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

A Lopez-Girona1, B Furnari, O Mondesert

  • 1Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA.

Nature
|January 29, 1999
PubMed

Insights

Rad24, a 14-3-3 protein, controls the location of Cdc25 in fission yeast cells. DNA damage triggers Chk1 and Rad24 to export Cdc25 from the nucleus, enforcing the DNA-damage checkpoint.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • DNA damage triggers cell-cycle checkpoints to allow DNA repair before cell division.
  • The Chk1 protein phosphorylates Cdc25, a mitotic inducer, to enforce this checkpoint.
  • 14-3-3 proteins bind to phosphorylated Cdc25, but their regulatory role remains unclear.

Purpose of the Study:

  • To investigate the role of the 14-3-3 protein Rad24 in the DNA-damage checkpoint.
  • To elucidate how 14-3-3 proteins regulate the intracellular distribution of Cdc25.

Main Methods:

  • Fission yeast genetics
  • Analysis of protein localization (nuclear accumulation/export)
  • Checkpoint assays
  • Site-directed mutagenesis of a putative nuclear-export signal in Rad24.

Main Results:

  • Elimination of Rad24 leads to nuclear accumulation of Cdc25.
  • DNA-damage checkpoint activation induces net nuclear export of Cdc25, dependent on Chk1 and Rad24.
  • Mutation of a nuclear-export signal in Rad24 disrupts Rad24 localization, Cdc25 export, and the DNA-damage checkpoint.

Conclusions:

  • Rad24 regulates the intracellular distribution of Cdc25 in response to DNA damage.
  • Rad24 functions as a nuclear-export signal, enhancing Cdc25 export from the nucleus.
  • This mechanism is crucial for enforcing the DNA-damage checkpoint in fission yeast.

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