title: Destroying the ring: Freeing DNA from Ku with ubiquitin.
abstract: The Ku heterodimer, consisting of the proteins Ku70 and Ku80, is the central component of the non-homologous end joining (NHEJ) pathway of double strand break (DSB) repair. Ku is able to recognize and bind a DSB by virtue of its ring-like structure. Both pre-repair and topologically trapped post-repair Ku heterodimers are thought to be inhibitory to multiple cellular processes. Thus, a regulated mechanism for the removal of Ku from chromatin was predicted to exist. Recent evidence shows that Ku80 is removed from DNA through a ubiquitin-mediated process. Similar processes have been shown to be involved in the regulated dissociation of a host of other proteins from chromatin, and this appears to be a general and conserved mechanism for the regulation of chromatin-associated factors. A potential mechanism for this pathway is discussed.
authors.affiliation: Laboratory of Chromosome and Cell Biology, Rockefeller University, 1230 York Avenue, New York, NY 10065, USA. PostowL@rockfeller.edu
authors.forename: Lisa
authors.initials: L
authors.lastname: Postow
mesh_terms: D034961:Antigens, Nuclear / Q000737:chemistry / Q000378:metabolism*; D004247:DNA / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D053903:DNA Breaks, Double-Stranded; D004260:DNA Repair; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D000072200:Ku Autoantigen; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D055503:Protein Multimerization; D025801:Ubiquitin / Q000378:metabolism*
chemical_list: D034961:Antigens, Nuclear; D004268:DNA-Binding Proteins; D025801:Ubiquitin; D004247:DNA; C000606509:Xrcc6 protein, human; D000072200:Ku Autoantigen