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
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.
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“From the first targeted pathway, PP2A regulates proteins involved in smooth muscle contraction [54].”
From Hsa-mir-548 family expression in human reproductive tissues (2021) · cites this paper as [54]
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Cited by
Hsa-mir-548 family expression in human reproductive tissues
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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
- Cited by
- 48
- References
- 281
- Language
- en
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