1998年10月
Atypical protein kinase C lambda binds and regulates p70 S6 kinase
BIOCHEMICAL JOURNAL
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- 巻
- 335
- 号
- 開始ページ
- 417
- 終了ページ
- 424
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- 出版者・発行元
- PORTLAND PRESS
p70 S6 kinase (p70 S6K) has been implicated in the regulation of cell cycle progression. However, the mechanism of its activation is not fully understood. In the present work, evidence is provided that an atypical protein kinase C (PKC) isotype, PKC lambda, is indispensable, but not sufficient, for the activation of p70 S6K. Both the regulatory and kinase domains of PKC lambda associate directly with p70 S6K. Overexpression of the kinase domain without kinase activity or the regulatory domain of PKC lambda results in the suppression of the serum-induced activation of p70 S6K. In addition, two types of dominant-negative mutants of PKC lambda, as well as a kinase-deficient mutant of p70 S6K, suppress serum-induced DNA synthesis and E2F activation. The overexpression of the active form of PKC lambda, however, fails to activate p70 S6K. These results suggest that PKC lambda is a mediator in the regulation of p70 S6K activity and plays an important role in cell cycle progression.
- リンク情報
- ID情報
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- ISSN : 0264-6021
- PubMed ID : 9761742
- Web of Science ID : WOS:000076759700030