Ontology highlight
ABSTRACT:
SUBMITTER: Singh N
PROVIDER: S-EPMC3437875 | biostudies-literature | 2012 Sep
REPOSITORIES: biostudies-literature
Singh Namit N Basnet Harihar H Wiltshire Timothy D TD Mohammad Duaa H DH Thompson James R JR Héroux Annie A Botuyan Maria Victoria MV Yaffe Michael B MB Couch Fergus J FJ Rosenfeld Michael G MG Mer Georges G
Proceedings of the National Academy of Sciences of the United States of America 20120820 36
Tyr142, the C-terminal amino acid of histone variant H2A.X is phosphorylated by WSTF (Williams-Beuren syndrome transcription factor), a component of the WICH complex (WSTF-ISWI chromatin-remodeling complex), under basal conditions in the cell. In response to DNA double-strand breaks (DSBs), H2A.X is instantaneously phosphorylated at Ser139 by the kinases ATM and ATR and is progressively dephosphorylated at Tyr142 by the Eya1 and Eya3 tyrosine phosphatases, resulting in a temporal switch from a p ...[more]