title: Dun1 counts on rad53 to be turned on.
abstract: In a recent issue of Molecular Cell, Lee et al. (2008) demonstrate that the forkhead-associated (FHA) domain of Dun1, a Chk2-related kinase involved in DNA damage signaling, selectively binds a diphosphorylated motif found in its paralog and upstream regulator Rad53.
authors.affiliation: Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Avenue, Toronto, ON M5G 1X5, Canada.
authors.forename: Wei
authors.initials: W
authors.lastname: Zhang
authors.forename: Daniel
authors.initials: D
authors.lastname: Durocher
mesh_terms: D018797:Cell Cycle Proteins / Q000737:chemistry / Q000378:metabolism*; D064447:Checkpoint Kinase 2; D010766:Phosphorylation; D011485:Protein Binding; D011494:Protein Kinases / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D018797:Cell Cycle Proteins; D029701:Saccharomyces cerevisiae Proteins; D011494:Protein Kinases; C104169:DUN1 protein, S cerevisiae; D064447:Checkpoint Kinase 2; D017346:Protein Serine-Threonine Kinases; C067022:RAD53 protein, S cerevisiae