Posphorylation of three particulate proteins with molecular masses of 34, 26, and 22 kDa was stimulated in the presence of cyclic AMP / 3-isobutyl-1-methylxanthine in saponin-permeabilized rat parotid acinar cells. When the particulate fraction isolated from the cells labeled with [γ-32P]ATP was incubated at 30°C, dephosphorylation of the 26 kDa phosphoprotein occurred in the presence of Mg2+ or Mn2+. Okadaic acid had no effect on the Mg2+-dependent dephosphorylation of the 26 kDa phosphoprotein. Addition of the recombinant type 2C phosphatase, Mg2+-dependent and okadaic acid-insensitive phosphatase, caused a remarkable dephosphorylation of the 26 kDa phosphoprotein. These observations strongly suggest type 2C phosphatase is involved in the dephosphorylation of the 26 kDa phosphoprotein.
|Number of pages||7|
|Journal||Biochemical and biophysical research communications|
|Publication status||Published - 1994 Apr 15|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology