Evidence map›Paper›PMID 15075373›Full record

ArticleMolecular biology of the cell2004

Deficiencies in the endoplasmic reticulum (ER)-membrane protein Gab1p perturb transfer of glycosylphosphatidylinositol to proteins and cause perinuclear ER-associated actin bar formation.

Stephen J Grimme, Xiang-Dong Gao, Paul S Martin, Kim Tu, Serguei E Tcheperegine, Kathleen Corrado, Anne E Farewell, Peter Orlean, Erfei Bi

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.0field-weighted citation impact, top 28% 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

12 citing papers in PubMed, 34 citations in OpenAlex.

  1. Molecular Insights into Fungal Glycosylphosphatidylinositol Transamidase Complex.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. The proteomic response ofmicroLife · 2025
    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

9 authors at 3 institutions in 2 countries.

Stephen J GrimmeDepartment of Microbiology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.
Xiang-Dong Gao
Paul S Martin
Kim Tu
Serguei E Tcheperegine
Kathleen Corrado
Anne E Farewell
Peter Orlean
Erfei Bi
University of Pennsylvania · USUniversity of Illinois Urbana-Champaign · USUniversity of Michigan · US

Funding

MORPHOGENESIS AND CYTOKINESIS IN THE YEAST CELL CYCLER37GM031006 · NIGMS · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI PRINGLE, JOHN R · 2000 to 2010
$4.8M
SIGNALING MECHANISMS IN CELL POLARITY IN YEASTR01GM059216 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI BI, ERFEI · 1999 to 2012
$3.8M
PATHWAYS FOR GLYCOSYLPHOSPHATIDYLINOSITOL ASSEMBLYR01GM046220 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI ORLEAN, PETER AB · 1991 to 2003
$1.1M
GENETIC STUDY OF THE YEAST CELL CYCLER01GM031006 · NIGMS · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI PRINGLE, JOHN R · 1986 to 1999
–
NIGMS NIH HHS GM-31006NIGMS NIH HHS GM-46220NIGMS NIH HHS GM-59216NIGMS NIH HHS R01 GM031006NIGMS NIH HHS R01 GM046220NIGMS NIH HHS R01 GM059216NIGMS NIH HHS R37 GM031006
6 · The paper itself

Abstract

The essential GAB1 gene, which encodes an endoplasmic reticulum (ER)-membrane protein, was identified in a screen for mutants defective in cellular morphogenesis. A temperature-sensitive gab1 mutant accumulates complete glycosylphosphatidylinositol (GPI) precursors, and its temperature sensitivity is suppressed differentially by overexpression of different subunits of the GPI transamidase, from strong suppression by Gpi8p and Gpi17p, to weak suppression by Gaa1p, and to no suppression by Gpi16p. In addition, both Gab1p and Gpi17p localize to the ER and are in the same protein complex in vivo. These findings suggest that Gab1p is a subunit of the GPI transamidase with distinct relationships to other subunits in the same complex. We also show that depletion of Gab1p or Gpi8p, but not Gpi17p, Gpi16p, or Gaa1p causes accumulation of cofilin-decorated actin bars that are closely associated with the perinuclear ER, which highlights a functional interaction between the ER network and the actin cytoskeleton.

Indexed as

ActinsAcyltransferasesAllelesAmino Acid SequenceCell MembraneCell PolarityCloning, MolecularConserved SequenceEndoplasmic ReticulumGene DeletionGenes, EssentialGlycosylphosphatidylinositolsMembrane ProteinsMolecular Sequence DataProtein BindingProtein SubunitsActinsAcyltransferasesCOOH-terminal signal transamidaseGlycosylphosphatidylinositolsMembrane ProteinsProtein SubunitsSaccharomyces cerevisiae Proteins

Identifiers

PMID15075373
PMCPMC420100
OpenAlexW2098159200

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.