| Literature DB >> 27723720 |
Thomas E Bass1, Jessica W Luzwick1, Gina Kavanaugh1, Clinton Carroll1, Huzefa Dungrawala1, Gloria G Glick1, Michael D Feldkamp2, Reid Putney2, Walter J Chazin2, David Cortez1.
Abstract
The ATR checkpoint kinase coordinates cellular responses to DNA replication stress. Budding yeast contain three activators of Mec1 (the ATR orthologue); however, only TOPBP1 is known to activate ATR in vertebrates. We identified ETAA1 as a replication stress response protein in two proteomic screens. ETAA1-deficient cells accumulate double-strand breaks, sister chromatid exchanges, and other hallmarks of genome instability. They are also hypersensitive to replication stress and have increased frequencies of replication fork collapse. ETAA1 contains two RPA-interaction motifs that localize ETAA1 to stalled replication forks. It also interacts with several DNA damage response proteins including the BLM/TOP3α/RMI1/RMI2 and ATR/ATRIP complexes. It binds ATR/ATRIP directly using a motif with sequence similarity to the TOPBP1 ATR-activation domain; and like TOPBP1, ETAA1 acts as a direct ATR activator. ETAA1 functions in parallel to the TOPBP1/RAD9/HUS1/RAD1 pathway to regulate ATR and maintain genome stability. Thus, vertebrate cells contain at least two ATR-activating proteins.Entities:
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Year: 2016 PMID: 27723720 PMCID: PMC5245861 DOI: 10.1038/ncb3415
Source DB: PubMed Journal: Nat Cell Biol ISSN: 1465-7392 Impact factor: 28.824