Evidence map›Paper›PMID 18523008›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Yeast UCS proteins promote actomyosin interactions and limit myosin turnover in cells.

Matthew Lord, Thomas E Sladewski, Thomas D Pollard

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

22 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. 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
  5. Article
  6. Chaperone-enhanced purification of unconventional myosin 15, a molecular motor specialized for stereocilia protein trafficking.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  7. Myosin chaperones.Current opinion in structural biology · 2014
    Review
  8. The UNC-45 myosin chaperone: from worms to flies to vertebrates.International review of cell and molecular biology · 2014
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. UNC-45/CRO1/She4p (UCS) protein forms elongated dimer and joins two myosin heads near their actin binding region.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  18. Article
  19. Article
  20. 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

3 authors at 2 institutions in 2 countries.

Matthew LordDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405, USA.
Thomas E Sladewski
Thomas D Pollard
University of Vermont · USInstitut thématique Génétique, génomique et bioinformatique · FR

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

Two functions are proposed for the conserved family of UCS proteins: helping to fold myosin motor proteins and stimulating the motor function of folded myosins. We examined both functions in yeast. The fission yeast UCS protein (Rng3p) concentrates in nodes containing myosin-II (Myo2) and other proteins that condense into the cytokinetic contractile ring. Both the N-terminal (central) and C-terminal (UCS) domains of Rng3p can concentrate independently in contractile rings, but only full-length Rng3p supports contractile ring function in vivo. The presence of Rng3p in ATPase assays doubles the apparent affinity (K(ATPase)) of both native Myo2 and recombinant heads of Myo2 for actin filaments. Rng3p promotes gliding of actin filaments by full-length Myo2 molecules, but not Myo2 heads alone. Myo2 isolated from mutant strains defective for Rng3p function is soluble and supports actin filament gliding. In budding yeast the single UCS protein (She4p) acts on both myosin-I isoforms (Myo3p and Myo5p) and one of two myosin-V isoforms (Myo4p). Myo5p turns over approximately 10 times faster in she4Delta cells than wild-type cells, reducing the level of Myo5p in cells 10-fold and in cortical actin patches approximately 4-fold. Nevertheless, Myo5p isolated from she4Delta cells has wild-type ATPase and motility activities. Thus, a fraction of this yeast myosin can fold de novo in the absence of UCS proteins, but UCS proteins promote myosin stability and interactions with actin.

Indexed as

ActinsActomyosinAdenosine TriphosphatasesCytoskeletal ProteinsEnzyme ActivationMolecular Motor ProteinsMotionMutationMyosin Heavy ChainsMyosinsMyosin Type IMyosin Type IIMyosin Type VProtein BindingProtein Structure, TertiarySaccharomyces cerevisiaeActinsActomyosinAdenosine TriphosphatasesCytoskeletal ProteinsMolecular Motor ProteinsMYO2 protein, S cerevisiaeMYO2 protein, S pombeMYO5 protein, S cerevisiaeMyosin Heavy ChainsMyosinsMyosin Type IMyosin Type IIMyosin Type VRng3 protein, S pombeSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsSHE4 protein, S cerevisiae

Identifiers

PMID18523008
PMCPMC2430351
OpenAlexW1997266868

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.