Evidence map›Paper›PMID 10087263›Full record

ArticleThe Journal of cell biology1999

A Cdc24p-Far1p-Gbetagamma protein complex required for yeast orientation during mating.

A Nern, R A Arkowitz

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

95 citing papers in PubMed, 204 citations in OpenAlex.

  1. Role of Gα-MAPK interaction in mating ofMolecular biology of the cell · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Mechanism of commitment to a mating partner inMolecular biology of the cell · 2022
    Article
  9. Orientation of Cell Polarity by Chemical Gradients.Annual review of biophysics · 2022
    Review
  10. Article
  11. Article
  12. Chemotactic movement of a polarity site enables yeast cells to find their mates.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Mitotic and pheromone-specific intrinsic polarization cues interfere with gradient sensing inProceedings of the National Academy of Sciences of the United States of America · 2020
    Article

35 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

A NernDivision of Cell Biology, MRC Laboratory of Molecular Biology, Cambridge, CB2 2QH, United Kingdom.
R A Arkowitz
MRC Laboratory of Molecular Biology · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Oriented cell growth requires the specification of a site for polarized growth and subsequent orientation of the cytoskeleton towards this site. During mating, haploid Saccharomyces cerevisiae cells orient their growth in response to a pheromone gradient overriding an internal landmark for polarized growth, the bud site. This response requires Cdc24p, Far1p, and a heterotrimeric G-protein. Here we show that a two- hybrid interaction between Cdc24p and Gbeta requires Far1p but not pheromone-dependent MAP-kinase signaling, indicating Far1p has a role in regulating the association of Cdc24p and Gbeta. Binding experiments demonstrate that Cdc24p, Far1p, and Gbeta form a complex in which pairwise interactions can occur in the absence of the third protein. Cdc24p localizes to sites of polarized growth suggesting that this complex is localized. In the absence of CDC24-FAR1-mediated chemotropism, a bud site selection protein, Bud1p/Rsr1p, is essential for morphological changes in response to pheromone. These results suggest that formation of a Cdc24p-Far1p-Gbetagamma complex functions as a landmark for orientation of the cytoskeleton during growth towards an external signal.

Indexed as

GTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsGuanine Nucleotide Exchange FactorsHeterotrimeric GTP-Binding ProteinsRepressor ProteinsSaccharomyces cerevisiae ProteinsAmino Acid SequenceBinding SitesCell CycleCell Cycle ProteinsCyclin-Dependent Kinase Inhibitor ProteinsCytoskeletonFungal ProteinsGTP-Binding ProteinsMacromolecular SubstancesModels, BiologicalCDC24 protein, S cerevisiaeCell Cycle ProteinsCyclin-Dependent Kinase Inhibitor ProteinsFAR1 protein, S cerevisiaeFungal ProteinsG-protein Beta gammaGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsGTP-Binding ProteinsGuanine Nucleotide Exchange FactorsHeterotrimeric GTP-Binding ProteinsMacromolecular SubstancesPheromonesProto-Oncogene ProteinsRepressor ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID10087263
PMCPMC2150586
OpenAlexW1911465857

What OpenQuestion holds

Texttitle and abstract
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.