SUMOylation modulates the stability and function of PI3K-p110β

Class I PI3K are heterodimers composed of a p85 regulatory subunit and p110 catalytic involved in multiple cellular functions. Recently, the p110β has emerged as class isoform playing major role tumorigenesis. Understanding its regulation is crucial for control pathway p110β-driven cancers. Here we sought to evaluate putative by SUMO. Our data show that can be modified SUMO1 SUMO2 vitro, transfected cells under completely endogenous conditions, supporting physiological relevance SUMOylation. We identify lysine residue 952, located at activation loop p110β, essential SUMOylation stabilizes protein increasing AKT which promotes cell growth oncogenic transformation. Finally, p85β counteracts conjugation SUMO p110β. In summary, our reveal novel interacting partner with positive effect on pathway.