Evidence map›Paper›PMID 11481347›Full record

ArticleThe Journal of cell biology2001

Myosin light chain kinase binding to a unique site on F-actin revealed by three-dimensional image reconstruction.

V Hatch, G Zhi, L Smith, J T Stull, R Craig, W Lehman

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2001. 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
1.2field-weighted citation impact, top 23% 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, 40 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Cytoskeletal protein kinases: titin and its relations in mechanosensing.Pflugers Archiv : European journal of physiology · 2011
    Review
  12. Biochemistry of smooth muscle myosin light chain kinase.Archives of biochemistry and biophysics · 2011
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

6 authors at 3 institutions in 1 country.

V HatchDepartment of Physiology and Biophysics, Boston University School of Medicine, Boston, MA 02118-2526, USA.
G Zhi
L Smith
J T Stull
R Craig
W Lehman
The University of Texas Southwestern Medical Center · USBoston University · USUniversity of Massachusetts Chan Medical School · US

Funding

THIN FILAMENTS AND VERTEBRATE SMOOTH MUSCLE CONTRACTIONR01HL036153 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI William J Lehman · 1986 to 2026
$6.5M
Thin Filaments and Muscle RegulationR37HL036153 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI LEHMAN, WILLIAM J · 2008 to 2017
$4.1M
MYOSIN LIGHT CHAIN KINASE FUNCTION IN SMOOTH MUSCLER01HL026043 · NHLBI · UT SOUTHWESTERN MEDICAL CENTER · PI STULL, JAMES T · 1985 to 2009
$3.4M
STRUCTURAL BASIS OF SMOOTH MUSCLE CONTRACTIONR01HL062468 · NHLBI · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI CRAIG, ROGER W · 1999 to 2002
$1.1M
BIOCHEMICAL MECHANISMS OF SMOOTH MUSCLE CONTRACTIONR37HL026043 · NHLBI · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI STULL, JAMES T · 1991 to 1999
–
THIN FILAMENTS AND VERTEBRATE SMOOTH MUSCLE CONTRACTIONR55HL036153 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI LEHMAN, WILLIAM J · 1992 to 1992
–
CRYOELECTRON MICROSCOPE AND CRYO-ULTRAMICROTOMES10RR008426 · NCRR · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI CRAIG, ROGER W · 1993 to 1993
–
NCRR NIH HHS RR-08426NHLBI NIH HHS HL-26043NHLBI NIH HHS HL-36153NHLBI NIH HHS HL-62468NHLBI NIH HHS R01 HL026043NHLBI NIH HHS R01 HL036153NHLBI NIH HHS R37 HL026043NHLBI NIH HHS R37 HL036153
6 · The paper itself

Abstract

Ca2+-calmodulin-dependent phosphorylation of myosin regulatory light chains by the catalytic COOH-terminal half of myosin light chain kinase (MLCK) activates myosin II in smooth and nonmuscle cells. In addition, MLCK binds to thin filaments in situ and F-actin in vitro via a specific repeat motif in its NH2 terminus at a stoichiometry of one MLCK per three actin monomers. We have investigated the structural basis of MLCK-actin interactions by negative staining and helical reconstruction. F-actin was decorated with a peptide containing the NH2-terminal 147 residues of MLCK (MLCK-147) that binds to F-actin with high affinity. MLCK-147 caused formation of F-actin rafts, and single filaments within rafts were used for structural analysis. Three-dimensional reconstructions showed MLCK density on the extreme periphery of subdomain-1 of each actin monomer forming a bridge to the periphery of subdomain-4 of the azimuthally adjacent actin. Fitting the reconstruction to the atomic model of F-actin revealed interaction of MLCK-147 close to the COOH terminus of the first actin and near residues 228-232 of the second. This unique location enables MLCK to bind to actin without interfering with the binding of any other key actin-binding proteins, including myosin, tropomyosin, caldesmon, and calponin.

Indexed as

ActinsAnimalsImage Processing, Computer-AssistedMicroscopy, ElectronModels, MolecularMuscle, SkeletalMyosin-Light-Chain KinasePeptidesProtein Structure, TertiaryRabbitsActinsMLCK peptideMyosin-Light-Chain KinasePeptides

Identifiers

PMID11481347
PMCPMC2196421
OpenAlexW2125576825

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.