Evidence map›Paper›PMID 21284933›Full record

ReviewArchives of biochemistry and biophysics2011

Myosin light chain kinase and the role of myosin light chain phosphorylation in skeletal muscle.

James T Stull, Kristine E Kamm, Rene Vandenboom

Abstract readReview
In one paragraph

Review in Archives of biochemistry and biophysics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.

0numbers the graph read from it
0cells of the map it votes in
106citing papers in PubMed
8.8field-weighted citation impact, top 2% 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

106 citing papers in PubMed, 189 citations in OpenAlex.

  1. Trial
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  5. Review
  6. Article
  7. Article
  8. Integrative Transcriptomic and Proteomic Analysis RevealsAnimals : an open access journal from MDPI · 2025
    Article
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  18. Review
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  20. Ablation of skeletal muscle estrogen receptor alpha impairs contractility in male mice.Journal of applied physiology (Bethesda, Md. : 1985) · 2024
    Article

46 more citing papers are in PubMed but not listed here.

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.

James T StullDepartment of Physiology, University of Texas Southwestern Medical Center, Dallas, 75390-9040, USA. james.stull@utsouthwestern.edu
Kristine E Kamm
Rene Vandenboom
Brock University · CAThe University of Texas Southwestern Medical Center · US

Funding

Transcriptional control of muscle growth and remodelingP01HL006296 · NHLBI · UT SOUTHWESTERN MEDICAL CENTER · PI BASSEL-DUBY, RHONDA · 1985 to 2006
$14.8M
Roles of Myosin Light Chain Kinases in the HeartR01HL080536 · NHLBI · UT SOUTHWESTERN MEDICAL CENTER · PI STULL, JAMES T · 2006 to 2010
$1.9M
NHLBI NIH HHS P01 HL006296NHLBI NIH HHS R01 HL080536PHS HHS HLR01HL080536
6 · The paper itself

Abstract

Skeletal muscle myosin light chain kinase (skMLCK) is a dedicated Ca(2+)/calmodulin-dependent serine-threonine protein kinase that phosphorylates the regulatory light chain (RLC) of sarcomeric myosin. It is expressed from the MYLK2 gene specifically in skeletal muscle fibers with most abundance in fast contracting muscles. Biochemically, activation occurs with Ca(2+) binding to calmodulin forming a (Ca(2+))(4)•calmodulin complex sufficient for activation with a diffusion limited, stoichiometric binding and displacement of a regulatory segment from skMLCK catalytic core. The N-terminal sequence of RLC then extends through the exposed catalytic cleft for Ser15 phosphorylation. Removal of Ca(2+) results in the slow dissociation of calmodulin and inactivation of skMLCK. Combined biochemical properties provide unique features for the physiological responsiveness of RLC phosphorylation, including (1) rapid activation of MLCK by Ca(2+)/calmodulin, (2) limiting kinase activity so phosphorylation is slower than contraction, (3) slow MLCK inactivation after relaxation and (4) much greater kinase activity relative to myosin light chain phosphatase (MLCP). SkMLCK phosphorylation of myosin RLC modulates mechanical aspects of vertebrate skeletal muscle function. In permeabilized skeletal muscle fibers, phosphorylation-mediated alterations in myosin structure increase the rate of force-generation by myosin cross bridges to increase Ca(2+)-sensitivity of the contractile apparatus. Stimulation-induced increases in RLC phosphorylation in intact muscle produces isometric and concentric force potentiation to enhance dynamic aspects of muscle work and power in unfatigued or fatigued muscle. Moreover, RLC phosphorylation-mediated enhancements may interact with neural strategies for human skeletal muscle activation to ameliorate either central or peripheral aspects of fatigue.

Indexed as

Amino Acid SequenceAnimalsHumansMolecular Sequence DataMuscle Fibers, SkeletalMuscle, SkeletalMyosin-Light-Chain KinaseMyosin Light ChainsPhosphorylationMyosin-Light-Chain KinaseMyosin Light Chains

Identifiers

PMID21284933
PMCPMC3101293
OpenAlexW2058608440

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.