Evidence map›Paper›PMID 10330187›Full record

ArticleMolecular and cellular biology1999

Yeast VSM1 encodes a v-SNARE binding protein that may act as a negative regulator of constitutive exocytosis.

V Lustgarten, J E Gerst

Erratum issuedAbstract read
In one paragraph

Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.3field-weighted citation impact, top 20% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

31 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Ddi1 is a ubiquitin-dependent protease.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  6. Article
  7. Article
  8. Transcriptional regulation of the 26S proteasome by Nrf1.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2018
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. HIV proteinase inhibitors target the Ddi1-like protein of Leishmania parasites.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011
    Article
  14. Article
  15. Article
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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

V LustgartenDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel.
J E Gerst
Weizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have screened for proteins that interact with v-SNAREs of the late secretory pathway in the yeast Saccharomyces cerevisiae. A novel protein, designated Vsm1, binds tightly to the Snc2 v-SNARE in the two-hybrid system and can be coimmunoprecipitated with Snc1 or Snc2 from solubilized yeast cell extracts. Disruption of the VSM1 gene results in an increase of proteins secreted into the medium but does not affect the processing or secretion of invertase. In contrast, VSM1 overexpression in cells which bear a temperature-sensitive mutation in the Sec9 t-SNARE (sec9-4 cells) results in the accumulation of non-invertase-containing low-density secretory vesicles, inhibits cell growth and the secretion of proteins into the medium, and blocks rescue of the temperature-sensitive phenotype by SNC1 overexpression. Yet, VSM1 overexpression does not affect yeast bearing a sec9-7 allele which, in contrast to sec9-4, encodes a t-SNARE protein capable of forming a stable SNARE complex in vitro at restrictive temperatures. On the basis of these results, we propose that Vsm1 is a novel v-SNARE-interacting protein that appears to act as negative regulator of constitutive exocytosis. Moreover, this regulation appears specific to one of two parallel exocytic paths which are operant in yeast cells.

Indexed as

Saccharomyces cerevisiae ProteinsVesicular Transport ProteinsAmino Acid Sequencebeta-Fructofuranosidasebeta-GlucosidaseCarrier ProteinsCell MembraneCoated VesiclesExocytosisFluorescent Antibody TechniqueFungal ProteinsGene Expression Regulation, FungalGlucan 1,3-beta-GlucosidaseGlycoside HydrolasesImmunoblottingMembrane Proteinsbeta-Fructofuranosidasebeta-GlucosidaseCarrier ProteinsDDI1 protein, S cerevisiaeFungal ProteinsGlucan 1,3-beta-GlucosidaseGlycoside HydrolasesMembrane ProteinsR-SNARE ProteinsSaccharomyces cerevisiae ProteinsSNARE ProteinsSNC1 protein, S cerevisiaeSNC2 protein, S cerevisiaeVesicular Transport Proteins

Identifiers

PMID10330187
PMCPMC104406
OpenAlexW2159257811

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.