Isoform-specific phosphorylation of fission yeast type 2C protein phosphatase

Takayasu Kobayashi, Mahito Sadaie, Motoko Ohnishi, Hong Wang, Shoko Ikeda, Masahito Hanada, Yuchio Yanagawa, Tasuku Nakajima, Shinri Tamura

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)


Protein phosphatase 2C (PP2C) is one of the four major protein serine/threonine phosphatases of eukaryotes and is implicated in the regulation of various cellular functions. With the goal of elucidating the mechanism responsible for regulating PP2C functions, we investigated the significance of phosphorylation of fission yeast Ptc1, Ptc2, and Ptc3, the yeast orthologs of mammalian PP2C. Both Ptc2 and Ptc3 but not Ptc1 were phosphorylated stoichiometrically by casein kinase II on serine residues at their carboxy-terminal regions. Mutational analysis of Ptc2 and Ptc3 revealed that serine residues of the conserved sequence (Ser-X-Ser-X-X-(Glu/Asp) of these proteins were the phosphorylation sites. Interestingly, the activities of Ptc2 and Ptc3 were decreased 25 ± 7.5% and increased 55 ± 3.7%, respectively, by phosphorylation. In addition, the same site(s) of Ptc2 was phosphorylated when the protein was expressed in fission yeast cells. These results suggest that phosphorylation of PP2C plays important physiological roles in fission yeast cells.

Original languageEnglish
Pages (from-to)296-300
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - 1998 Oct 9


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