Evidence map›Paper›PMID 11931630›Full record

ArticleThe Biochemical journal2002

Integrin-linked kinase phosphorylates the myosin phosphatase target subunit at the inhibitory site in platelet cytoskeleton.

Eniko Kiss, Andrea Murányi, Csilla Csortos, Pál Gergely, Masaaki Ito, David J Hartshorne, Ferenc Erdodi

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 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed, 85 citations in OpenAlex.

  1. Article
  2. Article
  3. Regulation of myosin light-chain phosphorylation and its roles in cardiovascular physiology and pathophysiology.Hypertension research : official journal of the Japanese Society of Hypertension · 2022
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Signaling in muscle contraction.Cold Spring Harbor perspectives in biology · 2015
    Review
  9. Article
  10. Platelet mechanosensing of substrate stiffness during clot formation mediates adhesion, spreading, and activation.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Integrin-linked kinase: a Scaffold protein unique among its ilk.Journal of cell communication and signaling · 2011
    Article
  16. MAPKs represent novel therapeutic targets for gastrointestinal motility disorders.World journal of gastrointestinal pathophysiology · 2011
    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

7 authors at 2 institutions in 2 countries.

Eniko KissDepartment of Medical Chemistry, University of Debrecen, Medical and Health Science Center, H-4026 Debrecen, Bem tér 18/B, Hungary.
Andrea Murányi
Csilla Csortos
Pál Gergely
Masaaki Ito
David J Hartshorne
Ferenc Erdodi
University of Debrecen · HUMie University · JP

Funding

BIOCHEMISTRY OF CONTRACTILE PROTEINSR01HL023615 · NHLBI · UNIVERSITY OF ARIZONA · PI HARTSHORNE, DAVID JOHN · 1985 to 2009
$2.8M
NHLBI NIH HHS HL 23615
6 · The paper itself

Abstract

The myosin phosphatase (MP) composed of the catalytic subunit of type 1 protein phosphatase and myosin phosphatase target subunit isoform 1 (MYPT1) was identified as the major serine/threonine phosphatase component in the platelet-cytoskeleton fraction. MYPT1 was phosphorylated by cytoskeletal kinase(s), but the identity of the kinase(s) and the effect of phosphorylation were not established. Incubation of platelet-cytoskeletal fraction with MgATP or MgATP[S] (magnesium adenosine 5'-[gamma-thio]triphosphate) caused a decrease in the 20 kDa light-chain of smooth-muscle myosin (MLC20) phosphatase and phosphorylase phosphatase activities. MYPT1 contains a phosphorylation site, Thr-695, involved in the inhibition of MP in a RhoA/Rho kinase-dependent manner. The cytoskeletal kinase(s) phosphorylated Thr-695 of glutathione S-transferase (GST)-MYPT1, as determined with an antibody specific for phosphorylated Thr-695. The level of Rho kinase was low in the cytoskeletal fraction and was detected primarily in the membrane and cytosolic fractions. The phosphorylation of Thr-695 by the cytoskeletal kinase(s) was not affected by Rho kinase inhibitor, Y-27632, suggesting that kinase(s) other than Rho kinase were involved. In-gel kinase assay identified a kinase at 54-59 kDa that phosphorylated the C-terminal fragment of MYPT1 (GST-MYPT1(667-1004)). Western blots detected both zipper-interacting protein kinase (ZIPK) and integrin-linked kinase (ILK) at 54-59 kDa in the cytoskeleton and membrane fractions. Cytoskeletal ZIPK and ILK were separated and partially purified by chromatography on SP-Sepharose and on MonoQ. ZIPK preferentially phosphorylated MLC20 and had low activity on MYPT1. ILK phosphorylated both MLC20 and MYPT1 and phosphorylation of MYPT1 occured on Thr-695. The above results raise the potential for regulation of MP activity in platelet cytoskeleton by ILK and suggest an alternative to the Rho-linked pathway.

Indexed as

Adenosine TriphosphateAdultBinding SitesBlood PlateletsCytoskeletonHumansIn Vitro TechniquesMyosin-Light-Chain PhosphatasePhosphoprotein PhosphatasesPhosphorylationProtein Serine-Threonine KinasesProtein SubunitsRecombinant Fusion ProteinsScaffold Protein ILKAdenosine TriphosphateMyosin-Light-Chain PhosphatasePhosphoprotein PhosphatasesProtein Serine-Threonine KinasesProtein SubunitsRecombinant Fusion ProteinsScaffold Protein ILK

Identifiers

PMID11931630
PMCPMC1222641
OpenAlexW2037202171

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.