For each citation that was shared on social media (LinkedIn,
Facebook, or Twitter) with the “@GenScript” tag, the author will be rewarded with a $10
Amazon gift card or 2,000 GS points.
Regulation of PTP1B activation through disruption of redox-complex formation
Nat Chem Biol.2020;
Londhe AD, Bergeron A, Curley SM, Zhang F, Rivera KD, Kannan A, Coulis G, Rizvi SHM, Kim SJ, Pappin DJ, Tonks NK, Linhardt RJ, Boivin B, , .
We have identified a molecular interaction between the reversibly oxidized form of protein tyrosine phosphatase 1B (PTP1B) and 14-3-3ζ that regulates PTP1B activity. Destabilizing the transient interaction between 14-3-3ζ and PTP1B prevented PTP1B inactivation by reactive oxygen species and decreased epidermal growth factor receptor phosphorylation. Our data suggest that destabilizing the interaction between 14-3-3ζ and the reversibly oxidized and inactive form of PTP1B may establish a path to PTP1B activation in cells.
We have identified a molecular interaction between the reversibly oxidized form of protein tyrosine phosphatase 1B (PTP1B) and 14-3-3ζ that regulates PTP1B activity. Destabilizing the transient interaction between 14-3-3ζ and PTP1B prevented PTP1B inactivation by reactive oxygen species and decreased epidermal growth factor receptor phosphorylation. Our data suggest that destabilizing the interaction between 14-3-3ζ and the reversibly oxidized and inactive form of PTP1B may establish a path to PTP1B activation in cells.