Evidence map›Paper›PMID 25712463›Full record

ArticleCytoskeleton (Hoboken, N.J.)2015

Myosin motor isoforms direct specification of actomyosin function by tropomyosins.

Joseph E Clayton, Luther W Pollard, George G Murray, Matthew Lord

Abstract read
In one paragraph

Article in Cytoskeleton (Hoboken, N.J.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.5field-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

16 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Actin-tropomyosin distribution in non-muscle cells.Journal of muscle research and cell motility · 2020
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  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. Article
  15. Article
  16. Review
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 1 institution in 1 country.

Joseph E ClaytonDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, Vermont, United States of America.
Luther W Pollard
George G Murray
Matthew Lord
University of Vermont · 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 GM097193NIGMS NIH HHS R01 GM097193
6 · The paper itself

Abstract

Myosins and tropomyosins represent two cytoskeletal proteins that often work together with actin filaments in contractile and motile cellular processes. While the specialized role of tropomyosin in striated muscle myosin-II regulation is well characterized, its role in nonmuscle myosin regulation is poorly understood. We previously showed that fission yeast tropomyosin (Cdc8p) positively regulates myosin-II (Myo2p) and myosin-V (Myo52p) motors. To understand the broader implications of this regulation we examined the role of two mammalian tropomyosins (Tpm3.1cy/Tm5NM1 and Tpm4.2cy/Tm4) recently implicated in cancer cell proliferation and metastasis. Like Cdc8p, the Tpm3.1cy and Tpm4.2cy isoforms significantly enhance Myo2p and Myo52p motor activity, converting nonprocessive Myo52p molecules into processive motors that can walk along actin tracks as single molecules. In contrast to the positive regulation of Myo2p and Myo52p, Cdc8p and the mammalian tropomyosins potently inhibited skeletal muscle myosin-II, while having negligible effects on the highly processive mammalian myosin-Va. In support of a conserved role for certain tropomyosins in regulating nonmuscle actomyosin structures, Tpm3.1cy supported normal contractile ring function in fission yeast. Our work reveals that actomyosin regulation by tropomyosin is dependent on the myosin isoform, highlighting a general role for specific isoforms of tropomyosin in sorting myosin motor outputs.

Indexed as

Actin CytoskeletonActomyosinAdenosine TriphosphatasesCell Cycle ProteinsCell MovementCytoskeletal ProteinsEscherichia coliExonsGene Expression RegulationGreen Fluorescent ProteinsHumansMolecular Motor ProteinsMuscle, SkeletalMyosin Heavy ChainsMyosinsMyosin Type VActomyosinAdenosine TriphosphatasesCdc8 protein, S pombeCell Cycle ProteinsCytoskeletal ProteinsGreen Fluorescent ProteinsMolecular Motor ProteinsMyo52 protein, S pombeMYO5A protein, humanMyosin Heavy ChainsMyosinsMyosin Type VProtein IsoformsSchizosaccharomyces pombe ProteinsTropomyosinactinmotor sortingmyosin isoformsregulationtropomyosin isoforms

Identifiers

PMID25712463
PMCPMC4414888
OpenAlexW2137487074

What OpenQuestion holds

Textmetadata
LicenceTDM
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.