Evidence map›Paper›PMID 39504958›Full record

ArticleCell2024

Recognition of BACH1 quaternary structure degrons by two F-box proteins under oxidative stress.

Shiyun Cao, Sheena Faye Garcia, Huigang Shi, Ellie I James, Yuki Kito, Hui Shi, Haibin Mao, Sharon Kaisari, Gergely Rona, Sophia Deng and 7 more

Abstract read
In one paragraph

Article in Cell, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

28 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Localized heme sensing through a ternary molecular glue.bioRxiv : the preprint server for biology · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Dissecting the Interplay Between NRF2 and BACH1 at CsMBEs.Antioxidants (Basel, Switzerland) · 2025
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

17 authors.

Shiyun CaoDepartment of Pharmacology, University of Washington, Box 357280, Seattle, WA 98195, USA; Howard Hughes Medical Institute, University of Washington, Seattle, WA 98195, USA.
Sheena Faye GarciaDepartment of Biochemistry and Molecular Pharmacology, New York University Grossman School of Medicine, New York, NY, 10016, USA; Laura and Isaac Perlmutter Cancer Center, New York University Grossman School of Medicine, New York, NY 10016, USA.
Huigang ShiDepartment of Pharmacology, University of Washington, Box 357280, Seattle, WA 98195, USA; Howard Hughes Medical Institute, University of Washington, Seattle, WA 98195, USA.
Ellie I JamesDepartment of Medicinal Chemistry, University of Washington, Seattle, WA 98195, USA; Molecular Engineering & Science Institute, University of Washington, Seattle, WA 98195, USA.
Yuki KitoDepartment of Biochemistry and Molecular Pharmacology, New York University Grossman School of Medicine, New York, NY, 10016, USA; Laura and Isaac Perlmutter Cancer Center, New York University Grossman School of Medicine, New York, NY 10016, USA.
Hui ShiDepartment of Pharmacology, University of Washington, Box 357280, Seattle, WA 98195, USA; Howard Hughes Medical Institute, University of Washington, Seattle, WA 98195, USA.
Haibin MaoDepartment of Pharmacology, University of Washington, Box 357280, Seattle, WA 98195, USA; Howard Hughes Medical Institute, University of Washington, Seattle, WA 98195, USA.
Sharon KaisariDepartment of Biochemistry and Molecular Pharmacology, New York University Grossman School of Medicine, New York, NY, 10016, USA; Laura and Isaac Perlmutter Cancer Center, New York University Grossman School of Medicine, New York, NY 10016, USA.
Gergely RonaDepartment of Biochemistry and Molecular Pharmacology, New York University Grossman School of Medicine, New York, NY, 10016, USA; Laura and Isaac Perlmutter Cancer Center, New York University Grossman School of Medicine, New York, NY 10016, USA; Howard Hughes Medical Institute, New York University Grossman School of Medicine, New York, NY 10016, USA; Institute of Molecular Life Sciences, HUN-REN Research Centre for Natural Sciences, Budapest, Hungary.
Sophia DengDepartment of Biochemistry and Molecular Pharmacology, New York University Grossman School of Medicine, New York, NY, 10016, USA; Laura and Isaac Perlmutter Cancer Center, New York University Grossman School of Medicine, New York, NY 10016, USA.
Hailey V GoldbergDepartment of Biochemistry and Molecular Pharmacology, New York University Grossman School of Medicine, New York, NY, 10016, USA; Laura and Isaac Perlmutter Cancer Center, New York University Grossman School of Medicine, New York, NY 10016, USA.
Jackeline PonceDepartment of Biochemistry and Molecular Pharmacology, New York University Grossman School of Medicine, New York, NY, 10016, USA; Laura and Isaac Perlmutter Cancer Center, New York University Grossman School of Medicine, New York, NY 10016, USA; Proteomics Laboratory, Division of Advanced Research Technologies, New York University Grossman School of Medicine, New York, NY 10016, USA.
Beatrix UeberheideDepartment of Biochemistry and Molecular Pharmacology, New York University Grossman School of Medicine, New York, NY, 10016, USA; Laura and Isaac Perlmutter Cancer Center, New York University Grossman School of Medicine, New York, NY 10016, USA; Proteomics Laboratory, Division of Advanced Research Technologies, New York University Grossman School of Medicine, New York, NY 10016, USA.
Luca LignittoDepartment of Biochemistry and Molecular Pharmacology, New York University Grossman School of Medicine, New York, NY, 10016, USA; Laura and Isaac Perlmutter Cancer Center, New York University Grossman School of Medicine, New York, NY 10016, USA; Cancer Research Center of Marseille (CRCM), CNRS, Aix Marseille University, INSERM, Institut Paoli-Calmettes, Marseille, France.
Miklos GuttmanDepartment of Medicinal Chemistry, University of Washington, Seattle, WA 98195, USA; Molecular Engineering & Science Institute, University of Washington, Seattle, WA 98195, USA.
Michele PaganoDepartment of Biochemistry and Molecular Pharmacology, New York University Grossman School of Medicine, New York, NY, 10016, USA; Laura and Isaac Perlmutter Cancer Center, New York University Grossman School of Medicine, New York, NY 10016, USA; Howard Hughes Medical Institute, New York University Grossman School of Medicine, New York, NY 10016, USA. Electronic address: michele.pagano@nyumc.org.
Ning ZhengDepartment of Pharmacology, University of Washington, Box 357280, Seattle, WA 98195, USA; Howard Hughes Medical Institute, University of Washington, Seattle, WA 98195, USA. Electronic address: nzheng@uw.edu.

Funding

Vaccine FacilityP30CA016087 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI ANIRBAN MAITRA · 1985 to 2026
$83.1M
Regulation of the cell proliferation by CRL ubiquitin ligases-diversity supplementR35GM136250 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI MICHELE PAGANO · 2020 to 2026
$2.7M
ThermoFisher Scientific Orbitrap Eclipse with ETD and UVPDS10OD030237 · OD · UNIVERSITY OF WASHINGTON · PI GUTTMAN, MIKLOS · 2022 to 2022
$1.2M
Acquisition of an Orbitrap Elite Mass Spectrometer with ETDS10OD010582 · OD · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI UEBERHEIDE, BEATRIX MAGDALENA · 2013 to 2013
$600k
NCI NIH HHS P30 CA016087NIGMS NIH HHS R35 GM136250NIH HHS S10 OD010582NIH HHS S10 OD030237
6 · The paper itself

Abstract

Ubiquitin-dependent proteolysis regulates diverse cellular functions with high substrate specificity, which hinges on the ability of ubiquitin E3 ligases to decode the targets' degradation signals, i.e., degrons. Here, we show that BACH1, a transcription repressor of antioxidant response genes, features two distinct unconventional degrons encrypted in the quaternary structure of its homodimeric BTB domain. These two degrons are both functionalized by oxidative stress and are deciphered by two complementary E3s. FBXO22 recognizes a degron constructed by the BACH1 BTB domain dimer interface, which is unmasked from transcriptional co-repressors after oxidative stress releases BACH1 from chromatin. When this degron is impaired by oxidation, a second BACH1 degron manifested by its destabilized BTB dimer is probed by a pair of FBXL17 proteins that remodels the substrate into E3-bound monomers for ubiquitination. Our findings highlight the multidimensionality of protein degradation signals and the functional complementarity of different ubiquitin ligases targeting the same substrate.

Indexed as

Basic-Leucine Zipper Transcription FactorsF-Box ProteinsOxidative StressAnimalsDegronsHEK293 CellsHumansMiceModels, MolecularProtein Structure, QuaternaryProteolysisUbiquitinationUbiquitin-Protein LigasesBACH1 protein, humanBasic-Leucine Zipper Transcription FactorsF-Box ProteinsUbiquitin-Protein LigasesBACH1BTBcullin-RING ligasesdegrondimerFBXL17FBXO22hemenitric oxideoxidative stressprotein degradationquaternary structureSCFtranscription factorubiquitin ligase

Identifiers

PMID39504958
PMCPMC11682927

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.