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

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

PloS one - 1 Jan 2012

Shanks Scott G, Carpp Lindsay N, Struthers Marion S, McCann Rebecca K, Bryant Nia J

Abstract excerpt

Intracellular membrane trafficking pathways must be tightly regulated to ensure proper functioning of all eukaryotic cells. Central to membrane trafficking is the formation of specific SNARE (soluble N-ethylmeleimide-sensitive factor attachment protein receptor) complexes between proteins on opposing lipid bilayers. The Sec1/Munc18 (SM) family of proteins play an essential role in SNARE-mediated membrane fusion,...

Read the complete abstract on PubMed

Topics

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

Share to Intracellular Space
Share to Munc18 Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Stability

Share to Protein Transport

Share to Qa-SNARE Proteins

Share to R-SNARE Proteins

Share to SNARE Proteins

Share to Vesicular Transport Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 23166732
DOI: 10.1371/journal.pone.0049628
PMCID: PMC3498219

Provenance

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

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Sec1/Munc18 protein Vps45 regulates cellular levels of its SNARE binding partners Tlg2 and Snc2 in Saccharomyces cerevisiae.PMID 23166732Read ↗

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

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

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

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

Mammalian VPS45 orchestrates trafficking through the endosomal systemSemantic proximity Read ↗

TOR complex 2 (TORC2) signaling and the ESCRT machinery cooperate in the protection of plasma membrane integrity in yeast.Semantic proximity Read ↗

A novel SNARE complex implicated in vesicle fusion with the endoplasmic reticulum.Semantic proximity Read ↗

Cytoplasm to vacuole trafficking of aminopeptidase I requires a t-SNARE-Sec1p complex composed of Tlg2p and Vps45p.Semantic proximity Read ↗

A role for Tlg1p in the transport of proteins within the Golgi apparatus of Saccharomyces cerevisiae.Semantic proximity Read ↗

Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosisSemantic proximity Read ↗

Characterization of a novel yeast SNARE protein implicated in Golgi retrograde traffic.Semantic proximity Read ↗

Two syntaxin homologues in the TGN/endosomal system of yeast.Semantic proximity Read ↗

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