Regulation of PTP1B activation through disruption of redox-complex formation

We have identified a molecular interaction between the reversibly oxidized form of PTP1B and 14-3-3ζ that regulates PTP1B activity. Destabilizing the transient interaction between 14-3-3ζ and PTP1B, prevented PTP1B inactivation by ROS and decreased EGFR phosphorylation. Our data suggest that destabi...

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Detalles Bibliográficos
Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2019
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6982540/
https://www.ncbi.nlm.nih.gov/pubmed/31873221
http://dx.doi.org/10.1038/s41589-019-0433-0
Descripción
Sumario:We have identified a molecular interaction between the reversibly oxidized form of PTP1B and 14-3-3ζ that regulates PTP1B activity. Destabilizing the transient interaction between 14-3-3ζ and PTP1B, prevented PTP1B inactivation by ROS and decreased EGFR 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.

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