Evidence map›Paper›PMID 15047864›Full record

ArticleMolecular biology of the cell2004

The Sec1/Munc18 protein, Vps33p, functions at the endosome and the vacuole of Saccharomyces cerevisiae.

Shoba Subramanian, Carol A Woolford, Elizabeth W Jones

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

26 citing papers in PubMed, 61 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Membrane Tethering Complexes in the Endosomal System.Frontiers in cell and developmental biology · 2016
    Review
  5. Function and regulation of the endosomal fusion and fission machineries.Cold Spring Harbor perspectives in biology · 2014
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Vps-C complexes: gatekeepers of endolysosomal traffic.Current opinion in cell biology · 2009
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Rabs and their effectors: achieving specificity in membrane traffic.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Shoba SubramanianDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, USA. shoba@andrew.cmu.edu
Carol A Woolford
Elizabeth W Jones
Carnegie Mellon University · US

Funding

GENETIC ANALYSIS OF ENZYME PROCESSING AND LOCALIZATIONR01GM029713 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI JONES, ELIZABETH W · 1985 to 2002
$848k
NIGMS NIH HHS GM29713
6 · The paper itself

Abstract

The Sec1/Munc18 (SM) family of proteins is thought to impart compartmental specificity to vesicle fusion reactions. Here we report characterization of Vps33p, an SM family member previously thought to act exclusively at the vacuolar membrane with the vacuolar syntaxin Vam3p. Vacuolar morphology of vps33Delta cells resembles that of cells lacking both Vam3p and the endosomal syntaxin Pep12p, suggesting that Vps33p may function with these syntaxins at the vacuole and the endosome. Consistent with this, vps33 mutants secrete the Golgi precursor form of the vacuolar hydrolase CPY into the medium. We also demonstrate that Vps33p acts at other steps, for vps33 mutants show severe defects in endocytosis at the late endosome. At the endosome, Vps33p and other class C members exist as a complex with Vps8p, a protein previously known to act in transport between the late Golgi and the endosome. Vps33p also interacts with Pep12p, a known interactor of the SM protein Vps45p. High copy PEP7/VAC1 suppresses vacuolar morphology defects of vps33 mutants. These findings demonstrate that Vps33p functions at multiple trafficking steps and is not limited to action at the vacuolar membrane. This is the first report demonstrating the involvement of a single syntaxin with two SM proteins at the same organelle.

Indexed as

Adaptor Proteins, Signal TransducingCathepsin ACytoskeletal ProteinsEndocytosisEndosomesGene DeletionGlycosylationGolgi ApparatusMating FactorMembrane ProteinsMultiprotein ComplexesMunc18 ProteinsNerve Tissue ProteinsPeptidesProtein BindingProtein PrecursorsAdaptor Proteins, Signal TransducingCathepsin ACytoskeletal ProteinsMating FactorMembrane ProteinsMultiprotein ComplexesMunc18 ProteinsNerve Tissue ProteinsPEP12 protein, S cerevisiaePEP7 protein, S cerevisiaePeptidesProtein PrecursorsQa-SNARE ProteinsSaccharomyces cerevisiae ProteinsSEC1 protein, S cerevisiaeVAM3 protein, S cerevisiaeVesicular Transport ProteinsVPS33 protein, S cerevisiaeVPS8 protein, S cerevisiae

Identifiers

PMID15047864
PMCPMC420085
OpenAlexW2156827542

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.