Evidence map›Paper›PMID 25264102›Full record

ArticleBiochemical and biophysical research communications2014

Redox-sensitive residue in the actin-binding interface of myosin.

Rebecca J Moen, Sinziana Cornea, Daniel E Oseid, Benjamin P Binder, Jennifer C Klein, David D Thomas

Abstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.8field-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

15 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Unique methionine-aromatic interactions govern the calmodulin redox sensor.Biochemical and biophysical research communications · 2018
    Article
  10. Review
  11. Article
  12. S-Glutathionylation and Redox Protein Signaling in Drug Addiction.Progress in molecular biology and translational science · 2016
    Article
  13. Impact of methionine oxidation on calmodulin structural dynamics.Biochemical and biophysical research communications · 2015
    Article
  14. The myosin super-relaxed state is disrupted by estradiol deficiency.Biochemical and biophysical research communications · 2015
    Article
  15. 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 2 institutions in 1 country.

Rebecca J MoenDepartment of Chemistry and Geology, Minnesota State University, Mankato, MN 56001, United States.
Sinziana CorneaDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, United States.
Daniel E OseidDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, United States.
Benjamin P BinderDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, United States.
Jennifer C KleinDepartment of Biology, University of Wisconsin, Lacrosse, Lacrosse, MN 54601, United States.
David D ThomasDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, United States. Electronic address: ddt@umn.edu.
University of Minnesota · USMinnesota State University, Mankato · US

Funding

TRAINING PROGRAM IN MUSCLE RESEARCHT32AR007612 · NIAMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI JAMES M ERVASTI, DAWN A LOWE · 2001 to 2026
$11.3M
Structural Dynamics of Muscle ContractionR01AR032961 · NIAMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI THOMAS, DAVID D · 1986 to 2018
$8.0M
Site-Directed Oxidative Modification of Muscle Protein Structural DynamicsR37AG026160 · NIA · UNIVERSITY OF MINNESOTA · PI THOMAS, DAVID D · 2011 to 2020
$4.5M
Structural and functional effects of site-directed oxidative modification of myosF31AG037303 · NIA · UNIVERSITY OF MINNESOTA · PI MOEN, REBECCA J · 2010 to 2013
$111k
NIAMS NIH HHS R01 AR032961NIAMS NIH HHS T32 AR007612NIA NIH HHS F31 AG037303NIA NIH HHS R37 AG026160
6 · The paper itself

Abstract

We have examined the chemical and functional reversibility of oxidative modification in myosin. Redox regulation has emerged as a crucial modulator of protein function, with particular relevance to aging. We previously identified a single methionine residue in Dictyostelium discoideum (Dicty) myosin II (M394, near the myosin cardiomyopathy loop in the actin-binding interface) that is functionally sensitive to oxidation. We now show that oxidation of M394 is reversible by methionine sulfoxide reductase (Msr), restoring actin-activated ATPase activity. Sequence alignment reveals that M394 of Dicty myosin II is a cysteine residue in all human isoforms of skeletal and cardiac myosin. Using Dicty myosin II as a model for site-specific redox sensitivity of this Cys residue, the M394C mutant can be glutathionylated in vitro, resulting in reversible inhibition of actin-activated ATPase activity, with effects similar to those of methionine oxidation at this site. This work illustrates the potential for myosin to function as a redox sensor in both non-muscle and muscle cells, modulating motility/contractility in response to oxidative stress.

Indexed as

ActinsAmino Acid SequenceBinding SitesCatalytic DomainGlutathioneHumansMolecular Sequence DataMutagenesis, Site-DirectedMyosinsOxidation-ReductionSequence Homology, Amino AcidActinsGlutathioneMyosinsDictyosteliumGlutathionylationMethionineMethionine sulfoxide reductase (Msr)Myosin IIReactive oxygen species (ROS)

Identifiers

PMID25264102
PMCPMC4272649
OpenAlexW2162252409

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.