TY - JOUR
T1 - Phosphorylation of Mei2 and Ste11 by Pat1 Kinase Inhibits Sexual Differentiation via Ubiquitin Proteolysis and 14-3-3 Protein in Fission Yeast
AU - Kitamura, Kenji
AU - Katayama, Satoshi
AU - Dhut, Susheela
AU - Sato, Masamitsu
AU - Watanabe, Yoshinori
AU - Yamamoto, Masayuki
AU - Toda, Takashi
N1 - Funding Information:
We thank Drs. Sergio Moreno, Paul Nurse, Hiroaki Seino, Nobukazu Tanaka, and Fumio Yamao for strains, plasmids, and antibodies. We thank Drs. Jacqueline Hayles and Frank Uhlman for critical reading of the manuscript and useful suggestions. S.K. was supported by JSPS Postdoctoral Fellowships for Research Abroad. This work is supported by the ICRF and the Human Frontier Science Program Research Grant (T.T.), and by Grant-in-Aid for Specially Promoted Research from the Ministry of Education, Science, Sports, and Culture of Japan (Y.W. and M.Y.).
PY - 2001/9
Y1 - 2001/9
N2 - Fission yeast Pat1 kinase inhibits sexual differentiation by phosphorylating the meiotic inducer Mei2 and the transcription factor Ste11. Here, we show how Pat1 downregulates these proteins. Mei2 is degraded via a ubiquitin-proteasome pathway in a phosphorylation-dependent fashion. The E2 Ubc2 and the E3 Ubr1 are required for this proteolysis. In addition, Pat1 negatively regulates Ste11 via Rad24/14-3-3, thereby repressing mei2+ transcription. The Pat1 phosphorylation sites of Ste11 match the consensus recognition sequence for 14-3-3. Rad24 binds preferentially to phosphorylated Ste11, and this binding results in inhibition of the transcriptional activation capacity of Ste11. Overall, therefore, these results show that Pat1 coordinates concerted molecular mechanisms that govern the sexual differentiation developmental decision.
AB - Fission yeast Pat1 kinase inhibits sexual differentiation by phosphorylating the meiotic inducer Mei2 and the transcription factor Ste11. Here, we show how Pat1 downregulates these proteins. Mei2 is degraded via a ubiquitin-proteasome pathway in a phosphorylation-dependent fashion. The E2 Ubc2 and the E3 Ubr1 are required for this proteolysis. In addition, Pat1 negatively regulates Ste11 via Rad24/14-3-3, thereby repressing mei2+ transcription. The Pat1 phosphorylation sites of Ste11 match the consensus recognition sequence for 14-3-3. Rad24 binds preferentially to phosphorylated Ste11, and this binding results in inhibition of the transcriptional activation capacity of Ste11. Overall, therefore, these results show that Pat1 coordinates concerted molecular mechanisms that govern the sexual differentiation developmental decision.
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U2 - 10.1016/S1534-5807(01)00037-5
DO - 10.1016/S1534-5807(01)00037-5
M3 - Article
C2 - 11702950
AN - SCOPUS:0035462049
SN - 1534-5807
VL - 1
SP - 389
EP - 399
JO - Developmental Cell
JF - Developmental Cell
IS - 3
ER -