Abstract:
: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.
journal_name
Dev Celljournal_title
Developmental cellauthors
Kitamura K,Katayama S,Dhut S,Sato M,Watanabe Y,Yamamoto M,Toda Tdoi
10.1016/s1534-5807(01)00037-5keywords:
subject
Has Abstractpub_date
2001-09-01 00:00:00pages
389-99issue
3eissn
1534-5807issn
1878-1551pii
S1534-5807(01)00037-5journal_volume
1pub_type
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