title: TOPping up ATR activity.
abstract: The nuclear protein kinase ATR is a key regulator of genome integrity that functions at checkpoints for damaged or incompletely replicated DNA. In this issue of Cell, Kumagai et al. (2006) shed light on the molecular mechanism that controls ATR. They report that a physical interaction between ATR and a distinct domain of TopBP1 greatly enhances ATR kinase activity.
authors.affiliation: Institute of Cancer Biology and Centre for Genotoxic Stress Research, Danish Cancer Society, Strandboulevarden 49, DK-2100 Copenhagen, Denmark. jb@cancer.dk
authors.forename: Jiri
authors.initials: J
authors.lastname: Bartek
authors.forename: Niels
authors.initials: N
authors.lastname: Mailand
mesh_terms: D000818:Animals; D064007:Ataxia Telangiectasia Mutated Proteins; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism*; D018797:Cell Cycle Proteins / Q000235:genetics / Q000378:metabolism*; D004260:DNA Repair; D004268:DNA-Binding Proteins; D004789:Enzyme Activation; D005786:Gene Expression Regulation; D006801:Humans; D008957:Models, Genetic; D009687:Nuclear Proteins; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism*; D029867:Xenopus Proteins / Q000235:genetics / Q000378:metabolism*
chemical_list: D002352:Carrier Proteins; D018797:Cell Cycle Proteins; D004268:DNA-Binding Proteins; D009687:Nuclear Proteins; C110513:TOPBP1 protein, human; D029867:Xenopus Proteins; C576898:Atr protein, Xenopus; D064007:Ataxia Telangiectasia Mutated Proteins; D017346:Protein Serine-Threonine Kinases