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Degradation of the SCF component Skp2 in cell-cycle phase G1 by the anaphase-promoting complex

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Listed:
  • Wenyi Wei

    (Dana–Farber Cancer Institute and Brigham and Women's Hospital)

  • Nagi G. Ayad

    (Harvard Medical School)

  • Yong Wan

    (Harvard Medical School)

  • Guo-Jun Zhang

    (Dana–Farber Cancer Institute and Brigham and Women's Hospital)

  • Marc W. Kirschner

    (Harvard Medical School)

  • William G. Kaelin

    (Dana–Farber Cancer Institute and Brigham and Women's Hospital
    Harvard Medical School)

Abstract

Cell-cycle transitions are driven by waves of ubiquitin-dependent degradation of key cell-cycle regulators. SCF (Skp1/Cullin/F-box protein) complexes and anaphase-promoting complexes (APC) represent two major classes of ubiquitin ligases whose activities are thought to regulate primarily the G1/S and metaphase/anaphase cell-cycle transitions, respectively1,2. The major target of the Skp1/Cul1/Skp2 (SCFSKP2) complex is thought to be the Cdk inhibitor p27 during S phase, whereas the principal targets for the APC are thought to be involved in chromatid separation (securin) and exit from mitosis (cyclin B). Although the role of the APC in mitosis is relatively clear, there is mounting evidence that APCs containing Cdh1 (APCCDH1) also have a function in the G1 phase of the cell cycle2,3. Here, we show that the F-box protein Skp2 is polyubiquitinated, and hence earmarked for destruction, by APCCDH1. As a result, accumulation of SCFSKP2 requires prior inactivation of APCCDH1. These findings provide an insight into the orchestration of SCF and APC activities during cell-cycle progression, and into the involvement of the APC in G1.

Suggested Citation

  • Wenyi Wei & Nagi G. Ayad & Yong Wan & Guo-Jun Zhang & Marc W. Kirschner & William G. Kaelin, 2004. "Degradation of the SCF component Skp2 in cell-cycle phase G1 by the anaphase-promoting complex," Nature, Nature, vol. 428(6979), pages 194-198, March.
    • Handle: RePEc:nat:nature:v:428:y:2004:i:6979:d:10.1038_nature02381
    DOI: 10.1038/nature02381
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    Cited by:

    1. Ji Min Lee & Henrik M. Hammarén & Mikhail M. Savitski & Sung Hee Baek, 2023. "Control of protein stability by post-translational modifications," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    2. Nishtha Pandey & P K Vinod, 2018. "Mathematical modelling of reversible transition between quiescence and proliferation," PLOS ONE, Public Library of Science, vol. 13(6), pages 1-15, June.
    3. Jeffrey V Wong & Bochong Li & Lingchong You, 2012. "Tension and Robustness in Multitasking Cellular Networks," PLOS Computational Biology, Public Library of Science, vol. 8(4), pages 1-12, April.
    4. Shizhong Ke & Fabin Dang & Lin Wang & Jia-Yun Chen & Mandar T. Naik & Wenxue Li & Abhishek Thavamani & Nami Kim & Nandita M. Naik & Huaxiu Sui & Wei Tang & Chenxi Qiu & Kazuhiro Koikawa & Felipe Batal, 2024. "Reciprocal antagonism of PIN1-APC/CCDH1 governs mitotic protein stability and cell cycle entry," Nature Communications, Nature, vol. 15(1), pages 1-21, December.
    5. Sang Bae Lee & Luciano Garofano & Aram Ko & Fulvio D’Angelo & Brulinda Frangaj & Danika Sommer & Qiwen Gan & KyeongJin Kim & Timothy Cardozo & Antonio Iavarone & Anna Lasorella, 2022. "Regulated interaction of ID2 with the anaphase-promoting complex links progression through mitosis with reactivation of cell-type-specific transcription," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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