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MYO16 — PRKAR1A

Text-mined interactions from Literome

Patterson et al., Endothelium : journal of endothelial cell research 2000 : Although PKA activation attenuated thrombin induced myosin light chain ( MLC ) phosphorylation, PKA inhibition per se did not cause MLC phosphorylation or affect [ Ca2+ ] i
Zhang et al., Am J Physiol Gastrointest Liver Physiol 2005 (Hypertension, Portal) : Inhibition of PKA selectively increased myosin phosphorylation to 34.7 +/- 4.18 %
Yang et al., Life Sci 2005 : We found : ( a ) in the absence of Ca ( 2+ ) /CaM, PKA slightly phosphorylated MLC(20) and stimulated the Mg ( 2+ ) -ATPase activity of myosin , which was strengthened significantly by arachidonic acid ( ACAD ) ; ( b ) Ca ( 2+ ) -independent phosphorylation of myosin by PKA was obviously less efficient than both Ca ( 2+ ) -dependent and independent phosphorylation of myosin by MLCK ; ( c ) micro-amount of calponin could not increase the precipitation of myosin phosphorylated by PKA, but it increased the precipitation of myosin phosphorylated by MLCK, suggesting the presence of conformational differences between the myosins phosphorylated by PKA and by MLCK