Evidence map›Paper›PMID 17210951›Full record

ArticleThe Journal of cell biology2007

The Golgi-resident protease Kex2 acts in conjunction with Prm1 to facilitate cell fusion during yeast mating.

Maxwell G Heiman, Alex Engel, Peter Walter

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

16 citing papers in PubMed, 38 citations in OpenAlex.

  1. Gut microbes · 2025
    Article
  2. Article
  3. Deletion of theMicroorganisms · 2020
    Article
  4. Article
  5. Cell biology of yeast zygotes, from genesis to budding.Biochimica et biophysica acta · 2015
    Review
  6. Article
  7. Article
  8. Genetic basis of cell-cell fusion mechanisms.Trends in genetics : TIG · 2013
    Review
  9. Review
  10. Article
  11. Structure of sterol aliphatic chains affects yeast cell shape and cell fusion during mating.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  12. Prm1 functions as a disulfide-linked complex in yeast mating.The Journal of biological chemistry · 2010
    Article
  13. Article
  14. Article
  15. Article
  16. Review
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.

Maxwell G HeimanHoward Hughes Medical Institute, Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158, USA.
Alex Engel
Peter Walter
University of California, San Francisco · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The molecular machines that mediate cell fusion are unknown. Previously, we identified a multispanning transmembrane protein, Prm1 (pheromone-regulated membrane protein 1), that acts during yeast mating (Heiman, M.G., and P. Walter. 2000. J. Cell Biol. 151:719-730). Without Prm1, a substantial fraction of mating pairs arrest with their plasma membranes tightly apposed yet unfused. In this study, we show that lack of the Golgi-resident protease Kex2 strongly enhances the cell fusion defect of Prm1-deficient mating pairs and causes a mild fusion defect in otherwise wild-type mating pairs. Lack of the Kex1 protease but not the Ste13 protease results in similar defects. Deltakex2 and Deltakex1 fusion defects were suppressed by osmotic support, a trait shared with mutants defective in cell wall remodeling. In contrast, other cell wall mutants do not enhance the Deltaprm1 fusion defect. Electron microscopy of Deltakex2-derived mating pairs revealed novel extracellular blebs at presumptive sites of fusion. Kex2 and Kex1 may promote cell fusion by proteolytically processing substrates that act in parallel to Prm1 as an alternative fusion machine, as cell wall components, or both.

Indexed as

Adenosine TriphosphatasesCarboxypeptidasesCation Transport ProteinsCell MembraneCell WallCongo RedCytoplasmic VesiclesCytoskeletal ProteinsDipeptidyl-Peptidases and Tripeptidyl-PeptidasesFungal ProteinsGlucan 1,3-beta-GlucosidaseGlycoproteinsGolgi ApparatusHeat-Shock ProteinsMembrane FusionMembrane ProteinsAdenosine Triphosphatasescarboxypeptidase DCarboxypeptidasesCation Transport ProteinsCongo RedCytoskeletal ProteinsDipeptidyl-Peptidases and Tripeptidyl-PeptidasesENA1 protein, S cerevisiaeEXG1 protein, S cerevisiaeFungal ProteinsFUS1 protein, S cerevisiaeFUS2 protein, S cerevisiaeGlucan 1,3-beta-GlucosidaseGlycoproteinsHeat-Shock ProteinsHSP150 protein, S cerevisiaeKEX2 protein, S cerevisiaeMembrane ProteinsMitogen-Activated Protein KinasesPIR1 protein, S cerevisiaePRM1 protein, S cerevisiaeProprotein ConvertasesSaccharomyces cerevisiae ProteinsSLT2 protein, S cerevisiaeSodium-Potassium-Exchanging ATPaseSTE13 protein, S cerevisiae

Identifiers

PMID17210951
PMCPMC2063940
OpenAlexW2156440600

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.