Evidence map›Paper›PMID 12144526›Full record

ArticleThe Biochemical journal2002

Phosphorylation of the myosin phosphatase inhibitors, CPI-17 and PHI-1, by integrin-linked kinase.

Jing Ti Deng, Cindy Sutherland, David L Brautigan, Masumi Eto, Michael P Walsh

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
4.4field-weighted citation impact, top 4% 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

53 citing papers in PubMed, 135 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Functional tuning of Vascular L-type CaFrontiers in physiology · 2022
    Review
  7. Article
  8. Review
  9. The Evolution of Duplicated Genes of the Cpi-17/Phi-1 (International journal of molecular sciences · 2020
    Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Calcium Sensitization Mechanisms in Gastrointestinal Smooth Muscles.Journal of neurogastroenterology and motility · 2016
    Review
  17. Review
  18. MYPT1 isoforms expressed in HEK293T cells are differentially phosphorylated after GTPγS treatment.Journal of smooth muscle research = Nihon Heikatsukin Gakkai kikanshi · 2016
    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

5 authors at 2 institutions in 1 country.

Jing Ti DengSmooth Muscle Research Group and Canadian Institutes of Health Research Group in Regulation of Vascular Contractility, University of Calgary Faculty of Medicine, 3330 Hospital Drive N.W., Calgary, Alberta T2N 4N1, Canada.
Cindy Sutherland
David L Brautigan
Masumi Eto
Michael P Walsh
University of Calgary · CACanadian Institutes of Health Research · CA

Funding

Phosphorylation & Function of Inhibitor-2R01GM056362 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI BRAUTIGAN, DAVID L. · 1997 to 2011
$2.4M
NCI NIH HHS CA 40042NIGMS NIH HHS GM 56362
6 · The paper itself

Abstract

Integrin-linked kinase (ILK) has been implicated in Ca(2+)- independent contraction of smooth muscle via its ability to phosphorylate myosin. We investigated the possibility that this kinase might also phosphorylate and regulate the myosin light-chain phosphatase inhibitor proteins CPI-17 [protein kinase C (PKC)-dependent phosphatase inhibitor of 17 kDa] and PHI-1 (phosphatase holoenzyme inhibitor-1), known substrates of PKC. Both phosphatase inhibitors were phosphorylated by ILK in an in-gel kinase assay and in solution. A Thr-->Ala mutation at Thr(38) of CPI-17 and Thr(57) of PHI-1 eliminated phosphorylation by ILK. Phosphopeptide mapping, phospho amino acid analysis and immunoblotting using phospho-specific antibodies indicated that ILK predominantly phosphorylated the site critical for potent inhibition, i.e. Thr(38) of CPI-17 or Thr(57) of PHI-1. CPI-17 and PHI-1 thiophosphorylated by ILK at Thr(38) or Thr(57) respectively inhibited myosin light-chain phosphatase (MLCP) activity bound to myosin, whereas the site-specific mutants CPI-17-Thr(38)Ala and PHI-1-Thr(57)Ala, treated with ILK under identical conditions, like the untreated wild-type proteins had no effect on the phosphatase. Consistent with these effects, both thiophospho-CPI-17 and -PHI-1 induced Ca(2+) sensitization of contraction of Triton X-100-demembranated rat-tail arterial smooth muscle, whereas CPI-17-Thr(38)Ala and PHI-1-Thr(57)Ala treated with ILK in the presence of adenosine 5'-[gamma-thio]triphosphate failed to evoke a contractile response. We conclude that ILK may activate smooth-muscle contraction both directly, via phosphorylation of myosin, and indirectly, via phosphorylation and activation of CPI-17 and PHI-1, leading to inhibition of MLCP.

Indexed as

AnimalsCalciumIn Vitro TechniquesMaleMuscle ContractionMuscle ProteinsMuscle, Smooth, VascularMyosin-Light-Chain PhosphataseOctoxynolPeptide MappingPhosphoprotein PhosphatasesPhosphoproteinsPhosphorylationPoint MutationProteinsProtein Serine-Threonine KinasesCalciumMuscle ProteinsMyosin-Light-Chain PhosphataseOctoxynolphosphoprotein phosphatase inhibitor 1Phosphoprotein PhosphatasesPhosphoproteinsPpp1r14a protein, ratProteinsProtein Serine-Threonine KinasesScaffold Protein ILK

Identifiers

PMID12144526
PMCPMC1222907
OpenAlexW2073947893

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.