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Dual BACH1 regulation by complementary SCF-type E3 ligases.

Benedikt Goretzki1, Maryam Khoshouei1, Martin Schröder1

  • 1Discovery Sciences, Novartis Biomedical Research, Basel, Switzerland.

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|December 10, 2024
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Summary
This summary is machine-generated.

This study reveals how the BACH1 protein, a regulator of oxidative stress and oncogene, is controlled by two ubiquitin ligases. A switch mechanism allows FBXO22 or FBXL17 to bind BACH1 depending on its structural state, impacting cancer and oxidative stress disorders.

Keywords:
BACH1Cullin-RING ligasesF-boxFBXL17FBXO22S-nitrosylation hemecysteine modificationligase switchoxidative stress

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • Broad-complex, tramtrack, and bric-à-brac domain (BTB) and CNC homolog 1 (BACH1) is a key regulator of cellular oxidative stress and an oncogene.
  • BACH1 is post-translationally regulated by SCFFBXO22 and SCFFBXL17 ubiquitin ligases, but the recognition mechanism under oxidative stress is unknown.

Purpose of the Study:

  • To elucidate the mechanism by which FBXO22 and FBXL17 recognize BACH1 under oxidative stress conditions.
  • To understand the ligase switch mechanism controlling BACH1's post-translational regulation.

Main Methods:

  • Structural analysis of the BACH1 BTB dimer and its interaction with FBXO22.
  • Investigating the impact of cancer-associated mutations and cysteine modifications on BACH1 stability and ligase binding.
  • Characterizing BACH1 recognition by FBXL17 as a monomer.

Main Results:

  • FBXO22 recognizes a quaternary degron within a domain-swapped β-sheet of the BACH1 BTB dimer.
  • Cancer mutations and cysteine modifications destabilize the FBXO22 degron, impairing binding.
  • These modifications expose a distinct degron at the dimer interface, enabling FBXL17 to bind monomeric BACH1.

Conclusions:

  • A ligase switch mechanism regulates BACH1 by FBXO22 and FBXL17 based on BTB domain stability.
  • These findings provide mechanistic insights into oxidative stress response.
  • The study may inform therapeutic strategies for oxidative stress-related disorders and cancer.