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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 .
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.
For example, the human genome contains over 40 different myosin genes. These differences in shape also determine the speed at which myosins can move along actin filaments. The hydrolysis of ATP and the subsequent release of the phosphate group causes the "power stroke", in which the "lever arm" or "neck" region of the heavy chain is dragged ...
The structure and function of cytochrome b 6 f (in chloroplasts) is very similar to cytochrome bc 1 (Complex III in mitochondria). Both are transmembrane structures that remove electrons from a mobile, lipid-soluble electron carrier (plastoquinone in chloroplasts; ubiquinone in mitochondria) and transfer them to a mobile, water-soluble electron ...
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.
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