How ATR turns on: TopBP1 goes on ATRIP with ATR.
Copyright policy )How ATR turns on: TopBP1 goes on ATRIP with ATR.
In this issue of Genes & Development, Mordes and colleagues (pp. 1478-1489) reveal intriguing mechanistic insights into activation of the ATR (ATM and Rad3-related) kinase critical for DNA damage resistance. They identify conserved regulatory domains within ATR and its binding partner ATRIP (ATR-interacting protein), which are contacted by the ATR activator TopBP1. These discoveries expand on our understanding of the regulation of other PIKK family members, which also contain these domains, and illustrate how functional diversity has been achieved among these kinases.
- Howard Hughes Medical Institute United States
- Harvard University United States
- Brigham and Women's Faulkner Hospital United States
DNA-Binding Proteins, Humans, Nuclear Proteins, Cell Cycle Proteins, Ataxia Telangiectasia Mutated Proteins, Protein Serine-Threonine Kinases, Carrier Proteins, Conserved Sequence, Adaptor Proteins, Signal Transducing, DNA Damage, Protein Binding
DNA-Binding Proteins, Humans, Nuclear Proteins, Cell Cycle Proteins, Ataxia Telangiectasia Mutated Proteins, Protein Serine-Threonine Kinases, Carrier Proteins, Conserved Sequence, Adaptor Proteins, Signal Transducing, DNA Damage, Protein Binding
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