Evidence map›Paper›PMID 27528075›Full record

ArticleCell biochemistry and function2016

Myosin light chain kinase steady-state kinetics: comparison of smooth muscle myosin II and nonmuscle myosin IIB as substrates.

Diego B Alcala, Brian D Haldeman, Richard K Brizendine, Agata K Krenc, Josh E Baker, Ronald S Rock, Christine R Cremo

Open access · greenAbstract read
In one paragraph

Article in Cell biochemistry and function, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.7field-weighted citation impact, top 25% 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

8 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Hypoxic modulation of fetal vascular MLCK abundance, localization, and function.American journal of physiology. Regulatory, integrative and comparative physiology · 2021
    Article
  6. Article
  7. Article
  8. 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

7 authors at 2 institutions in 1 country.

Diego B AlcalaDepartment of Pharmacology, University of Nevada Reno School of Medicine, Reno, Nevada, USA.
Brian D HaldemanDepartment of Pharmacology, University of Nevada Reno School of Medicine, Reno, Nevada, USA.
Richard K BrizendineDepartment of Pharmacology, University of Nevada Reno School of Medicine, Reno, Nevada, USA.
Agata K KrencDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA.
Josh E BakerDepartment of Pharmacology, University of Nevada Reno School of Medicine, Reno, Nevada, USA.
Ronald S RockDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA.
Christine R CremoDepartment of Pharmacology, University of Nevada Reno School of Medicine, Reno, Nevada, USA. cremo@unr.edu.ORCID http://orcid.org/0000-0001-5516-5222
University of Nevada, Reno · USUniversity of Illinois Chicago · US

Funding

Allostery in myosins studied at the molecular levelR01GM078450 · NIGMS · UNIVERSITY OF CHICAGO · PI ROCK, RONALD S · 2006 to 2015
$2.8M
Myosin light chain kinase interactions that influence the rate of smooth muscle aR01HL110214 · NHLBI · UNIVERSITY OF NEVADA RENO · PI BAKER, JONATHAN E., CREMO, CHRISTINE R · 2011 to 2014
$2.0M
Force-sensitive macromolecular cytoskeletal assemblyR01GM109863 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI ROBINSON, DOUGLAS N, ROCK, RONALD S · 2014 to 2017
$1.1M
NHLBI NIH HHS R01 HL110214NIGMS NIH HHS R01 GM078450NIGMS NIH HHS R01 GM109863
6 · The paper itself

Abstract

Myosin light chain kinase (MLCK) phosphorylates S19 of the myosin regulatory light chain (RLC), which is required to activate myosin's ATPase activity and contraction. Smooth muscles are known to display plasticity in response to factors such as inflammation, developmental stage, or stress, which lead to differential expression of nonmuscle and smooth muscle isoforms. Here, we compare steady-state kinetics parameters for phosphorylation of different MLCK substrates: (1) nonmuscle RLC, (2) smooth muscle RLC, and heavy meromyosin subfragments of (3) nonmuscle myosin IIB, and (4) smooth muscle myosin II. We show that MLCK has a ~2-fold higher k SIGNIFICANCE OF THE STUDY: Phosphorylation of nonmuscle and smooth muscle myosin by myosin light chain kinase (MLCK) is required for activation of myosin's ATPase activity. In smooth muscles, nonmuscle myosin coexists with smooth muscle myosin, but the two myosins have very different chemo-mechanical properties relating to their ability to maintain force. Differences in specificity of MLCK for different myosin isoforms had not been previously investigated. We show that the MLCK prefers smooth muscle myosin by a significant factor. These data suggest that nonmuscle myosin is phosphorylated more slowly than smooth muscle myosin during a contraction cycle.

Indexed as

Amino Acid SequenceAnimalsChickensKineticsModels, MolecularMyosin-Light-Chain KinaseMyosin SubfragmentsNonmuscle Myosin Type IIBPhosphorylationSmooth Muscle MyosinsSubstrate SpecificityMyosin-Light-Chain KinaseMyosin SubfragmentsNonmuscle Myosin Type IIBSmooth Muscle Myosinsmyosin light chain kinasemyosin regulatory light chainnonmuscle myosinphosphorylationsmooth musclesmooth muscle myosinsteady-state kinetics

Identifiers

PMID27528075
PMCPMC5076371
OpenAlexW2517602844

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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.