Evidence map›Paper›PMID 10069805›Full record

ArticleMolecular biology of the cell1999

GCS1, an Arf guanosine triphosphatase-activating protein in Saccharomyces cerevisiae, is required for normal actin cytoskeletal organization in vivo and stimulates actin polymerization in vitro.

I J Blader, M J Cope, T R Jackson, A A Profit, A F Greenwood, D G Drubin, G D Prestwich, A B Theibert

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

16 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
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  7. "Sleeping beauty": quiescence in Saccharomyces cerevisiae.Microbiology and molecular biology reviews : MMBR · 2004
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. The Arf GTPase-activating protein ASAP1 regulates the actin cytoskeleton.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Article
  15. Filling in the GAPs in the ADP-ribosylation factor story.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Article
  16. Article
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

8 authors at 5 institutions in 2 countries.

I J BladerDepartments of Neurobiology and Cell Biology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.
M J Cope
T R Jackson
A A Profit
A F Greenwood
D G Drubin
G D Prestwich
A B Theibert
University of Alabama at Birmingham · USUniversity of California, Berkeley · USBabraham Institute · GBState University of New York · USUniversity of Utah · US

Funding

Phosphoinositide and Inositol Polyphosphate ProbesR01NS029632 · NINDS · UNIVERSITY OF UTAH · PI PRESTWICH, GLENN DOWNES · 1992 to 2007
$2.5M
INOSITOL POLYPHOSPHATE RECEPTORSR29MH050102 · NIMH · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI THEIBERT, ANNE B · 1993 to 1997
–
NIMH NIH HHS R29 MH050102NINDS NIH HHS R01 NS029632
6 · The paper itself

Abstract

Recent cloning of a rat brain phosphatidylinositol 3,4, 5-trisphosphate binding protein, centaurin alpha, identified a novel gene family based on homology to an amino-terminal zinc-binding domain. In Saccharomyces cerevisiae, the protein with the highest homology to centaurin alpha is Gcs1p, the product of the GCS1 gene. GCS1 was originally identified as a gene conditionally required for the reentry of cells into the cell cycle after stationary phase growth. Gcs1p was previously characterized as a guanosine triphosphatase-activating protein for the small guanosine triphosphatase Arf1, and gcs1 mutants displayed vesicle-trafficking defects. Here, we have shown that similar to centaurin alpha, recombinant Gcs1p bound phosphoinositide-based affinity resins with high affinity and specificity. A novel GCS1 disruption strain (gcs1Delta) exhibited morphological defects, as well as mislocalization of cortical actin patches. gcs1Delta was hypersensitive to the actin monomer-sequestering drug, latrunculin-B. Synthetic lethality was observed between null alleles of GCS1 and SLA2, the gene encoding a protein involved in stabilization of the actin cytoskeleton. In addition, synthetic growth defects were observed between null alleles of GCS1 and SAC6, the gene encoding the yeast fimbrin homologue. Recombinant Gcs1p bound to actin filaments, stimulated actin polymerization, and inhibited actin depolymerization in vitro. These data provide in vivo and in vitro evidence that Gcs1p interacts directly with the actin cytoskeleton in S. cerevisiae.

Indexed as

GTPase-Activating ProteinsMicrofilament ProteinsSaccharomyces cerevisiae ProteinsActinsADP-Ribosylation Factor 1ADP-Ribosylation FactorsAmino Acid SequenceAnimalsBinding SitesCarrier ProteinsCytoskeletal ProteinsCytoskeletonDNA-Binding ProteinsFungal ProteinsGene DeletionGTP-Binding ProteinsActinsADP-Ribosylation Factor 1ADP-Ribosylation FactorsCarrier ProteinsCytoskeletal ProteinsDNA-Binding ProteinsFungal ProteinsGCS1 protein, S cerevisiaeGTPase-Activating ProteinsGTP-Binding ProteinsMembrane GlycoproteinsMicrofilament ProteinsPhosphatidylinositolsplastinSaccharomyces cerevisiae ProteinsSLA2 protein, S cerevisiaeZinc

Identifiers

PMID10069805
PMCPMC25189
OpenAlexW2119161370

What OpenQuestion holds

Texttitle and abstract
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.