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Thus, myosin phosphatase undoes the muscle contraction process initiated by myosin light-chain kinase. The enzyme is composed of three subunits: the catalytic region ( protein phosphatase 1 , or PP1), the myosin binding subunit (MYPT1), and a third subunit (M20) of unknown function.
Protein kinase C and ROC Kinase are involved in regulating Calcium ion intake; these Calcium ions, in turn stimulate a MYLK, forcing a contraction. [9] Rho kinase also modulates the activity of MYLK by downregulating the activity of MYLK's counterpart protein: Myosin Light Chain Phosphatase (MYLP). [10]
Rho-associated kinase (Rho-kinase), which is activated by GTP. RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase. [6]
Myosin light chain kinase (MLCK) inhibitors are one of the few peptides that can cross the plasma membrane relatively quickly. Under stressful conditions, MLCK's in the human body promotes increased permeability of microvessels. It is thought that MLCK phosphorylates endothelial myosin, leading to cell contraction.
Protein phosphatase 1 regulatory subunit 12B is an enzyme that in humans is encoded by the PPP1R12B gene. [5] [6] Myosin light chain phosphatase (MLCP) consists of three subunits- catalytic subunit, large subunit/myosin binding subunit (MBS) and small subunit (sm-M20). This gene is a multi-functional gene which encodes both MBS and sm-M20.
The myosin light chain phosphatase is inhibited to increase the gain or sensitivity of myosin light chain kinase to calcium. There are a number of cell signalling pathways believed to regulate this decrease in myosin light chain phosphatase: a RhoA-Rock kinase pathway, a Protein kinase C-Protein kinase C potentiation inhibitor protein 17 (CPI ...
Secondly, ROCK inactivates MLC phosphatase, leading to increased levels of phosphorylated MLC. Thus in both cases, ROCK activation by Rho induces the formation of actin stress fibers , actin filament bundles of opposing polarity, containing myosin II, tropomyosin, caldesmon and MLC-kinase, and consequently of focal contacts, which are immature ...
/calmodulin-dependent protein kinase II (CaM kinase II or CaMKII) is a serine/threonine-specific protein kinase that is regulated by the Ca 2+ /calmodulin complex. CaMKII is involved in many signaling cascades and is thought to be an important mediator of learning and memory. [1] CaMKII is also necessary for Ca 2+