Evidence map›Paper›PMID 12810699›Full record

ArticleThe Journal of cell biology2003

Formin-dependent actin assembly is regulated by distinct modes of Rho signaling in yeast.

Yuqing Dong, David Pruyne, Anthony Bretscher

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

71 citing papers in PubMed, 161 citations in OpenAlex.

  1. Article
  2. Cryo-EM structure revealed a novel F-actin binding motif in abioRxiv : the preprint server for biology · 2025
    Article
  3. Article
  4. Roles for the canonical polarity machinery in thebioRxiv : the preprint server for biology · 2025
    Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Mechanics and regulation of cytokinesis in budding yeast.Seminars in cell & developmental biology · 2017
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. STRIPAK complexes: structure, biological function, and involvement in human diseases.The international journal of biochemistry & cell biology · 2014
    Review

11 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

3 authors at 1 institution in 1 country.

Yuqing DongDepartment of Molecular Biology and Genetics, Cornell University, 353 Biotechnology Building, Ithaca, NY 14853, USA.
David Pruyne
Anthony Bretscher
Cornell University · US

Funding

MICROFILAMENTS IN THE YEAST SACCHAROMYCES CEREVISIAER01GM039066 · NIGMS · CORNELL UNIVERSITY ITHACA · PI BRETSCHER, ANTHONY P. · 1988 to 2018
$7.3M
NIGMS NIH HHS GM39066NIGMS NIH HHS R01 GM039066
6 · The paper itself

Abstract

Formins are actin filament nucleators regulated by Rho-GTPases. In budding yeast, the formins Bni1p and Bnr1p direct the assembly of actin cables, which guide polarized secretion and growth. From the six yeast Rho proteins (Cdc42p and Rho1-5p), we have determined that four participate in the regulation of formin activity. We show that the essential function of Rho3p and Rho4p is to activate the formins Bni1p and Bnr1p, and that activated alleles of either formin are able to bypass the requirement for these Rho proteins. Through a separate signaling pathway, Rho1p is necessary for formin activation at elevated temperatures, acting through protein kinase C (Pkc1p), the major effector for Rho1p signaling to the actin cytoskeleton. Although Pkc1p also activates a MAPK pathway, this pathway does not function in formin activation. Formin-dependent cable assembly does not require Cdc42p, but in the absence of Cdc42p function, cable assembly is not properly organized during initiation of bud growth. These results show that formin function is under the control of three distinct, essential Rho signaling pathways.

Indexed as

Cytoskeletal ProteinsActin CytoskeletonCarrier Proteinscdc42 GTP-Binding Protein, Saccharomyces cerevisiaeCells, CulturedGTP-Binding ProteinsMicrofilament ProteinsProtein Kinase Crho GTP-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionTemperatureBni1 protein, S cerevisiaeBNR1 protein, S cerevisiaeCarrier Proteinscdc42 GTP-Binding Protein, Saccharomyces cerevisiaeCytoskeletal ProteinsGTP-Binding ProteinsMicrofilament ProteinsProtein Kinase CRHO1 protein, S cerevisiaeRHO3 protein, S cerevisiaeRHO4 protein, S cerevisiaerho GTP-Binding ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID12810699
PMCPMC2173006
OpenAlexW1979145729

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.