title: H2AX regulates meiotic telomere clustering.
abstract: The histone H2A variant H2AX is phosphorylated in response to DNA double-strand breaks originating from diverse origins, including dysfunctional telomeres. Here, we show that normal mitotic telomere maintenance does not require H2AX. Moreover, H2AX is dispensable for the chromosome fusions arising from either critically shortened or deprotected telomeres. However, H2AX has an essential role in controlling the proper topological distribution of telomeres during meiotic prophase I. Our results suggest that H2AX is a downstream effector of the ataxia telangiectasia-mutated kinase in controlling telomere movement during meiosis.
authors.affiliation: Experimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
authors.forename: Oscar
authors.initials: O
authors.lastname: Fernandez-Capetillo
authors.forename: Bodo
authors.initials: B
authors.lastname: Liebe
authors.forename: Harry
authors.initials: H
authors.lastname: Scherthan
authors.forename: Andre
authors.initials: A
authors.lastname: Nussenzweig
mesh_terms: D000818:Animals; D006657:Histones / Q000172:deficiency / Q000378:metabolism*; D017404:In Situ Hybridization, Fluorescence; D008540:Meiosis / Q000502:physiology*; D051379:Mice; D016615:Telomere / Q000502:physiology*
chemical_list: D006657:Histones; C475961:gamma-H2AX protein, mouse