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Cited by 48

The DOI matches its Crossref record; 281 of the 281 references it cites were found in a registry or an index.

Role of serine-threonine phosphoprotein phosphatases in smooth muscle contractility

Butler, Trent, Paul, Jonathan, Europe-Finner, Nick, Smith, Roger, Chan, Eng-Cheng·2013·American Journal of Physiology-Cell Physiology
DOI 10.1152/ajpcell.00161.2012
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Abstract

The degree of phosphorylation of myosin light chain 20 (MLC20) is a major determinant of force generation in smooth muscle. Myosin phosphatases (MPs) contain protein phosphatase (PP) 1 as catalytic subunits and are the major enzymes that dephosphorylate MLC20. MP regulatory targeting subunit 1 (MYPT1), the main regulatory subunit of MP in all smooth muscles, is a key convergence point of contractile and relaxatory pathways. Combinations of regulatory mechanisms, including isoform splicing, multiple phosphorylation sites, and scaffolding proteins, modulate MYPT1 activity with tissue and agonist specificities to affect contraction and relaxation. Other members of the PP1 family that do not target myosin, as well as PP2A and PP2B, dephosphorylate a range of proteins that affect smooth muscle contraction. This review discusses the role of phosphatases in smooth muscle contractility with a focus on MYPT1 in uterine smooth muscle. Myometrium shares characteristics of vascular and other visceral smooth muscles yet, during healthy pregnancy, undergoes hypertrophy, hyperplasia, quiescence, and labor as physiological processes. Myometrium presents an accessible model for the study of normal and pathological smooth muscle function, and a better understanding of myometrial physiology may allow the development of novel therapeutics for the many disorders of myometrial physiology from preterm labor to dysmenorrhea.

Overview

Integrity signals

Registry

Crossref · 10.1152/ajpcell.00161.2012

Cites

281 of 281 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Verification

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Citations

Cites

Research works printed but not linked: 12

  1. Boghaert ER, 1997, Cell Growth Differ, 8, 881
  2. 10.1210/jcem.86.8.7727 · DOI
  3. Dodge KL, 1999, Mol Endocrinol, 13, 1977
  4. Ekerhovd E, 1999, Obstet Gynecol, 93, 987
  5. Fetalvero KM, 2008, J Clin Invest, 118, 3966
  6. 10.1042/bj3530417 · DOI · Paper page
  7. Lartey J, 2010, Reprod Sci, 17
  8. Lartey J, 2010, Reprod Sci, 17
  9. Mehats C, 2000, J Pharmacol Exp Ther, 292, 817
  10. 10.1042/bj3560257 · DOI
  11. Somlyo AP, 1976, Fed Proc, 35, 1288
  12. Tichenor JN. Stretch-Activated Potassium Channels in Human Myometrium and Aspects of cGMP Signaling (Dissertation). Reno, NV: University of Nevada, 2008, p. 204.

Cited by

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Metadata

Authors
Butler, T., Paul, J., Europe-Finner, N., Smith, R., & Chan, E.-C.
Affiliations
  • Mothers and Babies Research Centre, Faculty of Health, University of Newcastle, Callaghan, New South Wales, Australia;
  • Reproductive and Vascular Research Group, Institute of Cellular Medicine, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne, United Kingdom
Venue
American Journal of Physiology-Cell Physiology
Publisher
American Physiological Society
Published
2013-03-15
Volume
304
Issue
6
Pages
C485-C504
ISSN
  • 0363-6143
  • 1522-1563
DOI
10.1152/ajpcell.00161.2012
Cited by
48
References
281
Language
en

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Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.