Novel in vitro and in vivo phosphorylation sites on protein phosphatase 1 inhibitor CPI-17.

@article{Dubois2003NovelIV,
  title={Novel in vitro and in vivo phosphorylation sites on protein phosphatase 1 inhibitor CPI-17.},
  author={Thierry Dubois and Steven B. Howell and Eva Zemlickova and Mich{\`e}le Learmonth and Andy D Cronshaw and Alastair Aitken},
  journal={Biochemical and biophysical research communications},
  year={2003},
  volume={302 2},
  pages={
          186-92
        }
}
CPI-17 is a protein phosphatase 1 (PP1) inhibitor that has been shown to act on the myosin light chain phosphatase. CPI-17 is phosphorylated on Thr-38 in vivo, thus enhancing its ability to inhibit PP1. Thr-38 has been shown to be the target of several protein kinases in vitro. Originally, the expression of CPI-17 was proposed to be smooth muscle specific. However, it has recently been found in platelets and we show in this report that it is endogenously phosphorylated in brain on Ser-128 in a… CONTINUE READING

Citations

Publications citing this paper.
SHOWING 1-10 OF 13 CITATIONS

Myosin phosphatase: Structure, regulation and function

  • Molecular and Cellular Biochemistry
  • 2004
VIEW 7 EXCERPTS
CITES BACKGROUND
HIGHLY INFLUENCED