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• W2912672694 abstract "The ATR kinase controls cell cycle transitions and the DNA damage response. ATR activity is regulated through two ATR-activating proteins, ETAA1 and TOPBP1. To examine how each activator contributes to ATR signaling, we used quantitative mass spectrometry to identify changes in protein phosphorylation in ETAA1- or TOPBP1-deficient cells. We identified 724, 285, and 118 phosphosites to be regulated by TOPBP1, ETAA1, or both ATR activators, respectively. Gene ontology analysis of TOPBP1- and ETAA1-dependent phosphoproteins revealed TOPBP1 to be a primary ATR activator for replication stress, while ETAA1 regulates mitotic ATR signaling. Inactivation of ATR or ETAA1, but not TOPBP1, results in decreased Aurora B kinase activity during mitosis. Additionally, ATR activation by ETAA1 is required for proper chromosome alignment during metaphase and for a fully functional spindle assembly checkpoint response. Thus, we conclude that ETAA1 and TOPBP1 regulate distinct aspects of ATR signaling with ETAA1 having a dominant function in mitotic cells." @default.
• W2912672694 created "2019-02-21" @default.
• W2912672694 creator A5019856599 @default.
• W2912672694 creator A5037162298 @default.
• W2912672694 date "2019-02-12" @default.
• W2912672694 modified "2023-10-13" @default.
• W2912672694 title "Quantitative phosphoproteomics reveals mitotic function of the ATR activator ETAA1" @default.
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• W2912672694 doi "https://doi.org/10.1083/jcb.201810058" @default.
• W2912672694 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6446857" @default.
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• W2912672694 hasPublicationYear "2019" @default.
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