Evidence map›Paper›PMID 22573890›Full record

ArticleMolecular biology of the cell2012

Fission yeast Cyk3p is a transglutaminase-like protein that participates in cytokinesis and cell morphogenesis.

Luther W Pollard, Masayuki Onishi, John R Pringle, Matthew Lord

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

20 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
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  4. Cleavage-furrow formation without F-actin inProceedings of the National Academy of Sciences of the United States of America · 2020
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  7. TwoThe Journal of cell biology · 2019
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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

4 authors at 2 institutions in 1 country.

Luther W PollardDepartment of Molecular Physiology & Biophysics, University of Vermont, Burlington, VT 05405, USA.
Masayuki Onishi
John R Pringle
Matthew Lord
Stanford University · USUniversity of Vermont · 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
Specification of actomyosin function in the cellR01GM097193 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI LOWEY, SUSAN · 2012 to 2016
$1.5M
GENETIC STUDY OF THE YEAST CELL CYCLER01GM031006 · NIGMS · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI PRINGLE, JOHN R · 1986 to 1999
–
NIGMS NIH HHS GM097193NIGMS NIH HHS GM31006NIGMS NIH HHS R01 GM031006NIGMS NIH HHS R01 GM097193NIGMS NIH HHS R37 GM031006
6 · The paper itself

Abstract

Cell morphogenesis is a complex process that relies on a diverse array of proteins and pathways. We have identified a transglutaminase-like protein (Cyk3p) that functions in fission yeast morphogenesis. The phenotype of a cyk3 knockout strain indicates a primary role for Cyk3p in cytokinesis. Correspondingly, Cyk3p localizes both to the actomyosin contractile ring and the division septum, promoting ring constriction, septation, and subsequent cell separation following ring disassembly. In addition, Cyk3p localizes to polarized growth sites and plays a role in cell shape determination, and it also appears to contribute to cell integrity during stationary phase, given its accumulation as dynamic puncta at the cortex of such cells. Our results and the conservation of Cyk3p across fungi point to a role in cell wall synthesis and remodeling. Cyk3p possesses a transglutaminase domain that is essential for function, even though it lacks the catalytic active site. In a wider sense, our work illustrates the physiological importance of inactive members of the transglutaminase family, which are found throughout eukaryotes. We suggest that the proposed evolution of animal transglutaminase cross-linking activity from ancestral bacterial thiol proteases was accompanied by the emergence of a subclass whose function does not depend on enzymatic activity.

Indexed as

CytokinesisMorphogenesisCell Cycle ProteinsCell PolarityContractile ProteinsGene Knockout TechniquesGreen Fluorescent ProteinsKineticsProtein Structure, TertiaryProtein TransportRecombinant Fusion ProteinsSchizosaccharomycesSchizosaccharomyces pombe ProteinsSequence DeletionSpindle ApparatusTime-Lapse ImagingCell Cycle ProteinsContractile ProteinsCyk3 protein, S pombeGreen Fluorescent ProteinsRecombinant Fusion ProteinsSchizosaccharomyces pombe Proteins

Identifiers

PMID22573890
PMCPMC3386208
OpenAlexW2116549724

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.