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Updated: Jan 7, 2026

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale
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NFE2L1/Nrf1 forms a coactivator complex post-peptide:N-glycanase-mediated sequence editing and mitigates proteasome

Yukiko Yoshida1, Meari Okada1, Naoko Arai1

  • 1Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Tokyo 156-8506, Japan.

Proceedings of the National Academy of Sciences of the United States of America
|December 30, 2025
PubMed
Summary

Nuclear factor erythroid 2-like 1 (Nrf1) is activated by sequence editing, a unique process for transcription factors. This editing is crucial for proteasome gene expression and cell survival, but its constitutive activation can be toxic.

Keywords:
HCFC1NFE2L1NGLY1Nrf1proteasome

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