MDM2 ubiquitinates DYRK2 in the nucleus, leading to proteasome-mediated degradation of DYRK2. This results in the removal of nuclear DYRK2 and exclusive localization of DYRK2 in the cytosol in the absence of DNA damage. ATM-mediated phosphorylation of DYRK2 prevents ubiquitination of DYRK2 by MDM2, leading to accumulation of nuclear DYRK2 (Taira et al. 2010).
Yamamoto, H, Miki, Y, Taira, N, Yoshida, K, Yamaguchi, T
ubiquitin protein ligase activity of p-S166,S188-MDM2 dimer, p-S166,S188-MDM2:MDM4 [nucleoplasm]
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