Evidence map›Paper›PMID 15067022›Full record

ArticleThe Journal of cell biology2004

Pheromone-induced polarization is dependent on the Fus3p MAPK acting through the formin Bni1p.

Dina Matheos, Metodi Metodiev, Eric Muller, David Stone, Mark D Rose

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

54 citing papers in PubMed, 115 citations in OpenAlex.

  1. Article
  2. Article
  3. The Macroevolution of Filamentation Morphology Across thebioRxiv : the preprint server for biology · 2025
    Article
  4. Role of Gα-MAPK interaction in mating ofMolecular biology of the cell · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Orientation of Cell Polarity by Chemical Gradients.Annual review of biophysics · 2022
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. 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
  18. Article
  19. Calcineurin, the CaMolecular biology of the cell · 2017
    Article
  20. 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

5 authors at 2 institutions in 1 country.

Dina MatheosDepartment of Molecular Biology, Princeton University, Princeton, NJ 08544-1014, USA.
Metodi Metodiev
Eric Muller
David Stone
Mark D Rose
Princeton University · USUniversity of Illinois Chicago · US

Funding

Mechanisms of Nuclear and Cell Fusion in YeastR01GM037739 · NIGMS · PRINCETON UNIVERSITY · PI ROSE, MARK DAVID · 1987 to 2016
$7.4M
NIGMS NIH HHS GM37739NIGMS NIH HHS R01 GM037739
6 · The paper itself

Abstract

During mating, budding yeast cells reorient growth toward the highest concentration of pheromone. Bni1p, a formin homologue, is required for this polarized growth by facilitating cortical actin cable assembly. Fus3p, a pheromone-activated MAP kinase, is required for pheromone signaling and cell fusion. We show that Fus3p phosphorylates Bni1p in vitro, and phosphorylation of Bni1p in vivo during the pheromone response is dependent on Fus3p. fus3 mutants exhibited multiple phenotypes similar to bni1 mutants, including defects in actin and cell polarization, as well as Kar9p and cytoplasmic microtubule localization. Disruption of the interaction between Fus3p and the receptor-associated Galpha subunit caused similar mutant phenotypes. After pheromone treatment, Bni1p-GFP and Spa2p failed to localize to the cortex of fus3 mutants, and cell wall growth became completely unpolarized. Bni1p overexpression suppressed the actin assembly, cell polarization, and cell fusion defects. These data suggest a model wherein activated Fus3p is recruited back to the cortex, where it activates Bni1p to promote polarization and cell fusion.

Indexed as

Actin CytoskeletonCell MovementCell PolarityCell SizeCytoskeletal ProteinsGene Expression Regulation, FungalGTP-Binding ProteinsMicrofilament ProteinsMicrotubulesMitogen-Activated Protein KinasesMutationNuclear ProteinsPheromonesPhosphorylationReproductionSaccharomyces cerevisiaeBni1 protein, S cerevisiaeCytoskeletal ProteinsFUS3 protein, S cerevisiaeGTP-Binding ProteinsKAR9 protein, S cerevisiaeMicrofilament ProteinsMitogen-Activated Protein KinasesNuclear ProteinsPheromonesSaccharomyces cerevisiae ProteinsSPA2 protein, S cerevisiae

Identifiers

PMID15067022
PMCPMC2172092
OpenAlexW2149705535

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.