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TitleDual BACH1 regulation by complementary SCF-type E3 ligases.
Journal, issue, pagesCell, Vol. 187, Issue 26, Page 7585-7602.e25, Year 2024
Publish dateDec 26, 2024
AuthorsBenedikt Goretzki / Maryam Khoshouei / Martin Schröder / Patrick Penner / Luca Egger / Christine Stephan / Dayana Argoti / Nele Dierlamm / Jimena Maria Rada / Sandra Kapps / Catrin Swantje Müller / Zacharias Thiel / Merve Mutlu / Claude Tschopp / David Furkert / Felix Freuler / Simon Haenni / Laurent Tenaillon / Britta Knapp / Alexandra Hinniger / Philipp Hoppe / Enrico Schmidt / Sascha Gutmann / Mario Iurlaro / Grigory Ryzhakov / César Fernández /
PubMed AbstractBroad-complex, tramtrack, and bric-à-brac domain (BTB) and CNC homolog 1 (BACH1) is a key regulator of the cellular oxidative stress response and an oncogene that undergoes tight post-translational ...Broad-complex, tramtrack, and bric-à-brac domain (BTB) and CNC homolog 1 (BACH1) is a key regulator of the cellular oxidative stress response and an oncogene that undergoes tight post-translational control by two distinct F-box ubiquitin ligases, SCF and SCF. However, how both ligases recognize BACH1 under oxidative stress is unclear. In our study, we elucidate the mechanism by which FBXO22 recognizes a quaternary degron in a domain-swapped β-sheet of the BACH1 BTB dimer. Cancer-associated mutations and cysteine modifications destabilize the degron and impair FBXO22 binding but simultaneously expose an otherwise shielded degron in the dimer interface, allowing FBXL17 to recognize BACH1 as a monomer. These findings shed light on a ligase switch mechanism that enables post-translational regulation of BACH1 by complementary ligases depending on the stability of its BTB domain. Our results provide mechanistic insights into the oxidative stress response and may spur therapeutic approaches for targeting oxidative stress-related disorders and cancer.
External linksCell / PubMed:39657677
MethodsEM (single particle) / X-ray diffraction
Resolution1.47 - 3.4 Å
Structure data

19766

8s7d

EMDB-19766, PDB-8s7d:
Cryo-EM structure of SKP1-FBXO22 in complex with a BACH1 BTB dimer at 3.2A resolution
Method: EM (single particle) / Resolution: 3.2 Å

19768

8s7e

EMDB-19768, PDB-8s7e:
Cryo-EM structure of SKP1-FBXO22
Method: EM (single particle) / Resolution: 3.4 Å

PDB-9gp5:
Homodimer of BACH1 F9A mutant BTB domain
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-9gr9:
Homodimer of BACH1 BTB domain
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

PDB-9gra:
Homodimer of BACH1 BTB domain in complex with 2-Methyl-2,4-pentanediol
Method: X-RAY DIFFRACTION / Resolution: 1.47 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-MRD:
(4R)-2-METHYLPENTANE-2,4-DIOL / precipitant*YM

Source
  • homo sapiens (human)
KeywordsLIGASE / SKP1-FBXO22 E3 ligase SCF F-box protein BACH1 BTB / SKP1-FBXO22 E3 ligase SCF F-box protein / DNA BINDING PROTEIN / BACH1 / back-to-back domain / BTB domain

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