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Background MLC phosphatase is a trimeric enzyme composed of a catalytic subunit, a 20-kDa subunit of unknown function, and a myosin targeting subunit (MYPT1). During NO stimulation, PKGIa mediated phosphorylation of MYPT1 increases MLC phosphatase activity, which produces a decrease in force. Further, alternative splicing of a 3’ exon produces two MYPT1 isoforms, which differ by the presence or absence of a leucine zipper (LZ); a LZ+ MYPT1 isoform is required for PKGIa induced smooth muscle relaxation.

Differential phosphorylation of LZ+/LZ- MYPT1 isoforms by PKGIα: implication for vascular reactivity