Regulation of PTP1B activation through disruption of redox-complex formation
Cited 14 time in 
Metadata Downloads
- Title
- Regulation of PTP1B activation through disruption of redox-complex formation
- Author(s)
- A D Londhe; A Bergeron; S M Curley; F Zhang; K D Rivera; A Kannan; G Coulis; S H M Rizvi; Seung Jun Kim; D J Pappin; N K Tonks; R J Linhardt; B Boivin
- Bibliographic Citation
- Nature Chemical Biology, vol. 16, pp. 122-125
- Publication Year
- 2020
- 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.
- ISSN
- 1552-4450
- Publisher
- Springer-Nature Pub Group
- Type
- Article
- Appears in Collections:
- Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
- Files in This Item:
There are no files associated with this item.
Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.