Regulation of PTP1B activation through disruption of redox-complex formation.

Avinash D LondheAlexandre BergeronStephanie M CurleyFuming ZhangKeith D RiveraAkaash KannanGérald CoulisSyed H M RizviSeung Jun KimDarryl J PappinNicholas K TonksRobert J LinhardtBenoit Boivin

Published in: Nature chemical biology (2019)

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.

Keyphrases

epidermal growth factor receptor
reactive oxygen species
tyrosine kinase
induced apoptosis
advanced non small cell lung cancer
protein kinase
cell death
signaling pathway
deep learning
low density lipoprotein
endoplasmic reticulum stress
blood brain barrier