Evidence map›Paper›PMID 11598009›Full record

ArticleThe EMBO journal2001

Cdc42p functions at the docking stage of yeast vacuole membrane fusion.

O Müller, D I Johnson, A Mayer

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

38 citing papers in PubMed, 76 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Plant vacuole morphology and vacuolar trafficking.Frontiers in plant science · 2014
    Review
  8. Article
  9. GTPase networks in membrane traffic.Annual review of biochemistry · 2012
    Review
  10. Article
  11. Polarity proteins Bem1 and Cdc24 are components of the filamentous fungal NADPH oxidase complex.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  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.

O MüllerFriedrich-Miescher-Laboratorium der Max-Planck-Gesellschaft, Spemannstrasse 37-39, 72076 Tübingen, Germany.
D I Johnson
A Mayer
Friedrich Miescher Laboratory · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane fusion reactions have been considered to be primarily regulated by Rab GTPases. In the model system of homotypic vacuole fusion in the yeast Saccharomyces cerevisiae, we show that Cdc42p, a member of the Rho family of GTPases, has a direct role in membrane fusion. Genetic evidence suggested a relationship between Cdc42p and Vtc1p/Nrf1p, a central part of the vacuolar membrane fusion machinery. Vacuoles from cdc42 temperature-sensitive mutants are deficient for fusion at the restrictive temperature. Specific amino acid changes on the Cdc42p protein surface in these mutants define the putative interaction domain that is crucial for its function in membrane fusion. Affinity-purified antibodies to this domain inhibited the in vitro fusion reaction. Using these antibodies in kinetic analyses and assays for subreactions of the priming, docking and post-docking phase of the reaction, we show that Cdc42p action follows Ypt7p-dependent tethering, but precedes the formation of trans-SNARE complexes. Thus, our data define an effector binding domain of Cdc42p by which it regulates the docking reaction of vacuole fusion.

Indexed as

Adenosine TriphosphatasesSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsAllelesCalciumCarrier Proteinscdc42 GTP-Binding Protein, Saccharomyces cerevisiaeChelating AgentsEgtazic AcidFungal ProteinsGuanosine 5'-O-(3-Thiotriphosphate)Macromolecular SubstancesMembrane FusionMembrane ProteinsMolecular ChaperonesProtein Transport1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acidAdenosine TriphosphatasesCalciumCarrier Proteinscdc42 GTP-Binding Protein, Saccharomyces cerevisiaeChelating AgentsEgtazic AcidFungal ProteinsGuanosine 5'-O-(3-Thiotriphosphate)Macromolecular SubstancesMembrane ProteinsMolecular Chaperonesrab GTP-Binding ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSEC17 protein, S cerevisiaeSEC18 protein, S cerevisiaeSNARE ProteinsSoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsVesicular Transport ProteinsVTC1 protein, S cerevisiaeYPT7 protein, S cerevisiae

Identifiers

PMID11598009
PMCPMC125663
OpenAlexW1976127915

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.