Akt regulates RSK2 to alter phosphorylation level of H2A.X in breast cancer.

ABSTRACT: Histone H2AX (H2A.X) is a variant of the histone H2A family. Phosphorylation of H2A.X is a marker of DNA strand breaks and the presence or absence of H2A.X is closely related to tumor susceptibility and drug resistance. The present study found that the activity of the serine/threonine kinase Akt was negatively associated with H2A.X phosphorylated at the Ser16 site (H2A.X S16ph), but the mechanism of the inverse relationship remains elusive. The aim of the present study was to elucidate the mechanism of action between Akt and H2A.X S16ph and the exact role of this mechanism. Western blot analysis was performed to detect the regulatory association between p-Akt and H2A.X S16ph/p-RSK2, and immunoprecipitation and chromatin immunoprecipitation were performed to prove that Akt, RSK2 and H2A.X c

SUBMITTER: Guo ZF 

PROVIDER: S-EPMC7816342 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature