MYPT1 Protein Isoforms Are Differentially Phosphorylated by Protein Kinase G*

  title={MYPT1 Protein Isoforms Are Differentially Phosphorylated by Protein Kinase G*},
  author={Samantha L. Yuen and Ozgur Ogut and Frank V. Brozovich},
  booktitle={The Journal of biological chemistry},
Smooth muscle relaxation in response to NO signaling is due, in part, to a Ca(2+)-independent activation of myosin light chain (MLC) phosphatase by protein kinase G Iα (PKGIα). MLC phosphatase is a trimeric complex of a 20-kDa subunit, a 38-kDa catalytic subunit, and a 110-133-kDa myosin-targeting subunit (MYPT1). Alternative mRNA splicing produces four MYPT1 isoforms, differing by the presence or absence of a central insert and leucine zipper (LZ). The LZ domain of MYPT1 has been shown to be… CONTINUE READING


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Publications referenced by this paper.
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J. Biol. Chem • 1999
View 1 Excerpt

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