Thiophosphorylation of the 130-kDa subunit of myosin light chain phosphatase decreases its activity, suggesting a regulatory role for phosphorylation of this subunit in smooth muscle contraction.
Pretreatment of α-toxin-permeabilized smooth muscle with ATPγS (adenosine 5ʹ-O-(thiotriphosphate)) under conditions resulting in minimal (<1%) thiophosphorylation of the myosin light chain increases the subsequent calcium sensitivity of force output and myosin light chain phosphorylation. The change in calcium sensitivity results at least in part from a 5-fold decrease in myosin light chain phosphatase activity. One of the few proteins thiophosphorylated under these conditions is the 130-kDa subunit of myosin light chain phosphatase. These results suggest that thiophosphorylation of this subunit leads to a decrease in the activity of the phosphatase, and that phosphorylation and dephosphorylation of the subunit may play a role in regulating myosin light chain phosphatase activity. Pretreatment of α-toxin-permeabilized smooth muscle with ATPγS (adenosine 5ʹ-O-(thiotriphosphate)) under conditions resulting in minimal (<1%) thiophosphorylation of the myosin light chain increases the subsequent calcium sensitivity of force output and myosin light chain phosphorylation. The change in calcium sensitivity results at least in part from a 5-fold decrease in myosin light chain phosphatase activity. One of the few proteins thiophosphorylated under these conditions is the 130-kDa subunit of myosin light chain phosphatase. These results suggest that thiophosphorylation of this subunit leads to a decrease in the activity of the phosphatase, and that phosphorylation and dephosphorylation of the subunit may play a role in regulating myosin light chain phosphatase activity.
Trinkle‐Mulcahy et al. (1995) studied this question.