Evidence map›Paper›PMID 24361582›Full record

ArticleJournal of structural biology2014

Role of the essential light chain in the activation of smooth muscle myosin by regulatory light chain phosphorylation.

Kenneth A Taylor, Michael Feig, Charles L Brooks, Patricia M Fagnant, Susan Lowey, Kathleen M Trybus

Abstract read
In one paragraph

Article in Journal of structural biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

14 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  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. Effect of ATP and regulatory light-chain phosphorylation on the polymerization of mammalian nonmuscle myosin II.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Amplitude of the actomyosin power stroke depends strongly on the isoform of the myosin essential light chain.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  13. Article
  14. 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

6 authors at 3 institutions in 1 country.

Kenneth A TaylorThe Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306-4380, United States. Electronic address: taylor@bio.fsu.edu.
Michael FeigDepartment of Molecular Biology, TPC6, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States.
Charles L BrooksDepartment of Molecular Biology, TPC6, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States.
Patricia M FagnantHealth Science Research Facility 130, 149 Beaumont Avenue, Department of Molecular Physiology & Biophysics, University of Vermont, Burlington, VT 05405, United States.
Susan LoweyHealth Science Research Facility 130, 149 Beaumont Avenue, Department of Molecular Physiology & Biophysics, University of Vermont, Burlington, VT 05405, United States.
Kathleen M TrybusHealth Science Research Facility 130, 149 Beaumont Avenue, Department of Molecular Physiology & Biophysics, University of Vermont, Burlington, VT 05405, United States.
University of Vermont · USScripps Research Institute · USFlorida State University · US

Funding

WEB BASED DOCUMENTATION &TUTORIALS FOR YAMMPP41RR012255 · NCRR · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI BROOKS, CHARLES L · 1997 to 2009
$10.4M
SMOOTH MUSCLE MYOSIN--CONFORMATION AND ACTIVITYR01HL038113 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI TRYBUS, KATHLEEN M · 1993 to 2011
$3.9M
EM Studies of Dimeric Molecular MotorsR01AR047421 · NIAMS · FLORIDA STATE UNIVERSITY · PI TAYLOR, KENNETH ALLEN · 2001 to 2011
$2.6M
MYOSIN DOMAIN INTERACTIONS DURING THE CONTRACTILE CYCLER01AR053975 · NIAMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI LOWEY, SUSAN · 2007 to 2011
$1.9M
VASCULAR SMOOTH MUSCLE MYOSIN--CONFORMATION &ACTIVITYR29HL038113 · NHLBI · BRANDEIS UNIVERSITY · PI TRYBUS, KATHLEEN M · 1987 to 1991
–
NCRR NIH HHS P41 RR012255NCRR NIH HHS RR12255NHLBI NIH HHS HL38113NHLBI NIH HHS R01 HL038113NIAMS NIH HHS AR47421NIAMS NIH HHS AR53975NIAMS NIH HHS R01 AR047421NIAMS NIH HHS R01 AR053975
6 · The paper itself

Abstract

The activity of smooth and non-muscle myosin II is regulated by phosphorylation of the regulatory light chain (RLC) at serine 19. The dephosphorylated state of full-length monomeric myosin is characterized by an asymmetric intramolecular head-head interaction that completely inhibits the ATPase activity, accompanied by a hairpin fold of the tail, which prevents filament assembly. Phosphorylation of serine 19 disrupts these head-head interactions by an unknown mechanism. Computational modeling (Tama et al., 2005. J. Mol. Biol. 345, 837-854) suggested that formation of the inhibited state is characterized by both torsional and bending motions about the myosin heavy chain (HC) at a location between the RLC and the essential light chain (ELC). Therefore, altering relative motions between the ELC and the RLC at this locus might disrupt the inhibited state. Based on this hypothesis we have derived an atomic model for the phosphorylated state of the smooth muscle myosin light chain domain (LCD). This model predicts a set of specific interactions between the N-terminal residues of the RLC with both the myosin HC and the ELC. Site directed mutagenesis was used to show that interactions between the phosphorylated N-terminus of the RLC and helix-A of the ELC are required for phosphorylation to activate smooth muscle myosin.

Indexed as

Computational BiologyMyosin Light ChainsPhosphorylationSmooth Muscle MyosinsMyosin Light ChainsSmooth Muscle MyosinsATPaseModelingMotilityPhosphorylation

Identifiers

PMID24361582
PMCPMC4065857
OpenAlexW1985145950

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.