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Vol. 11, Issue 1, 1-11, January 2000
Departments of Molecular Biology and Cell Biology, The Scripps
Research Institute, La Jolla, California, 92037
The protein kinase Chk1 enforces the DNA damage checkpoint. This
checkpoint delays mitosis until damaged DNA is repaired. Chk1 regulates
the activity and localization of Cdc25, the tyrosine phosphatase that
activates the cdk Cdc2. Here we report that Mik1, a tyrosine kinase
that inhibits Cdc2, is positively regulated by the DNA damage
checkpoint. Mik1 is required for checkpoint response in strains that
lack Cdc25. Long-term DNA damage checkpoint arrest fails in
mik1 cells. DNA damage increases Mik1 abundance in a
Chk1-dependent manner. Ubiquitinated Mik1 accumulates in a proteasome
mutant, which indicates that Mik1 normally has a short half-life. Thus,
the DNA damage checkpoint might regulate Mik1 degradation. Mik1 protein
and mRNA oscillate during the unperturbed cell cycle, with peak amounts
detected around S phase. These data indicate that regulation of Mik1
abundance helps to couple mitotic onset to the completion of DNA
replication and repair. Coordinated negative regulation of Cdc25 and
positive regulation of Mik1 ensure the effective operation of the DNA
damage checkpoint.
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