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Article

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

The Journal of cell biology - 19 Jun 2006

Carpp Lindsay N, Ciufo Leonora F, Shanks Scott G, Boyd Alan, Bryant Nia J

Abstract excerpt

Sec1p/Munc18 (SM) proteins are essential for SNARE-mediated membrane trafficking. The formulation of unifying hypotheses for the function of the SM protein family has been hampered by the observation that two of its members bind their cognate syntaxins (Sxs) in strikingly different ways. The SM protein Vps45p binds its Sx Tlg2p in a manner analogous to that captured by the Sly1p-Sed5p crystal structure, whereby...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 16769821
DOI: 10.1083/jcb.200512024
PMCID: PMC3215948

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Sec1p/Munc18 protein Vps45p binds its cognate SNARE proteins via two distinct modes.PMID 16769821Read ↗

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

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

Selective activation of cognate SNAREpins by Sec1/Munc18 proteins.Semantic proximity Read ↗

The Sec1/Munc18 Protein Groove Plays a Conserved Role in Interaction with Sec9p/SNAP-25.Semantic proximity Read ↗

Structure-based functional analysis reveals a role for the SM protein Sly1p in retrograde transport to the endoplasmic reticulum.Semantic proximity Read ↗

Chaperoning SNARE Folding and Assembly.Semantic proximity Read ↗

The trans-SNARE-regulating function of Munc18-1 is essential to synaptic exocytosis.Semantic proximity Read ↗

SNARE bundle and syntaxin N-peptide constitute a minimal complement for Munc18-1 activation of membrane fusion.Semantic proximity Read ↗

Identification of functionally interacting SNAREs by using complementary substitutions in the conserved '0' layer.Semantic proximity Read ↗

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