Cdc2 tyrosine phosphorylation is not required for the S-phase DNA damage checkpoint in fission yeast
Graduate School of Biomedical Sciences; Department of Biochemistry and Molecular Pharmacology
Life Sciences | Medicine and Health Sciences
The S-phase DNA damage checkpoint slows replication when damage occurs during S phase. Cdc25, which activates Cdc2 by dephosphorylating tyrosine-15, has been shown to be a downstream target of the checkpoint in metazoans, but its role is not clear in fission yeast. The dephosphorylation of Cdc2 has been assumed not to play a role in S-phase regulation because cells replicate in the absence of Cdc25, demonstrating that tyrosine-15 phosphorylated dc2 is sufficient for S phase. However, it has been reported recently that Cdc25 is involved in the slowing of S phase in response to damage in fission yeast, suggesting a modulatory role for Cdc2 dephosphorylation in S phase. We have investigated the role of Cdc25 and the tyrosine phosphorylation of Cdc2 in the S-phase damage checkpoint, and our results show that Cdc2 phosphorylation is not a target of the checkpoint. The checkpoint was not compromised in a Cdc25 overexpressing strain, a strain carrying nonphosphorylatable form of Cdc2, or in a strain lacking Cdc25. Our results are consistent with a strictly Cdc2-Y15 phosphorylation-independent mechanism of the fission yeast S-phase DNA damage checkpoint.
DOI of Published Version
Cell Cycle. 2006 Nov 1;5(21):2495-500. Epub 2006 Sep 19.
Cell cycle (Georgetown, Tex.)
Kommajosyula N, Rhind NR. (2006). Cdc2 tyrosine phosphorylation is not required for the S-phase DNA damage checkpoint in fission yeast. Morningside Graduate School of Biomedical Sciences Student Publications. https://doi.org/10.4161/cc.5.21.3423. Retrieved from https://escholarship.umassmed.edu/gsbs_sp/620