MISC

2000年12月15日

Regulation of Wee1 kinase in response to protein synthesis inhibition

FEBS Letters
  • Masako Suda
  • ,
  • Shinya Yamada
  • ,
  • Takashi Toda
  • ,
  • Tokichi Miyakawa
  • ,
  • Dai Hirata

486
3
開始ページ
305
終了ページ
309
記述言語
英語
掲載種別
DOI
10.1016/S0014-5793(00)02299-7

To investigate the mechanism coupling growth (protein synthesis) with cell division, we examined the relationship between the tyrosine kinase Wee1 that inhibits Cdc2-Cdc13 mitosis-inducing kinase by phosphorylating it, and protein synthesis inhibition in fission yeast. The wee1-50 mutant showed supersensitivity to protein synthesis inhibitor, cycloheximide. Wee1 was essential for the G2 delay upon a partial inhibition of protein synthesis. Indeed, the protein synthesis inhibition caused an increase in the Wee1 protein by the Sty1/Spc1 MAPK-dependent transcriptional and the Sty1/Spc1 MAPK-independent post-transcriptional regulations. Further, the results indicated that the post-transcriptional regulation is important for the G2 delay. Copyright (C) 2000 Federation of European Biochemical Societies.

リンク情報
DOI
https://doi.org/10.1016/S0014-5793(00)02299-7
CiNii Articles
http://ci.nii.ac.jp/naid/10010560539
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/11119724
ID情報
  • DOI : 10.1016/S0014-5793(00)02299-7
  • ISSN : 0014-5793
  • CiNii Articles ID : 10010560539
  • PubMed ID : 11119724
  • SCOPUS ID : 0034672545

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