Evidence map›Paper›PMID 22948155›Full record

ArticleThe Journal of biological chemistry2012

Cross-talk between Rho-associated kinase and cyclic nucleotide-dependent kinase signaling pathways in the regulation of smooth muscle myosin light chain phosphatase.

Michael E Grassie, Cindy Sutherland, Annegret Ulke-Lemée, Mona Chappellaz, Enikö Kiss, Michael P Walsh, Justin A MacDonald

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
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

24 citing papers in PubMed.

  1. Differential expression of the enzymes regulating myosin light chain phosphorylation are responsible for the slower relaxation of pulmonary artery than mesenteric artery in rats.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2024
    Article
  2. Article
  3. Article
  4. 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
  5. Statins change the cytokine profile inFrontiers in immunology · 2022
    Article
  6. Article
  7. Article
  8. Article
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  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Review
  16. Regulation of pulmonary endothelial barrier function by kinases.American journal of physiology. Lung cellular and molecular physiology · 2016
    Review
  17. Article
  18. Article
  19. MYPT1 isoforms expressed in HEK293T cells are differentially phosphorylated after GTPγS treatment.Journal of smooth muscle research = Nihon Heikatsukin Gakkai kikanshi · 2016
    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.

Michael E GrassieSmooth Muscle Research Group and Libin Cardiovascular Institute of Alberta, University of Calgary, Calgary, Alberta T2N 4Z6, Canada.
Cindy Sutherland
Annegret Ulke-Lemée
Mona Chappellaz
Enikö Kiss
Michael P Walsh
Justin A MacDonald

Funding

Canadian Institutes of Health Research MOP-111262Canadian Institutes of Health Research MOP-72720
6 · The paper itself

Abstract

Ca(2+) sensitization of smooth muscle contraction depends upon the activities of protein kinases, including Rho-associated kinase, that phosphorylate the myosin phosphatase targeting subunit (MYPT1) at Thr(697) and/or Thr(855) (rat sequence numbering) to inhibit phosphatase activity and increase contractile force. Both Thr residues are preceded by the sequence RRS, and it has been suggested that phosphorylation at Ser(696) prevents phosphorylation at Thr(697). However, the effects of Ser(854) and dual Ser(696)-Thr(697) and Ser(854)-Thr(855) phosphorylations on myosin phosphatase activity and contraction are unknown. We characterized a suite of MYPT1 proteins and phosphospecific antibodies for specificity toward monophosphorylation events (Ser(696), Thr(697), Ser(854), and Thr(855)), Ser phosphorylation events (Ser(696)/Ser(854)) and dual Ser/Thr phosphorylation events (Ser(696)-Thr(697) and Ser(854)-Thr(855)). Dual phosphorylation at Ser(696)-Thr(697) and Ser(854)-Thr(855) by cyclic nucleotide-dependent protein kinases had no effect on myosin phosphatase activity, whereas phosphorylation at Thr(697) and Thr(855) by Rho-associated kinase inhibited phosphatase activity and prevented phosphorylation by cAMP-dependent protein kinase at the neighboring Ser residues. Forskolin induced phosphorylation at Ser(696), Thr(697), Ser(854), and Thr(855) in rat caudal artery, whereas U46619 induced Thr(697) and Thr(855) phosphorylation and prevented the Ser phosphorylation induced by forskolin. Furthermore, pretreatment with forskolin prevented U46619-induced Thr phosphorylations. We conclude that cross-talk between cyclic nucleotide and RhoA signaling pathways dictates the phosphorylation status of the Ser(696)-Thr(697) and Ser(854)-Thr(855) inhibitory regions of MYPT1 in situ, thereby regulating the activity of myosin phosphatase and contraction.

Indexed as

15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic AcidAmino Acid SubstitutionAnimalsColforsinCyclic AMPMaleMuscle ContractionMutation, MissenseMyocytes, Smooth MusclePhosphorylationProtein Phosphatase 1RatsRats, Sprague-DawleyrhoA GTP-Binding Proteinrho-Associated KinasesSecond Messenger Systems15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic AcidColforsinCyclic AMPPpp1r12a protein, ratProtein Phosphatase 1rhoA GTP-Binding Proteinrho-Associated KinasesSmooth Muscle MyosinsVasoconstrictor Agents

Identifiers

PMID22948155
PMCPMC3476302

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.