Abstract:
: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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Kobayashi T,Sadaie M,Ohnishi M,Wang H,Ikeda S,Hanada M,Yanagawa Y,Nakajima T,Tamura Sdoi
10.1006/bbrc.1998.9467subject
Has Abstractpub_date
1998-10-09 00:00:00pages
296-300issue
1eissn
0006-291Xissn
1090-2104pii
S0006-291X(98)99467-0journal_volume
251pub_type
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