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Nuclear localization of Cdc25 is regulated by DNA damage and a 14-3-3 protein

Author

Listed:
  • Antonia Lopez-Girona
  • Beth Furnari
  • Odile Mondesert

    (The Scripps Research Institute)

  • Paul Russell

    (The Scripps Research Institute)

Abstract

DNA damage activates a cell-cycle checkpoint that prevents mitosis while DNA repair is under way1. The protein Chk1 enforces this checkpoint by phosphorylating the mitotic inducer Cdc25 (2–6). Phosphorylation of Cdc25 by Chk1 creates a binding site in Cdc25 for 14-3-3 proteins5,6,7,8, but it is not known how 14-3-3 proteins regulate Cdc25. Rad24 is a 14-3-3 protein that is important in the DNA-damage checkpoint in fission yeast9. Here we show that Rad24 controls the intracellular distribution of Cdc25. Elimination of Rad24 causes nuclear accumulation of Cdc25. Activation of the DNA-damage checkpoint causes the net nuclear export of Cdc25 by a process that requires Chk1, Rad24 and nuclear-export machinery. Mutation of a putative nuclear-export signal in Rad24 impairs the nuclear exclusion of Rad24, the damage-induced nuclear export of Cdc25 and the damage checkpoint. Thus, Rad24 appears to function as an attachable nuclear-export signal that enhances the nuclear export of Cdc25 in response to DNA damage.

Suggested Citation

  • Antonia Lopez-Girona & Beth Furnari & Odile Mondesert & Paul Russell, 1999. "Nuclear localization of Cdc25 is regulated by DNA damage and a 14-3-3 protein," Nature, Nature, vol. 397(6715), pages 172-175, January.
    • Handle: RePEc:nat:nature:v:397:y:1999:i:6715:d:10.1038_16488
    DOI: 10.1038/16488
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    Cited by:

    1. Zhuo Han & Rui Wang & Pengliang Chi & Zihan Zhang & Ling Min & Haizhan Jiao & Guojin Ou & Dan Zhou & Dandan Qin & Chengpeng Xu & Zheng Gao & Qianqian Qi & Jialu Li & Yuechao Lu & Xiang Wang & Jing Che, 2024. "The subcortical maternal complex modulates the cell cycle during early mammalian embryogenesis via 14-3-3," Nature Communications, Nature, vol. 15(1), pages 1-18, December.

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