A new study from the Perissi lab has revealed an unexpected layer of regulation in the insulin signaling cascade based on the opposing actions of the ubiquitin conjugating enzyme Ubc13 and its inhibitor GPS2. The work, recently published in Molecular Metabolism, shows that Ubc13-mediated ubiquitination of the AKT/PKB kinase is required for its phosphorylation and activation in the insulin signaling cascade. Conversely, loss of GPS2-mediated inhibition of Ubc13 activity promotes sustained insulin signaling both in vitro, in 3T3-L1 adipocytes, and in vivo in the adipose tissue of GPS2-AKO mice. Dr. Valentina Perissi and Carly Cederquist, the graduate student who led the project, discuss their finding in the 60 Second Metabolist video (below)