Regulation of PTP1B activation through disruption of redox-complex formation
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Authors
Londhe, Avinash D.
Bergeron, Alexandre
Curley, Stephanie M.
Zhang, Fuming
Rivera, Keith D.
Kannan, Akaash
Coulis, Gérald
Rizvi, Syed H.M.
Kim, Seung Jun
Pappin, Darryl J.
Issue Date
2020-02-01
Type
Article
Language
ENG
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Alternative Title
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.
Description
Nature Chemical Biology, 16, 122-125
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Full Citation
Regulation of PTP1B activation through disruption of redox-complex formation, A. D. Londhe, A. Bergeron, S. M. Curley, F. Zhang, K. D. Rivera, A. Kannan, G. Coulis, S. H. M. Rizvi, S. J. Kim, D. J. Pappin, N. K. Tonks, R. J. Linhardt, B. Boivin, Nature Chemical Biology, 16, 122-125, 2020.
Publisher
Nature
Terms of Use
Journal
Volume
Issue
PubMed ID
DOI
ISSN
15524469
15524450
15524450