Background: NFE2L3 is involved in carcinogenesis, stress response, differentiation, and inflammatory processes. Results: NFE2L3 is polyubiquitinated via the E3 ubiquitin ligase FBW7, which regulates its turnover. This process requires prior phosphorylation by GSK3. Conclusion: NFE2L3 is tightly regulated by FBW7 and GSK3 through polyubiquitination. Significance: Our data highlight the regulation of NFE2L3 by FBW7 and GSK3 and its potential role in cellular stress response.
CITATION STYLE
Kannan, M. B., Dodard-Friedman, I., & Blank, V. (2015). Stringent control of NFE2L3 (Nuclear Factor, Erythroid 2-Like 3; NRF3) protein degradation by FBW7 (F-box/WD Repeatcontaining Protein 7) and glycogen synthase kinase 3 (GSK3). Journal of Biological Chemistry, 290(43), 26292–26302. https://doi.org/10.1074/jbc.M115.666446
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