biostudies-literatureLondhe ADAmerican Heart AssociationNIDDK NIH HHSNHLBI NIH HHSU.S. Department of Health & Human Services | NIH | National Heart, Lung, and Blood InstituteNCI NIH HHSNIGMS NIH HHS122-125https://www.ebi.ac.uk/biostudies/studies/S-EPMC6982540biostudies-literatureUnknown16(2)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.Nature chemical biologyRegulation of PTP1B activation through disruption of redox-complex formation.PMC6982540P30 CA04550817GRNT33700265R15 HL138605R01 GM055989HL138605R01 DK124907Londhe ADZhang FKannan ALinhardt RJTonks NKBergeron ACurley SMRivera KDPappin DJCoulis GRizvi SHMKim SJBoivin BfalseRegulation of PTP1B activation through disruption of redox-complex formation.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.2020-01-01T00:00:00Z2020 Feb2026-04-14T21:15:39.956Z2020-06-26T07:04:57ZS-EPMC69825403187322110.1038/s41589-019-0433-0