Histone H2AX is phosphorylated in an ATR-dependent manner in response to replicational stress.

Article Details

Citation

Ward IM, Chen J

Histone H2AX is phosphorylated in an ATR-dependent manner in response to replicational stress.

J Biol Chem. 2001 Dec 21;276(51):47759-62. Epub 2001 Oct 22.

PubMed ID
11673449 [ View in PubMed
]
Abstract

H2AX, a member of the histone H2A family, is rapidly phosphorylated in response to ionizing radiation. This phosphorylation, at an evolutionary conserved C-terminal phosphatidylinositol 3-OH-kinase-related kinase (PI3KK) motif, is thought to be critical for recognition and repair of DNA double strand breaks. Here we report that inhibition of DNA replication by hydroxyurea or ultraviolet irradiation also induces phosphorylation and foci formation of H2AX. These phospho-H2AX foci colocalize with proliferating cell nuclear antigen (PCNA), BRCA1, and 53BP1 at the arrested replication fork in S phase cells. This response is ATR-dependent but does not require ATM or Hus1. Our findings suggest that, in addition to its role in the recognition and repair of double strand breaks, H2AX also participates in the surveillance of DNA replication.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Serine/threonine-protein kinase ATRQ13535Details