Cuadrado and colleagues first showed that GSK-3 inhibits NRF2 activity, but the identification of sites in NRF2 that are phosphorylated by GSK-3 was achieved several years later using two-dimensional electrophoresis and mass spectrometry: GSK-3 phosphorylates a group of Ser residues at the level of DSGIS motif in the Neh6 domain of NRF2, and this event represents the signal for the recognition by the adapter protein -TrCP, that targets NRF2 for ubiquitination and proteasomal degradation in a KEAP1-independent manner [150, 151]
doi: 10.3389/fphar.2024.1437939 Received 24 May 2024 Accepted 03 July 2024 Published 25 July 2024 Volume 15 - 2024 Edited by Marcos Roberto De Oliveira, Federal University of Rio Grande do Sul, Brazil Reviewed by Rosella Abeti, University College London, United Kingdom Andreia Neves Carvalho, University of Lisbon, Portugal Updates Copyright 2024 Mayer, Riera-Ponsati, Kauppinen, Klitgaard, Erler and Hansen
Mortensen KN, Sanggaard S, Mestre H, Lee H, Kostrikov S, Xavier ALR, et al
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