| Literature DB >> 31873221 |
Avinash D Londhe1, Alexandre Bergeron2,3, Stephanie M Curley1, Fuming Zhang4, Keith D Rivera5, Akaash Kannan1, Gérald Coulis1,3, Syed H M Rizvi1, Seung Jun Kim6, Darryl J Pappin5, Nicholas K Tonks5, Robert J Linhardt4, Benoit Boivin7,8,9,10.
Abstract
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.Entities:
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Year: 2019 PMID： 31873221 PMCID： PMC6982540 DOI： 10.1038/s41589-019-0433-0
Source DB: PubMed Journal: Nat Chem Biol ISSN： 1552-4450 Impact factor: 15.040