TY - JOUR
T1 - Isoform-specific phosphorylation of fission yeast type 2C protein phosphatase
AU - Kobayashi, Takayasu
AU - Sadaie, Mahito
AU - Ohnishi, Motoko
AU - Wang, Hong
AU - Ikeda, Shoko
AU - Hanada, Masahito
AU - Yanagawa, Yuchio
AU - Nakajima, Tasuku
AU - Tamura, Shinri
N1 - Funding Information:
We are grateful to Dr. Paul Russell for provision of pREP1, pGEX-KG-ptc1+, S. pombe ptc2+, and ptc3+ genomic DNAs. We also thank Mr. Kimio Konno for technical assistance and Ms. Noriko Yamagata and Ms. Yuki Sato for secretarial assistance. This work was supported in part by a Grant-in-Aid for Scientific Research on Priority Areas No. 10169205 from the Ministry of Education, Science, Sports and Culture of Japan, ONO Medical Research Foundation, Smoking Research Foundation, Nakayama Foundation of Human Science, and the 1st Toyota High-tec Research Grant Program.
PY - 1998/10/9
Y1 - 1998/10/9
N2 - 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.
AB - 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.
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U2 - 10.1006/bbrc.1998.9467
DO - 10.1006/bbrc.1998.9467
M3 - Article
C2 - 9790950
AN - SCOPUS:0032500754
SN - 0006-291X
VL - 251
SP - 296
EP - 300
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -