MTORC2 Regulates Non-homologous End Joining Through Modulating the Temporal Dynamics of 53BP1.

ABSTRACT: DNA damage repair is a critical biological process that maintains genomic integrity, and its dysregulation is closely related to tumorigenesis. To reveal the roles of mammalian target of rapamycin complex 2 (mTORC2) in DNA damage response (DDR), we investigated the temporal changes of cellular protein phosphorylation in mTORC2 deficient renal cancer cells in response to DNA double-strand break (DSB) induced by ionizing radiation (IR) using quantitative phosphoproteomics. The results showed that knockdown of Rictor, a specific component of mTORC2, induced profound changes in the dynamics of protein phosphorylation in response to IR. Intriguingly, the phosphorylation levels of multiple signaling molecules from the non-homologous end joining (NHEJ) pathway were affected by Rictor. Mechanistic

SUBMITTER: Wang C 

PROVIDER: S-EPMC12356323 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature