Phosphorylation of Mg2+-Dependent Protein Phosphatase α (Type 2Cα) by Casein Kinase II

Takayasu Kobayashi, Shin Ichiro Kanno, Takayuki Terasawa, Takashi Murakami, Motoko Ohnishi, Kenzo Ohtsuki, Akira Hiraga, Shinri Tamura

Research output: Contribution to journalArticlepeer-review

16 Citations (Scopus)


In this study we show that rat Mg2+-dependent protein phosphatase α (MPPα) expressed in Saccharomyces cerevisiae cells was phosphorylated on serine residues in vivo. The recombinant rat MPPα purified from Escherichia coli cells harboring an expression vector was phosphorylated in vitro by casein kinase II, but not by casein kinase I, to 1.5 mol phosphate per mol enzyme protein. Analysis by phosphopeptide mapping and amino acid analysis suggested that the sites of both in vivo and in vitro phosphorylation were the same and involved only serine residues. These results suggest that the rat MPPα expressed in yeast cells is phosphorylated by yeast casein kinase II in vivo. It is further proposed that the phosphorylation sites are located in the carboxyl terminal region of the enzyme molecule.

Original languageEnglish
Pages (from-to)484-489
Number of pages6
JournalBiochemical and biophysical research communications
Issue number1
Publication statusPublished - 1993 Aug 31

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'Phosphorylation of Mg2+-Dependent Protein Phosphatase α (Type 2Cα) by Casein Kinase II'. Together they form a unique fingerprint.

Cite this