Evidence map›Paper›PMID 19769984›Full record

ArticleJournal of molecular biology2009

The on-off switch in regulated myosins: different triggers but related mechanisms.

Daniel M Himmel, Suet Mui, Elizabeth O'Neall-Hennessey, Andrew G Szent-Györgyi, Carolyn Cohen

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

20 citing papers in PubMed, 34 citations in OpenAlex.

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  10. Review
  11. Structural basis of the relaxed state of a Ca2+-regulated myosin filament and its evolutionary implications.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  12. Allosteric communication in Dictyostelium myosin II.Journal of muscle research and cell motility · 2012
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Broad disorder and the allosteric mechanism of myosin II regulation by phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  19. Visualizing key hinges and a potential major source of compliance in the lever arm of myosin.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  20. Essential "ankle" in the myosin lever arm.Proceedings of the National Academy of Sciences of the United States of America · 2011
    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

5 authors at 1 institution in 1 country.

Daniel M HimmelRosenstiel Basic Medical Sciences Research Center, Biology Department, Brandeis University, Waltham, MA 02453-2728, USA. himmel@cabm.rutgers.edu
Suet Mui
Elizabeth O'Neall-Hennessey
Andrew G Szent-Györgyi
Carolyn Cohen
Brandeis University · US

Funding

MUSCLE STRUCTURE AND THE CONTRACTILE MECHANISMR01AR017346 · NIAMS · BRANDEIS UNIVERSITY · PI COHEN, CAROLYN · 1986 to 2012
$7.6M
REGULATORY DOMAIN/S1 CRYSTAL STRUCTURE--SCALLOP MYOSINR01AR041808 · NIAMS · BRANDEIS UNIVERSITY · PI COHEN, CAROLYN · 1995 to 1999
–
MUSCLE STRUCTURE AND THE CONTRACTILE MECHANISMR37AR017346 · NIAMS · BRANDEIS UNIVERSITY · PI COHEN, CAROLYN · 1990 to 1999
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NIAMS NIH HHS AR017346NIAMS NIH HHS AR041808NIAMS NIH HHS R01 AR017346NIAMS NIH HHS R37 AR017346
6 · The paper itself

Abstract

In regulated myosin, motor and enzymatic activities are toggled between the on-state and off-state by a switch located on its lever arm domain, here called the regulatory domain (RD). This region consists of a long alpha-helical "heavy chain" stabilized by a "regulatory" light chain (RLC) and an "essential" light chain (ELC). The on-state is activated by phosphorylation of the RLC of vertebrate smooth muscle RD or by direct binding of Ca(2+) to the ELC of molluscan RD. Crystal structures are available only for the molluscan RD. To understand in more detail the pathway between the on-state and the off-state, we have now also determined the crystal structure of a molluscan (scallop) RD in the absence of Ca(2+). Our results indicate that loss of Ca(2+) abolishes most of the interactions between the light chains and may increase the flexibility of the RD heavy chain. We propose that disruption of critical links with the C-lobe of the RLC is the key event initiating the off-state in both smooth muscle myosins and molluscan myosins.

Indexed as

Amino Acid SubstitutionAnimalsBinding SitesCalciumCrystallography, X-RayIn Vitro TechniquesModels, MolecularMolecular Motor ProteinsMutagenesis, Site-DirectedMyosin Light ChainsPectinidaeProtein ConformationProtein Structure, TertiaryRecombinant ProteinsStatic ElectricityCalciumMolecular Motor ProteinsMyosin Light ChainsRecombinant Proteins

Identifiers

PMID19769984
PMCPMC2997636
OpenAlexW2055876984

What OpenQuestion holds

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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.