Integrin-linked kinase is responsible for Ca2+-independent myosin diphosphorylation and contraction of vascular smooth muscle.

@article{Wilson2005IntegrinlinkedKI,
  title={Integrin-linked kinase is responsible for Ca2+-independent myosin diphosphorylation and contraction of vascular smooth muscle.},
  author={David Peter Wilson and Cindy Sutherland and Meredith A. Borman and Jing Ti Deng and Justin A. MacDonald and M. P. Walsh},
  journal={The Biochemical journal},
  year={2005},
  volume={392 Pt 3},
  pages={641-8}
}
Smooth muscle contraction is activated by phosphorylation at Ser-19 of LC20 (the 20 kDa light chains of myosin II) by Ca2+/calmodulin-dependent MLCK (myosin light-chain kinase). Diphosphorylation of LC20 at Ser-19 and Thr-18 is observed in smooth muscle tissues and cultured cells in response to various contractile stimuli, and in pathological circumstances associated with hypercontractility. MLCP (myosin light-chain phosphatase) inhibition can lead to LC20 diphosphorylation and Ca2+-independent… CONTINUE READING

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