The interplay between SUMOylation and phosphorylation of PKCδ facilitates oxidative stress‐induced apoptosis

Although the increase in number of identified posttranslational modifications (PTMs) has substantially improved our knowledge about substrate site specificity single PTMs, fact that different types PTMs can crosstalk and act concert to exert important regulatory mechanisms for protein function not gained much attention. Here, we show kinase Cδ (PKCδ) is SUMOylated at lysine 473 its C-terminal catalytic domain, SUMOylation increases PKCδ stability by repressing ubiquitination. In addition, uncover a functional interplay between phosphorylation PKCδ, which strengthen each other through recruiting SUMO E2/E3 ligases kinase, respectively, complexes. We PIAS2β as E3 ligase PKCδ. More importantly, enhancing an interdependent promotes apoptotic cell death induced H2O2. conclude represents mechanism kinase's oxidative damage.