Regulation of the cell cycle at the G1-S transition by proteolysis of cyclin E and p27Kip1

Kei Ichi Nakayama, Shigetsugu Hatakeyama, Keiko Nakayama

研究成果: ジャーナルへの寄稿評論記事

190 引用 (Scopus)

抄録

The transition from G1 phase to S phase of the mammalian cell cycle is controlled by many positive and negative regulators, among which cyclin E and p27Kip1, respectively, undergo the most marked changes in concentration at this transition. The abundance of both cyclin E and p27Kip1 is regulated predominantly by posttranslational mechanisms, in particular by proteolysis mediated by the ubiquitin-proteasome pathway. Cyclin E and p27Kip1 each bind to and undergo polyubiquitination by the same ubiquitin ligase, known as SCFSkp2. The degradation of cyclin E and p27Kip1 is greatly impaired in Skp2-deficient mice, resulting in intracellular accumulation of these proteins. In this article, recent progress in characterization of the molecular mechanisms that control the proteolysis of cyclin E and p27Kip1 is reviewed.

元の言語英語
ページ(範囲)853-860
ページ数8
ジャーナルBiochemical and Biophysical Research Communications
282
発行部数4
DOI
出版物ステータス出版済み - 1 1 2001

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Proteolysis
Cyclin E
Cell Cycle
Cells
Ubiquitin
G1 Phase
Proteasome Endopeptidase Complex
Ligases
S Phase
Degradation
Proteins

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

Regulation of the cell cycle at the G1-S transition by proteolysis of cyclin E and p27Kip1. / Nakayama, Kei Ichi; Hatakeyama, Shigetsugu; Nakayama, Keiko.

:: Biochemical and Biophysical Research Communications, 巻 282, 番号 4, 01.01.2001, p. 853-860.

研究成果: ジャーナルへの寄稿評論記事

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AB - The transition from G1 phase to S phase of the mammalian cell cycle is controlled by many positive and negative regulators, among which cyclin E and p27Kip1, respectively, undergo the most marked changes in concentration at this transition. The abundance of both cyclin E and p27Kip1 is regulated predominantly by posttranslational mechanisms, in particular by proteolysis mediated by the ubiquitin-proteasome pathway. Cyclin E and p27Kip1 each bind to and undergo polyubiquitination by the same ubiquitin ligase, known as SCFSkp2. The degradation of cyclin E and p27Kip1 is greatly impaired in Skp2-deficient mice, resulting in intracellular accumulation of these proteins. In this article, recent progress in characterization of the molecular mechanisms that control the proteolysis of cyclin E and p27Kip1 is reviewed.

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