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• W2013180816 abstract "Forkhead-associated (FHA) domains recognize phosphothreonines, and SQ/TQ cluster domains (SCDs) contain concentrated phosphorylation sites for ATM/ATR-like DNA-damage-response kinases. The Rad53-SCD1 has dual functions in regulating the activation of the Rad53-Dun1 checkpoint kinase cascade but with unknown molecular mechanisms. Here we present structural, biochemical, and genetic evidence that Dun1-FHA possesses an unprecedented diphosphothreonine-binding specificity. The Dun1-FHA has >100-fold increased affinity for diphosphorylated relative to monophosphorylated Rad53-SCD1 due to the presence of two separate phosphothreonine-binding pockets. In vivo, any single threonine of Rad53-SCD1 is sufficient for Rad53 activation and RAD53-dependent survival of DNA damage, but two adjacent phosphothreonines in the Rad53-SCD1 and two phosphothreonine-binding sites in the Dun1-FHA are necessary for Dun1 activation and DUN1-dependent transcriptional responses to DNA damage. The results uncover a phospho-counting mechanism that regulates the specificity of SCD, and provide mechanistic insight into a role of multisite phosphorylation in DNA-damage signaling." @default.
• W2013180816 created "2016-06-24" @default.
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• W2013180816 date "2008-06-01" @default.
• W2013180816 modified "2023-10-16" @default.
• W2013180816 title "Diphosphothreonine-Specific Interaction between an SQ/TQ Cluster and an FHA Domain in the Rad53-Dun1 Kinase Cascade" @default.
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• W2013180816 doi "https://doi.org/10.1016/j.molcel.2008.05.013" @default.
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• W2013180816 hasPublicationYear "2008" @default.
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