Background: Soluble epoxide hydrolase (sEH) is a cytosolic enzyme whose pharmacological inhibition or targeted deletion in mice has beneficial effects, including improved insulin signaling in liver and adipose tissue. Results: sEH inhibition or deficiency attenuates high fat diet-and chemical-induced endoplasmic reticulum (ER) stress in mice and cells, respectively. Conclusion: sEH modulates ER stress in a cell-autonomous manner. Significance: sEH may be a therapeutic target for mitigating complications associated with the metabolic syndrome.

Background: Tyrosine phosphorylation of PKM2 inhibits its activity; however, the phosphatase(s) that regulates PKM2 phosphorylation remains unidentified. Results: PKM2 is a novel PTP1B substrate and PKM2 Tyr-105 and Tyr-148 are key sites that mediate the interaction. Conclusion: PTP1B regulates PKM2 tyrosine phosphorylation and activity in adipocytes. Significance: These findings provide new insights into the regulation of adipose PKM2 activity.