DCLRE1C (ARTEMIS) possesses an intrinsic 5' to 3' exonuclease activity. Upon binding to PRKDC (DNA-PKcs) at DNA double strand breaks (DSBs) and undergoing PRKDC-mediated phosphorylation, DCLRE1C acquires endonucleolytic activity towards 5' and 3' overhangs at DNA double strand breaks, and it also acquires a hairpin opening activity (Ma et al. 2002, Ma et al. 2005). Autophosphorylation of PRKDC, although not required for the kinase activity of PRKDC, is needed for the activation of the endonucleolytic activity of DCLRE1C, probably by inducing a conformational change in PRKDC that provides DCLRE1C with access to DNA ends (Goodarzi et al. 2006, Niewolik et al. 2006, Jiang et al. 2015).
Zha, S, Crowe, JL, Dubois, RL, Nakajima, S, Lan, L, Liu, C, Yu, X, Liu, X, Li, C, Wang, Y, Lee, BJ, Jiang, W
Ye, R, Härer, C, Walker, SA, Douglas, P, Marchetti, C, Lees-Miller, SP, Jeggo, PA, Goodarzi, AA, Morrice, N, Riballo, E, Yu, Y
Lieber, MR, Schwarz, K, Lu, H, Pannicke, U, Niewolik, D, Ma, Y
Kulesza, P, Schwarz, K, Lieber, MR, Lu, H, Wang, LC, Pannicke, U, Zandi, E, Niewolik, D, Ma, Y
Schwarz, K, Pannicke, U, Lieber, MR, Ma, Y
endonuclease activity of p-T2609,S2612,T2638,T2647-PRKDC:XRCC5:XRCC6:p-S516,S645-DCLRE1C:DNA DSB ends [nucleoplasm]
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