Phosphorylation of both Thr695 and Thr850 on MYPT1 by Rho-kinase inhibits phosphatase activity with equivalent efficacy in A7r5 cells.
No immediate clinical implications for vascular disorders; leaves open translation of dual-site MYPT1 inhibition to human physiology.
Major sites for Rho-kinase on the myosin phosphatase target subunit (MYPT1) are Thr695 and Thr850. Phosphorylation of Thr695 inhibits phosphatase activity but the role of phosphorylation at Thr850 is not clear and is evaluated here. Phosphorylation of both Thr695 and Thr850 by Rho-kinase inhibited activity of the type 1 phosphatase catalytic subunit. Rates of phosphorylation of the two sites were similar and efficacy of inhibition following phosphorylation was equivalent for each site. Phosphorylation of each site on MYPT1 was detected in A7r5 cells, but Thr850 was preferred by Rho-kinase and Thr695 was phosphorylated by an unidentified kinase(s).
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Murányi et al. (2005) studied this question.
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