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Binding of calcium ion to this domain increases the affinity of MYLK binding to myosin light chain. This myosin binding domain is located at the C-Terminus end of the kinase. On the other side of the kinase at the N-Terminus end, sits the actin-binding domain, which allows MYLK to form interactions with actin filaments, keeping it in place. [4] [5]
In addition, using a separate promoter in an intron in the 3' region, it encodes telokin, a small protein identical in sequence to the C-terminus of myosin light chain kinase, that is independently expressed in smooth muscle and functions to stabilize unphosphorylated myosin filaments.
Myosin light chain kinase 4 also known as MYLK4 is an enzyme which in humans is encoded by the MYLK2 gene. [2] MYLK4 is a member of the myosin light-chain kinase family of serine/threonine-specific protein kinases that phosphorylate the regulatory light chain of myosin II .
In enzymology, a myosin-heavy-chain kinase (EC 2.7.11.7) is an enzyme that catalyzes the chemical reaction. ATP + [myosin heavy-chain] ADP + [myosin heavy-chain] phosphate Thus, the two substrates of this enzyme are ATP and myosin heavy-chain, whereas its two products are ADP and myosin heavy-chain phosphate.
Myosin X is an unconventional myosin motor, which is functional as a dimer. The dimerization of myosin X is thought to be antiparallel. [53] This behavior has not been observed in other myosins. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments.
Structurally, myosin light chains belong to the EF-hand family, a large family of Ca 2+ - binding proteins. MLCs contain two Ca 2+ - binding EF-hand motifs. MLCs isoforms modulate the Ca 2+ of force transduction and cross-bridge kinetics. Myosin light chains (MLCs) can be broadly classified into two groups: Essential or alkali MLC (MLC1 or ELC),
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 Rho-associated protein kinase are involved in regulating calcium ion intake; these calcium ions, in turn stimulate a myosin light chain kinase, forcing a contraction. [5] Rho-associated protein kinase are serine or threonine kinases that determine the calcium sensitivity in smooth muscle cells.