Evidence map›Paper›PMID 11294907›Full record

ArticleMolecular biology of the cell2001

Roles of a fimbrin and an alpha-actinin-like protein in fission yeast cell polarization and cytokinesis.

J Q Wu, J Bähler, J R Pringle

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

85 citing papers in PubMed, 154 citations in OpenAlex.

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  8. The role of the cytoskeleton in fibrotic diseases.Frontiers in cell and developmental biology · 2024
    Review
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25 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 2 countries.

J Q WuDepartment of Biology and Program in Molecular Biology and Biotechnology, University of North Carolina, Chapel Hill 27599, USA.
J Bähler
J R Pringle
University of North Carolina at Chapel Hill · 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
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 R01 GM031006NIGMS NIH HHS R37 GM031006
6 · The paper itself

Abstract

Eukaryotic cells contain many actin-interacting proteins, including the alpha-actinins and the fimbrins, both of which have actin cross-linking activity in vitro. We report here the identification and characterization of both an alpha-actinin-like protein (Ain1p) and a fimbrin (Fim1p) in the fission yeast Schizosaccharomyces pombe. Ain1p localizes to the actomyosin-containing medial ring in an F-actin-dependent manner, and the Ain1p ring contracts during cytokinesis. ain1 deletion cells have no obvious defects under normal growth conditions but display severe cytokinesis defects, associated with defects in medial-ring and septum formation, under certain stress conditions. Overexpression of Ain1p also causes cytokinesis defects, and the ain1 deletion shows synthetic effects with other mutations known to affect medial-ring positioning and/or organization. Fim1p localizes both to the cortical actin patches and to the medial ring in an F-actin-dependent manner, and several lines of evidence suggest that Fim1p is involved in polarization of the actin cytoskeleton. Although a fim1 deletion strain has no detectable defect in cytokinesis, overexpression of Fim1p causes a lethal cytokinesis defect associated with a failure to form the medial ring and concentrate actin patches at the cell middle. Moreover, an ain1 fim1 double mutant has a synthetical-lethal defect in medial-ring assembly and cell division. Thus, Ain1p and Fim1p appear to have an overlapping and essential function in fission yeast cytokinesis. In addition, protein-localization and mutant-phenotype data suggest that Fim1p, but not Ain1p, plays important roles in mating and in spore formation.

Indexed as

Microfilament ProteinsSchizosaccharomyces pombe ProteinsActininActinsAmino Acid SequenceAnimalsBase SequenceCell DivisionCell PolarityDNA, FungalFungal ProteinsMembrane GlycoproteinsMolecular Sequence DataMutagenesisSchizosaccharomycesActininActinsain1 protein, S pombeDNA, FungalFungal ProteinsMembrane GlycoproteinsMicrofilament ProteinsplastinSchizosaccharomyces pombe Proteins

Identifiers

PMID11294907
PMCPMC32287
OpenAlexW2149909679

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.