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Article

The N-terminal peptide of the syntaxin Tlg2p modulates binding of its closed conformation to Vps45p.

Proceedings of the National Academy of Sciences of the United States of America - 25 Aug 2009

Furgason Melonnie L M, MacDonald Chris, Shanks Scott G, Ryder Sean P, Bryant Nia J, Munson Mary

Abstract excerpt

The Sec1/Munc18 (SM) protein family regulates intracellular trafficking through interactions with individual SNARE proteins and assembled SNARE complexes. Revealing a common mechanism of this regulation has been challenging, largely because of the multiple modes of interaction observed between SM proteins and their cognate syntaxin-type SNAREs. These modes include binding of the SM to a closed conformation of...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 19667197
DOI: 10.1073/pnas.0902976106
PMCID: PMC2732825

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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

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Click a neighbor to travelStep 1 · 12 closest

The N-terminal peptide of the syntaxin Tlg2p modulates binding of its closed conformation to Vps45p.PMID 19667197Read ↗

Cellular levels of the syntaxin Tlg2p are regulated by a single mode of binding to Vps45p.Semantic proximity Read ↗

The Sec1p/Munc18 protein Vps45p binds its cognate SNARE proteins via two distinct modes.Semantic proximity Read ↗

Vps45p stabilizes the syntaxin homologue Tlg2p and positively regulates SNARE complex formation.Semantic proximity Read ↗

The Sec1/Munc18 protein Vps45 regulates cellular levels of its SNARE binding partners Tlg2 and Snc2 in Saccharomyces cerevisiae.Semantic proximity Read ↗

Mso1p regulates membrane fusion through interactions with the putative N-peptide-binding area in Sec1p domain 1.Semantic proximity Read ↗

Munc18-1 induces conformational changes of syntaxin-1 in multiple intermediates for SNARE assembly.Semantic proximity Read ↗

How Tlg2p/syntaxin 16 'snares’ Vps45Semantic proximity Read ↗

Rescue of Munc18-1 and -2 double knockdown reveals the essential functions of interaction between Munc18 and closed syntaxin in PC12 cells.Semantic proximity Read ↗

The length of cargo-protein transmembrane segments drives secretory transport by facilitating cargo concentration in export domains.Semantic proximity Read ↗

Syntaxin binding mechanism and disease-causing mutations in Munc18-2Semantic proximity Read ↗

Dynamic conformational changes in munc18 prevent syntaxin binding.Semantic proximity Read ↗

Syntaxin N-terminal peptide motif is an initiation factor for the assembly of the SNARE-Sec1/Munc18 membrane fusion complex.Semantic proximity Read ↗

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