Myosin phosphatase dephosphorylates myosin regulatory light chain

Stable Identifier
R-HSA-419232
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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In non-muscle cells, phosphorylation of myosin II regulates actomyosin contractility. The level of myosin phosphorylation depends mainly on the balance of two enzymes, the Ca2+-dependent MLC kinase (MLCK), and myosin phosphatase (MLCP). Phosphorylation of the regulatory light chain of myosin II (MRLC) induces its interaction with actin, activating myosin ATPase and resulting in enhanced cell contractility. Myosin phosphatase decreases MRLC phosphorylation, which inhibits binding to filamentous actin and stress fibre formation (Kimura et al. 1996, Nakai et al. 1997, Katoh et al. 2001, Iwasaki et al. 2001).
Literature References
PubMed ID Title Journal Year
8662509 Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase)

Fukata, Y, Kaibuchi, K, Ito, M, Feng, J, Nakano, T, Yamamori, B, Chihara, K, Kimura, K, Nakafuku, M, Amano, M, Okawa, K, Iwamatsu, A

Science 1996
9354661 Regulation of myosin phosphatase through phosphorylation of the myosin-binding subunit in platelet activation

Nakai, K, Suzuki, Y, Wada, H, Kaibuchi, K, Fujioka, M, Nishikawa, M, Ito, M, Kihira, H, Nakano, T, Shiku, H

Blood 1997
11942626 Diphosphorylated MRLC is required for organization of stress fibers in interphase cells and the contractile ring in dividing cells

Ishitobi, S, Iwasaki, T, Murata-Hori, M, Hosoya, H

Cell Struct. Funct. 2001
11331307 Rho-kinase--mediated contraction of isolated stress fibers

Onishi, H, Kano, Y, Kaibuchi, K, Fujiwara, K, Amano, M, Katoh, K

J. Cell Biol. 2001
Participants
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Catalyst Activity

myosin-light-chain-phosphatase activity of Myosin phosphatase [cytosol]

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