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

Analysis of SEC9 suppression reveals a relationship of SNARE function to cell physiology.

PloS one - 1 Jan 2009

Williams Daniel C, Novick Peter J

Abstract excerpt

BACKGROUND: Growth and division of Saccharomyces cerevisiae is dependent on the action of SNARE proteins that are required for membrane fusion. SNAREs are regulated, through a poorly understood mechanism, to ensure membrane fusion at the correct time and place within a cell. Although fusion of secretory vesicles with the plasma membrane is important for yeast cell growth, the relationship between exocytic SNAREs...

Read the complete abstract on PubMed

Topics

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

Share to Adaptor Proteins, Signal Transducing
Share to Qa-SNARE Proteins
Share to R-SNARE Proteins

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

Share to Saccharomyces cerevisiae Proteins

Share to SNARE Proteins

Share to Temperature

Share to Vacuolar Proton-Translocating ATPases

Share to Vacuoles

Source

Open in PubMed Open full text

Identifiers

PMID: 19421331
DOI: 10.1371/journal.pone.0005449
PMCID: PMC2674220

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

Analysis of SEC9 suppression reveals a relationship of SNARE function to cell physiology.PMID 19421331Read ↗

t-SNARE dephosphorylation promotes SNARE assembly and exocytosis in yeast.Semantic proximity Read ↗

Geranylgeranylated SNAREs are dominant inhibitors of membrane fusion.Semantic proximity Read ↗

Conserved alpha-helical segments on yeast homologs of the synaptobrevin/VAMP family of v-SNAREs mediate exocytic function.Semantic proximity Read ↗

Functional analysis of phosphorylation on Saccharomyces cerevisiae syntaxin 1 homologues Sso1p and Sso2p.Semantic proximity Read ↗

ER-associated retrograde SNAREs and the Dsl1 complex mediate an alternative, Sey1p-independent homotypic ER fusion pathway.Semantic proximity Read ↗

Yeast homologues of tomosyn and lethal giant larvae function in exocytosis and are associated with the plasma membrane SNARE, Sec9.Semantic proximity Read ↗

Binding interactions control SNARE specificity in vivo.Semantic proximity Read ↗

The yeast tumor suppressor homologue Sro7p is required for targeting of the sodium pumping ATPase to the cell surface.Semantic proximity Read ↗

An N-end rule destabilization mutant reveals pre-Golgi requirements for Sec7p in yeast membrane traffic.Semantic proximity Read ↗

Characterization of temperature-sensitive mutations in the yeast syntaxin 1 homologues Sso1p and Sso2p, and evidence of a distinct function for Sso1p in sporulation.Semantic proximity Read ↗

A random mutagenesis approach to isolate dominant-negative yeast sec1 mutants reveals a functional role for domain 3a in yeast and mammalian Sec1/Munc18 proteins.Semantic proximity Read ↗

Functional specialization within a vesicle tethering complex: bypass of a subset of exocyst deletion mutants by Sec1p or Sec4p.Semantic proximity Read ↗

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