Evidence map›Paper›PMID 7579704›Full record

ArticleMolecular biology of the cell1995

The rho-GAP encoded by BEM2 regulates cytoskeletal structure in budding yeast.

T Wang, A Bretscher

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

31 citing papers in PubMed, 64 citations in OpenAlex.

  1. Integrative Phosphoproteomic and Proteomic Analysis ofJournal of proteome research · 2025
    Article
  2. Journal of fungi (Basel, Switzerland) · 2022
    Article
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  9. Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  10. Article
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  15. Osmotic stress signaling and osmoadaptation in yeasts.Microbiology and molecular biology reviews : MMBR · 2002
    Review
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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.

T WangSection of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853, USA.
A Bretscher
Cornell University · US

Funding

MICROFILAMENTS IN THE YEAST SACCHAROMYCES CEREVISIAER01GM039066 · NIGMS · CORNELL UNIVERSITY ITHACA · PI BRETSCHER, ANTHONY P. · 1988 to 2018
$7.3M
PROTEINS IMPORTANT FOR TROPOMYOSIN FUNCTION IN YEASTF32GM017018 · NIGMS · CORNELL UNIVERSITY ITHACA · PI WANG, TONGTONG · 1994 to 1995
–
NIGMS NIH HHS 1F32GM-17018NIGMS NIH HHS GM-39066
6 · The paper itself

Abstract

Microfilaments are required for polarized growth and morphogenesis in Saccharomyces cerevisiae. To accomplish this, actin cables and patches are redistributed during the cell cycle to direct secretory components to appropriate sites for cell growth. A major component of actin cables is tropomyosin I, encoded by TPM1, that determines or stabilizes these structures. Disruption of TPM1 is not lethal but results in the loss of actin cables and confers a partial defect in polarized secretion. Using a synthetic lethal screen, we have identified seven mutations residing in six genes whose products are required in the absence of Tpm1p. Each mutant exhibited a morphological defect, suggesting a functional link to the actin cytoskeleton. Complementation cloning of one mutation revealed that it lies in BEM2, which encodes a GTPase-activating protein for the RHO1 product. bem2 mutations also show synthetic lethality with rho1 and mutations in certain other cytoskeletal genes (ACT1, MYO1, MYO2, and SAC6) but not with mutations in several noncytoskeletal genes. These data therefore provide a genetic link between the GAP encoded by BEM2 and the functional organization of microfilaments. In addition, we show that bem2 mutations confer benomyl sensitivity and have abnormal microtubule arrays, suggesting that the BEM2 product may also be involved directly or indirectly in regulating microtubule function.

Indexed as

rho GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsActin CytoskeletonActinsBenomylCytoskeletonFungal ProteinsGenes, FungalGenes, LethalGenetic Complementation TestGTPase-Activating ProteinsGTP-Binding ProteinsMicrotubulesMutationProteinsSaccharomyces cerevisiaeActinsBEM2 protein, S cerevisiaeBenomylFungal ProteinsGTPase-Activating ProteinsGTP-Binding ProteinsProteinsRHO1 protein, S cerevisiaerho GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsTropomyosin

Identifiers

PMID7579704
PMCPMC301259
OpenAlexW2169811658

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.