Evidence map›Paper›PMID 2174101›Full record

ArticleMolecular and cellular biochemistry1990

Phosphorylation of smooth muscle myosin by type II Ca2+/calmodulin-dependent protein kinase.

A M Edelman, W H Lin, D J Osterhout, M K Bennett, M B Kennedy, E G Krebs

Abstract read
PubMed Publisher
In one paragraph

Article in Molecular and cellular biochemistry, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

16 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Article
  3. Smooth muscle signalling pathways in health and disease.Journal of cellular and molecular medicine · 2008
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Calmodulin and the regulation of smooth muscle contraction.Molecular and cellular biochemistry · 1994
    Review
  14. Article
  15. G protein-mediated inhibition of myosin light-chain phosphatase in vascular smooth muscle.Proceedings of the National Academy of Sciences of the United States of America · 1991
    Article
  16. 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.

A M EdelmanDepartment of Pharmacology and Therapeutics, School of Medicine and Biomedical Sciences, State University of New York, Buffalo 14214.
W H Lin
D J Osterhout
M K Bennett
M B Kennedy
E G Krebs
University at Buffalo, State University of New York · USSeattle University · USCalifornia Institute of Technology · US

Funding

REGULATION OF CALMODULIN-DEPENDENT PROTEIN KINASESR01NS024738 · NINDS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI EDELMAN, ARTHUR M · 1994 to 1999
–
MYOSIN PHOSPHORYLATION IN THE NERVOUS SYSTEMR29NS024738 · NINDS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI EDELMAN, ARTHUR M · 1988 to 1993
–
NIGMS NIH HHS GM 07145NINDS NIH HHS NS 24738
6 · The paper itself

Abstract

Brain type II Ca2+/calmodulin-dependent protein kinase was found to phosphorylate smooth muscle myosin, incorporating maximally approximately 2 mol of phosphoryl per mol of myosin, exclusively on the 20,000 dalton light chain subunit. After maximal phosphorylation of myosin or the isolated 20,000 dalton light chain subunit by myosin light chain kinase, the addition of type II Ca2+/calmodulin-dependent protein kinase led to no further incorporation indicating the two kinases phosphorylated a common site. This conclusion was supported by two dimensional mapping of tryptic digests of myosin phosphorylated by the two kinases. By phosphoamino acid analysis the phosphorylated residue was identified as a serine. The phosphorylation by type II Ca2+/calmodulin-dependent protein kinase of myosin resulted in enhancement of its actin-activated Mg2(+)-ATPase activity. Taken together, these data strongly support the conclusion that type II Ca2+/calmodulin-dependent protein kinase phosphorylates the same amino acid residue on the 20,000 dalton light chain subunit of smooth muscle myosin as is phosphorylated by myosin light chain kinase and suggest an alternative mechanism for the regulation of actin-myosin interaction.

Indexed as

Amino AcidsAnimalsAutoradiographyBrainCa(2+) Mg(2+)-ATPaseCalcium-Calmodulin-Dependent Protein KinasesChickensElectrophoresis, Polyacrylamide GelMuscle, SmoothMyosinsPeptide MappingPhosphorus IsotopesPhosphorylationProtein KinasesAmino AcidsCa(2+) Mg(2+)-ATPaseCalcium-Calmodulin-Dependent Protein KinasesMyosinsPhosphorus IsotopesProtein Kinases

Identifiers

PMID2174101
OpenAlexW2040366611

What OpenQuestion holds

Textmetadata
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.