MLCP is involved in the Rho/ROCK pathway and regulates the interaction between actin and myosin. The importance of Ca2+calmodulin-dependent myosin light chain kinase (MLCK) for smooth muscle contraction is well documented.1 Until recently, myosin light chain (MLC) phosphatase …

The extent of MLC phosphorylation is regulated by two opposing pathways: myosin light-chain kinase (MLCK)-driven phosphorylation, and myosin light-chain phosphatase (MLCP)-driven dephosphorylation. Myosin light-chain phosphatase, more commonly called myosin phosphatase (EC 3.1.3.53), is an enzyme (specifically a serine/threonine-specific protein phosphatase) that dephosphorylates the regulatory light chain of myosin II.This dephosphorylation reaction occurs in smooth muscle tissue and initiates the relaxation process of the muscle cells. A smooth muscle phosphoprotein called CPI-17 specifically and potently inhibits MLCP in vitro andin situ and is activated when phosphorylated at Thr-38, which increases its inhibitory potency 1000-fold. Phosphorylation of myosin phosphatase target subunit 1 (MYPT1, an index of Rho kinase activity) was abrogated by inhibitors of Src, EGFR MEK, Erk1/2, and Rho kinase. We report here a novel signaling mechanism that activates MLC phosphorylation and smooth muscle contraction.

1999; 283:2083–2085.

It phosphorylates the regulatory myosin light chains of * myosin II, in order to facilitate myosin binding to * actin and therefore aid contractility. The study was supported by the Deutsche Forschungsgemeinschaft, Project A3 … Ca 2+ /calmodulin (CaM)-dependent phosphorylation of myosin regulatory light chain (RLC) in smooth muscle by myosin light chain kinase (MLCK) and dephosphorylation by myosin light chain phosphatase (MLCP) are subject to modulatory cascades that influence the sensitivity of RLC phosphorylation and hence contraction to intracellular Ca 2+ concentration ([Ca 2+] i). Acknowledgements. Myosin light chain phosphatase is a serine/threonine phos-phatase that consists of a 130-kDa regulatory subunit that binds myosin (MYPT1), a 37-kDa catalytic subunit PP1C and a 21-kDa subunit (M-21) of undetermined function (Hartshorne, 1998). Understanding this mechanism is of (patho)physiological significance because MLCP is a potent regulator of endothelial barrier function. H89 (N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide) is a compound characterized in vitro as a potent and selective inhibitor of protein kinase A (PKA). Acknowledgements DOI: 10.1091/mbc.E18-01-0056. In summary, this study has identified the mechanism by which external ATP causes a strong activation of myosin light chain phosphatase in endothelial cells. However, the myosin light chain kinase inhibitor ML-7 (1-(5-iodonaphthalene-1-sulfonyl)-homopiperazine, 10 µM) did not affect OVA-induced constriction. 27 Sanders LC, Matsumura F, Bokoch GM, de Lanerolle P. Inhibition of myosin light chain kinase by p21-activated kinase. Request PDF | On Sep 1, 2000, R J Solaro published Myosin Light Chain Phosphatase : A Cinderella of Cellular Signaling | Find, read and cite all the research you need on ResearchGate

We investigated whether TIMAP/PP1cβ could also function as a myosin phosphatase. The myosin light chain phosphatase (MLCP) is a cytoskeleton-associated protein phosphatase-1 (PP1) holoenzyme and a RhoA/ROCK effector, regulating cytoskeletal reorganization. 1 Introduction . In summary, this study has identified the mechanism by which external ATP causes a strong activation of myosin light chain phosphatase in endothelial cells. The myosin light-chain kinase MLCK-1 relocalizes during Caenorhabditis elegans ovulation to promote actomyosin bundle assembly and drive contraction. Endogenous PP1cβ, myosin light chain 2 (MLC2), and myosin IIA heavy chain coimmunoprecipitated from EC lysates with endogenous TIMAP, and endogenous MLC2 colocalized with TIMAP in EC projections.

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