+-dependent synaptotagmin binding to SNAP-25 is essential for Ca2+-triggered exocytosis.Semantic proximity Read ↗

SNARE complex formation is triggered by Ca2+ and drives membrane fusion.Semantic proximity Read ↗

SNAP25 disease mutations change the energy landscape for synaptic exocytosis due to aberrant SNARE interactions.Semantic proximity Read ↗

Removing the Gβγ-SNAP25 brake on exocytosis enhances insulin action, promotes adipocyte browning, and protects against diet-induced obesitySemantic proximity Read ↗

A discontinuous SNAP-25 C-terminal coil supports exocytosis.Semantic proximity Read ↗

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

Selective disruption of the mammalian secretory apparatus enhances or eliminates calcium current modulation in nerve endings.Semantic proximity Read ↗

Phosphomimetic mutation of Ser-187 of SNAP-25 increases both syntaxin binding and highly Ca2+-sensitive exocytosis.Semantic proximity Read ↗

Syntaxin requirement for Ca2+-triggered exocytosis in neurons and endocrine cells demonstrated with an engineered neurotoxin.Semantic proximity Read ↗

Structural determinants of synaptobrevin 2 function in synaptic vesicle fusion.Semantic proximity Read ↗

Structural and mechanistic insights into secretagogin-mediated exocytosis.Semantic proximity Read ↗

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