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Literature summary for 3.1.3.53 extracted from

  • Chen, C.; Chen, X.; Qiao, Y.; Wang, P.; He, W.; Zhang, C.; Zhao, W.; Gao, Y.; Chen, C.; Tao, T.; Sun, J.; Wang, Y.; Gao, N.; Kamm, K.; Stull, J.; Zhu, M.
    In vivo roles for myosin phosphatase targeting subunit-1 phosphorylation sites T694 and T852 in bladder smooth muscle contraction (2015), J. Physiol., 593, 681-700 .
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Mus musculus Q9DBR7
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Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phosphorylation of MYPT1 residue T694 is a primary mechanism contributing to inhibition of myosin light chain phosphatase activity and enhancement of myosin regulatory light chain phosphorylation in vivo Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
bladder
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 Mus musculus
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smooth muscle
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 Mus musculus
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General Information

General Information Comment Organism
physiological function phosphorylation of MYPT1 residue T694, but not T852, is a primary mechanism contributing to inhibition of myosin light chain phosphatase activity and enhancement of myosin regulatory light chain phosphorylation in vivo. Smooth muscles containing the T694A mutation show a significant reduction of force along with reduced myosin regulatory light chain phosphorylation. The contractile responses of the T694A mutant smooth muscle are independent of RhoA-associated protein kinase ROCK activation Mus musculus