Evidence map›Paper›PMID 12030846›Full record

ArticleThe Biochemical journal2002

Phosphorylation of the myosin phosphatase target subunit by integrin-linked kinase.

Andrea Murányi, Justin A MacDonald, Jing Ti Deng, David P Wilson, Timothy A J Haystead, Michael P Walsh, Ferenc Erdodi, Eniko Kiss, Yue Wu, David J Hartshorne

Open access · greenAbstract 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 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
5.4field-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

68 citing papers in PubMed, 168 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Role of ZIP kinase in development of myofibroblast differentiation from HPMCs.American journal of physiology. Lung cellular and molecular physiology · 2024
    Article
  6. Article
  7. Article
  8. Review
  9. Integrin-linked kinase (ILK): the known vs. the unknown and perspectives.Cellular and molecular life sciences : CMLS · 2022
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Calcium Sensitization Mechanisms in Gastrointestinal Smooth Muscles.Journal of neurogastroenterology and motility · 2016
    Review
  19. Review
  20. MYPT1 isoforms expressed in HEK293T cells are differentially phosphorylated after GTPγS treatment.Journal of smooth muscle research = Nihon Heikatsukin Gakkai kikanshi · 2016
    Article

8 more citing papers are in PubMed but not listed here.

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

10 authors at 2 institutions in 2 countries.

Andrea MurányiMuscle Biology Group, University of Arizona, Tucson, AZ 85721-0038, U.S.A.
Justin A MacDonald
Jing Ti Deng
David P Wilson
Timothy A J Haystead
Michael P Walsh
Ferenc Erdodi
Eniko Kiss
Yue Wu
David J Hartshorne
University of Calgary · CAUniversity of Debrecen · HU

Funding

THE CONTRACTILE SYSTEM OF VASCULAR SMOOTH MUSCLEP01HL019242 · NHLBI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI OWENS, GARY K · 1985 to 2009
$16.9M
BIOCHEMISTRY OF CONTRACTILE PROTEINSR01HL023615 · NHLBI · UNIVERSITY OF ARIZONA · PI HARTSHORNE, DAVID JOHN · 1985 to 2009
$2.8M
PROTEIN PHOSPHATASE 1 REGULATION BY MULTIPLE SUBUNITSR01DK052378 · NIDDK · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI HAYSTEAD, TIMOTHY A · 1997 to 2005
$1.4M
NHLBI NIH HHS HL19242NHLBI NIH HHS HL23615NIDDK NIH HHS DK52378
6 · The paper itself

Abstract

A mechanism proposed for regulation of myosin phosphatase (MP) activity is phosphorylation of the myosin phosphatase target subunit (MYPT1). Integrin-linked kinase (ILK) is associated with the contractile machinery and can phosphorylate myosin at the myosin light-chain kinase sites. The possibility that ILK may also phosphorylate and regulate MP was investigated. ILK was associated with the MP holoenzyme, shown by Western blots and in-gel kinase assays. MYPT1 was phosphorylated by ILK and phosphorylation sites in the N- and C-terminal fragments of MYPT1 were detected. From sequence analyses, three sites were identified: a primary site at Thr(709), and two other sites at Thr(695) and Thr(495). One of the sites for cAMP-dependent protein kinase (PKA) was Ser(694). Assays with the catalytic subunit of type 1 phosphatase indicated that only the C-terminal fragment of MYPT1 phosphorylated by zipper-interacting protein kinase, and ILK inhibited activity. The phosphorylated N-terminal fragment activated phosphatase activity and phosphorylation by PKA was without effect. Using full-length MYPT1 constructs phosphorylated by various kinases it was shown that Rho kinase gave marked inhibition; ILK produced an intermediate level of inhibition, which was considerably reduced for the Thr(695)-->Ala mutant; and PKA had no effect. In summary, phosphorylation of the various sites indicated that Thr(695) was the major inhibitory site, Thr(709) had only a slight inhibitory effect and Ser(694) had no effect. The findings that ILK phosphorylated both MYPT1 and myosin and the association of ILK with MP suggest that ILK may influence cytoskeletal structure or function.

Indexed as

Amino Acid SequenceAnimalsBlotting, WesternCatalytic DomainChickensChromatography, High Pressure LiquidCyclic AMPDose-Response Relationship, DrugMolecular Sequence DataMuscle, SmoothMutationMyosin-Light-Chain PhosphatasePhosphoprotein PhosphatasesPhosphorylationProtein BindingProtein Serine-Threonine KinasesCyclic AMPMyosin-Light-Chain PhosphatasePhosphoprotein PhosphatasesProtein Serine-Threonine KinasesScaffold Protein ILKSerineThreonine

Identifiers

PMID12030846
PMCPMC1222775
OpenAlexW2139582056

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.