Journal
NATURE CHEMICAL BIOLOGY
Volume 16, Issue 2, Pages 122-+Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41589-019-0433-0
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Funding
- National Institutes of Health [GM55989, HL138605]
- American Heart Association [17GRNT33700265]
- Heart and Stroke Foundation of Canada
- SUNY Research Foundation
- FRQS
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A transient interaction between 14-3-3 zeta and a loop of PTP1B is detected following PTP1B inactivation by reversible oxidation. We have identified a molecular interaction between the reversibly oxidized form of protein tyrosine phosphatase 1B (PTP1B) and 14-3-3 zeta that regulates PTP1B activity. Destabilizing the transient interaction between 14-3-3 zeta and PTP1B prevented PTP1B inactivation by reactive oxygen species and decreased epidermal growth factor receptor phosphorylation. Our data suggest that destabilizing the interaction between 14-3-3 zeta and the reversibly oxidized and inactive form of PTP1B may establish a path to PTP1B activation in cells.
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