biostudies-literatureZang YTippins FoundationNIDDK NIH HHSUPMC Hillman Cancer Center Animal Facility and the Tissue and Research Pathology ServicesNCI NIH HHSMellam Family FoundationNIGMS NIH HHS198-207https://www.ebi.ac.uk/biostudies/studies/S-EPMC5761340biostudies-literatureUnknown415ELL2 is an androgen-responsive gene that is expressed by prostate epithelial cells and is frequently down-regulated in prostate cancer. Deletion of Ell2 in the murine prostate induced murine prostatic intraepithelial neoplasia and ELL2 knockdown enhanced proliferation and migration in C4-2 prostate cancer cells. Here, knockdown of ELL2 sensitized prostate cancer cells to DNA damage and overexpression of ELL2 protected prostate cancer cells from DNA damage. Knockdown of ELL2 impaired non-homologous end joining repair but not homologous recombination repair. Transfected ELL2 co-immunoprecipitated with both Ku70 and Ku80 proteins. ELL2 could bind to and co-accumulate with Ku70/Ku80 proteins at sites of DNA damage. Knockdown of ELL2 dramatically inhibited Ku70 and Ku80 recruitment and retentioCancer lettersELL2 regulates DNA non-homologous end joining (NHEJ) repair in prostate cancer cells.PMC5761340R01 GM118833P30 CA0479041R50CA211242P50 CA180995P30CA0479049R01CA186780T32 DK0077741P50CA180995R50 CA211242R01 CA186780Xue BNelson JBZang YZhou YYang DAi JShan YQiu XPascal LEWang SLan LWang ZWei LZhong MfalseELL2 regulates DNA non-homologous end joining (NHEJ) repair in prostate cancer cells.ELL2 is an androgen-responsive gene that is expressed by prostate epithelial cells and is frequently down-regulated in prostate cancer. Deletion of Ell2 in the murine prostate induced murine prostatic intraepithelial neoplasia and ELL2 knockdown enhanced proliferation and migration in C4-2 prostate cancer cells. Here, knockdown of ELL2 sensitized prostate cancer cells to DNA damage and overexpression of ELL2 protected prostate cancer cells from DNA damage. Knockdown of ELL2 impaired non-homologous end joining repair but not homologous recombination repair. Transfected ELL2 co-immunoprecipitated with both Ku70 and Ku80 proteins. ELL2 could bind to and co-accumulate with Ku70/Ku80 proteins at sites of DNA damage. Knockdown of ELL2 dramatically inhibited Ku70 and Ku80 recruitment and retentio2018-01-01T00:00:00Z2018 Feb2026-05-06T00:21:51.994Z2019-08-04T07:05:39ZS-EPMC57613402917999810.1016/j.canlet.2017.11.028