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• W2050876926 abstract "In this study, we mutated autophosphorylation sites in Rad53 based on their conservation with previously identified autophosphorylation sites in the mammalian Rad53 ortholog, Chk2. As with wild-type Rad53, the autophosphorylation mutant, rad53-TA, undergoes Mec1/Tel1-dependent interactions with Rad9 and Dun1 in response to genotoxic stress. Whereas rad53-TA in vitro kinase activity is severely impaired, the rad53-TA strains are not completely deficient for cell-cycle checkpoint functions, indicating that the mutant kinase retains a basal level of function. We describe a genetic interaction among Rad53, Dun1, and the 14-3-3 proteins Bmh1 and Bmh2 and present evidence that 14-3-3 proteins directly facilitate Rad53 function in vivo . The data presented account for the previously observed checkpoint defects associated with 14-3-3 mutants in Saccharomyces pombe and Saccharomyces cerevisiae . The 14-3-3 functional interaction appears to modulate Rad53 activity, reminiscent of 14-3-3's effect on human Raf1 kinase and distinct from the indirect mode of regulation by 14-3-3 observed for Chk1 or Cdc25." @default.
• W2050876926 created "2016-06-24" @default.
• W2050876926 creator A5006649962 @default.
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• W2050876926 date "2007-02-20" @default.
• W2050876926 modified "2023-09-29" @default.
• W2050876926 title "The <i>Saccharomyces cerevisiae</i> 14-3-3 proteins Bmh1 and Bmh2 directly influence the DNA damage-dependent functions of Rad53" @default.
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• W2050876926 doi "https://doi.org/10.1073/pnas.0611259104" @default.
• W2050876926 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1797148" @default.
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