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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]
This gene, a muscle member of the immunoglobulin superfamily, encodes a myosin light-chain kinase, which is a calcium-/calmodulin-dependent enzyme.This kinase phosphorylates myosin regulatory light chains to facilitate myosin interaction with actin filaments to produce contractile activity.
228785 Ensembl ENSG00000101306 ENSMUSG00000027470 UniProt Q9H1R3 Q8VCR8 RefSeq (mRNA) NM_033118 NM_001081044 RefSeq (protein) NP_149109 NP_001074513 Location (UCSC) Chr 20: 31.82 – 31.83 Mb Chr 2: 152.75 – 152.76 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Myosin light chain kinase 2 also known as MYLK2 is an enzyme which in humans is encoded by the MYLK2 gene. Function This ...
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 .
RLC is phosphorylated by a cardiac-specific myosin light chain kinase , which was recently cloned. [17] Studies have supported a role for myosin phosphatase targeting subunit 2 (MYPT2, PPP1R12B) in the dephosphorylation of RLC. [18] Human RLC has an Asparagine at position 14 (Threonine in mouse) and a Serine at position 15 (same in mouse).
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.
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.
ROCK is a kinase that acts to phosphorylate MLCP (myosin-light-chain phosphatase), as well as the NMMII light chain, which inactivates MLCP and activates myosin. [6] This will lead to the accumulation of activated myosin motor proteins, which bind the actin filaments that were polymerized by mDia, to create stress fibers.