MYPT1 Protein Isoforms Are Differentially Phosphorylated by Protein Kinase G*

@inproceedings{Yuen2011MYPT1PI,
  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},
  year={2011}
}
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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References

Publications referenced by this paper.
Showing 1-2 of 2 references

Physiology of the Gastrointestinal Tract

D. J. Hartshorne
1987
View 10 Excerpts
Highly Influenced

37385–37390 PKG Differentially Phosphorylates MYPT1 Isoforms

J. Feng, M. Ito, +4 authors T. Nakano
J. Biol. Chem • 1999
View 1 Excerpt

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