Evidence map›Paper›PMID 10637292›Full record

ArticleMolecular biology of the cell2000

Myosin-II tails confer unique functions in Schizosaccharomyces pombe: characterization of a novel myosin-II tail.

M Bezanilla, T D Pollard

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

32 citing papers in PubMed, 57 citations in OpenAlex.

  1. Review
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  8. Interacting-heads motif has been conserved as a mechanism of myosin II inhibition since before the origin of animals.Proceedings of the National Academy of Sciences of the United States of America · 2018
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  9. Review
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  13. Fission yeast myosin Myo2 is down-regulated in actin affinity by light chain phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  14. Response to Zambon et al.Current biology : CB · 2017
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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

2 authors at 1 institution in 1 country.

M BezanillaBiochemistry Cellular and Molecular Biology Graduate Program, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
T D Pollard
Salk Institute for Biological Studies · US

Funding

Mechanism of cytokinesis in fission yeastR01GM026132 · NIGMS · YALE UNIVERSITY · PI POLLARD, THOMAS D. · 1985 to 2021
$8.8M
ACTIN-MYOSIN INTERACTIONS IN CELL MOTILITYR37GM026132 · NIGMS · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI POLLARD, THOMAS D. · 1988 to 1997
–
NIGMS NIH HHS GM-26132NIGMS NIH HHS R01 GM026132NIGMS NIH HHS R37 GM026132
6 · The paper itself

Abstract

Schizosaccharomyces pombe has two myosin-IIs, Myo2p and Myp2p, which both concentrate in the cleavage furrow during cytokinesis. We studied the phenotype of mutant myosin-II strains to examine whether these myosins have overlapping functions in the cell. myo2(+) is essential. myp2(+) cannot rescue loss of myo2(+) even at elevated levels of expression. myp2(+) is required under specific nutritional conditions; thus myo2(+) cannot rescue under these conditions. Studies with chimeras show that the tails rather than the structurally similar heads determine the gene-specific functions of myp2(+) and myo2(+). The Myo2p tail is a rod-shaped coiled-coil dimer that aggregates in low salt like other myosin-II tails. The Myp2p tail is monomeric in high salt and is insoluble in low salt. Biophysical properties of the full-length Myp2p tail and smaller subdomains indicate that two predicted coiled-coil regions fold back on themselves to form a rod-shaped antiparallel coiled coil. This suggests that Myp2p is the first type II myosin with only one head. The C-terminal two-thirds of Myp2p tail are essential for function in vivo and may interact with components of the salt response pathway.

Indexed as

Myosin Heavy ChainsMyosin Type IIMyosin Type VSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsAnimalsBinding SitesFungal ProteinsHumansMyosinsSchizosaccharomycesFungal ProteinsMYO2 protein, S cerevisiaeMYO2 protein, S pombeMyosin Heavy ChainsMyosinsMyosin Type IIMyosin Type VSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe Proteins

Identifiers

PMID10637292
PMCPMC14758
OpenAlexW2167786003

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.