Evidence map›Paper›PMID 7962097›Full record

ArticleThe Journal of cell biology1994

Control of cellular morphogenesis by the Ip12/Bem2 GTPase-activating protein: possible role of protein phosphorylation.

Y J Kim, L Francisco, G C Chen, E Marcotte, C S Chan

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
3.8field-weighted citation impact, top 5% 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

51 citing papers in PubMed, 85 citations in OpenAlex.

  1. Journal of fungi (Basel, Switzerland) · 2022
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  8. PP2A(Cdc55) regulates G1 cyclin stability.Cell cycle (Georgetown, Tex.) · 2013
    Article
  9. Article
  10. Review
  11. Exploring transcription regulation through cell-to-cell variability.Proceedings of the National Academy of Sciences of the United States of America · 2011
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  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
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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

5 authors at 1 institution in 1 country.

Y J KimDepartment of Microbiology, University of Texas, Austin 78712.
L Francisco
G C Chen
E Marcotte
C S Chan
The University of Texas at Austin · US

Funding

MOLECULAR ANALYSIS OF CHROMOSOME SEGREGATION IN YEASTR01GM045185 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI CHAN, CLARENCE S · 1991 to 1999
–
NIGMS NIH HHS GM45185
6 · The paper itself

Abstract

The IPL2 gene is known to be required for normal polarized cell growth in the budding yeast Saccharomyces cerevisiae. We now show that IPL2 is identical to the previously identified BEM2 gene. bem2 mutants are defective in bud site selection at 26 degrees C and localized cell surface growth and organization of the actin cytoskeleton at 37 degrees C. BEM2 encodes a protein with a COOH-terminal domain homologous to sequences found in several GTPase-activating proteins, including human Bcr. The GTPase-activating protein-domain from the Bem2 protein (Bem2p) or human Bcr can functionally substitute for Bem2p. The Rho1 and Rho2 GTPases are the likely in vivo targets of Bem2p because bem2 mutant phenotypes can be partially suppressed by increasing the gene dosage of RHO1 or RHO2. CDC55 encodes the putative regulatory B subunit of protein phosphatase 2A, and mutations in BEM2 have previously been identified as suppressors of the cdc55-1 mutation. We show here that mutations in the previously identified GRR1 gene can suppress bem2 mutations. grr1 and cdc55 mutants are both elongated in shape and cold-sensitive for growth, and cells lacking both GRR1 and CDC55 exhibit a synthetic lethal phenotype. bem2 mutant phenotypes also can be suppressed by the SSD1-vl (also known as SRK1) mutation, which was shown previously to suppress mutations in the protein phosphatase-encoding SIT4 gene. Cells lacking both BEM2 and SIT4 exhibit a synthetic lethal phenotype even in the presence of the SSD1-v1 suppressor. These genetic interactions together suggest that protein phosphorylation and dephosphorylation play an important role in the BEM2-mediated process of polarized cell growth.

Indexed as

Carrier ProteinsCell Cycle ProteinsGTPase-Activating ProteinsMonomeric GTP-Binding Proteinsrho GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsUbiquitin-Protein LigasesAmino Acid SequenceBase SequenceCell DivisionCell PolarityChitinEnzyme ActivationF-Box ProteinsFungal ProteinsGenes, FungalBEM2 protein, S cerevisiaeCarrier ProteinsCDC55 protein, S cerevisiaeCell Cycle ProteinsChitinF-Box ProteinsFungal ProteinsGRR1 protein, S cerevisiaeGTPase-Activating ProteinsGTP-Binding ProteinsGTP PhosphohydrolasesMonomeric GTP-Binding ProteinsProtein Phosphatase 2RHO1 protein, S cerevisiaeRHO2 protein, S cerevisiaerho GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligases

Identifiers

PMID7962097
PMCPMC2120258
OpenAlexW2151702365

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.