Author
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.; Tonks, Nicholas K.; Linhardt, Robert J.; Boivin, Benoit
Other Contributors
Date Issued
2020-02-01
Subject
Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
Degree
Terms of Use
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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.
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.
Department
The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
Publisher
Nature
Relationships
The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Nature Chemical Biology; https://harc.rpi.edu/;
Access
A full text version is available in DSpace@RPI;
