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SUMOylation modulates the stability and function of PI3K-p110β.

Ahmed El Motiam1, Carlos F de la Cruz-Herrera2, Santiago Vidal1

  • 1Centro de Investigación en Medicina Molecular (CIMUS), CIMUS, P2L7, Universidade de Santiago de Compostela and Instituto de Investigaciones Sanitarias (IDIS), Avda Barcelona, 15706, Santiago de Compostela, Spain.

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SUMOylation of the p110β subunit stabilizes it, enhancing PI3K pathway activation and promoting cancer growth. The p85β regulatory subunit counteracts this SUMOylation process.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Research

Background:

  • Class I PI3K, crucial for cellular functions, comprises p85 regulatory and p110 catalytic subunits.
  • The p110β catalytic subunit is increasingly recognized for its significant role in tumorigenesis.

Purpose of the Study:

  • To investigate the potential regulation of the p110β subunit by SUMOylation.
  • To understand the impact of SUMOylation on p110β activity and its role in cancer.

Main Methods:

  • In vitro and in vivo experiments including transfected cells and endogenous conditions.
  • Identification of the specific lysine residue responsible for SUMOylation.
  • Assessment of protein stability and AKT activation.
  • Evaluation of the interaction with the p85β regulatory subunit.

Main Results:

  • p110β undergoes SUMOylation by SUMO1 and SUMO2, confirmed in vitro, in transfected cells, and endogenously.
  • Lysine residue 952 in the p110β activation loop is essential for SUMOylation.
  • SUMOylation stabilizes p110β, enhances AKT activation, and promotes cell growth and oncogenic transformation.
  • The p85β regulatory subunit inhibits p110β SUMOylation.

Conclusions:

  • SUMOylation is a novel regulatory mechanism for p110β.
  • SUMOylation positively impacts PI3K pathway activation, contributing to p110β-driven cancers.
  • The p85β subunit acts as a negative regulator of p110β SUMOylation.