Evidence map›Paper›PMID 24244528›Full record

ArticlePloS one2013

UCS protein Rng3p is essential for myosin-II motor activity during cytokinesis in fission yeast.

Benjamin C Stark, Michael L James, Luther W Pollard, Vladimir Sirotkin, Matthew Lord

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.0field-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

11 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. TheJournal of cell science · 2019
    Article
  6. Article
  7. Review
  8. Article
  9. 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
  10. Article
  11. 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

5 authors at 2 institutions in 1 country.

Benjamin C StarkDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, Vermont, United States of America.
Michael L James
Luther W Pollard
Vladimir Sirotkin
Matthew Lord
University of Vermont · USSUNY Upstate Medical University · US

Funding

Specification of actomyosin function in the cellR01GM097193 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI LOWEY, SUSAN · 2012 to 2016
$1.5M
NIGMS NIH HHS R01 GM097193NIGMS NIH HHS R01: GM097193
6 · The paper itself

Abstract

UCS proteins have been proposed to operate as co-chaperones that work with Hsp90 in the de novo folding of myosin motors. The fission yeast UCS protein Rng3p is essential for actomyosin ring assembly and cytokinesis. Here we investigated the role of Rng3p in fission yeast myosin-II (Myo2p) motor activity. Myo2p isolated from an arrested rng3-65 mutant was capable of binding actin, yet lacked stability and activity based on its expression levels and inactivity in ATPase and actin filament gliding assays. Myo2p isolated from a myo2-E1 mutant (a mutant hyper-sensitive to perturbation of Rng3p function) showed similar behavior in the same assays and exhibited an altered motor conformation based on limited proteolysis experiments. We propose that Rng3p is not required for the folding of motors per se, but instead works to ensure the activity of intrinsically unstable myosin-II motors. Rng3p is specific to conventional myosin-II and the actomyosin ring, and is not required for unconventional myosin motor function at other actin structures. However, artificial destabilization of myosin-I motors at endocytic actin patches (using a myo1-E1 mutant) led to recruitment of Rng3p to patches. Thus, while Rng3p is specific to myosin-II, UCS proteins are adaptable and can respond to changes in the stability of other myosin motors.

Indexed as

Amino Acid SequenceCytokinesisModels, MolecularMolecular Sequence DataMutationMyosin Type IIProtein ConformationSchizosaccharomycesSchizosaccharomyces pombe ProteinsSequence AlignmentMyosin Type IISchizosaccharomyces pombe Proteins

Identifiers

PMID24244528
PMCPMC3828377
OpenAlexW2070640564

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.