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  2. Myosin light-chain kinase - Wikipedia

    en.wikipedia.org/wiki/Myosin_light-chain_kinase

    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]

  3. MYLK - Wikipedia

    en.wikipedia.org/wiki/MYLK

    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.

  4. Myosin - Wikipedia

    en.wikipedia.org/wiki/Myosin

    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.

  5. Myosin light chain - Wikipedia

    en.wikipedia.org/wiki/Myosin_light_chain

    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.

  6. Telokin - Wikipedia

    en.wikipedia.org/wiki/Telokin

    It is identical to the C-terminus of myosin light-chain kinase. Telokin may play a role in the stabilization of unphosphorylated smooth-muscle myosin filaments. [2] [3] Because of its origin as the C-terminal end of smooth muscle myosin light chain kinase, it is called "telokin" (from a combination of the Greek telos, "end" and kinase). [4]

  7. Motor protein - Wikipedia

    en.wikipedia.org/wiki/Motor_protein

    Myosin II is an elongated protein that is formed from two heavy chains with motor heads and two light chains. Each myosin head contains actin and ATP binding site. The myosin heads bind and hydrolyze ATP, which provides the energy to walk toward the plus end of an actin filament. Myosin II are also vital in the process of cell division. For ...

  8. MYLK3 - Wikipedia

    en.wikipedia.org/wiki/MYLK3

    213435 Ensembl ENSG00000140795 ENSMUSG00000031698 UniProt Q32MK0 Q3UIZ8 RefSeq (mRNA) NM_001308301 NM_182493 NM_001297612 NM_175441 RefSeq (protein) NP_001295230 NP_872299 NP_001284541 NP_780650 Location (UCSC) Chr 16: 46.7 – 46.79 Mb Chr 8: 86.05 – 86.11 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Myosin light chain kinase 3 also known as MYLK3, is an enzyme which in humans ...

  9. MYLK4 - Wikipedia

    en.wikipedia.org/wiki/MYLK4

    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 .