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TitleDET1 dynamics underlie cooperative ubiquitination by CRL4 complexes.
Journal, issue, pagesSci Adv, Vol. 11, Issue 9, Page eadq4187, Year 2025
Publish dateFeb 28, 2025
AuthorsAbigail E Burgess / Tarren A Loughran / Liam S Turk / Hunter G Nyvall / Jessica L Dunlop / Sam A Jamieson / Jack R Curry / John E Burke / Pavel Filipcik / Simon H J Brown / Peter D Mace /
PubMed AbstractTranscription factor ubiquitination is a decisive regulator of growth and development. The DET1-DDB1-DDA1 (DDD) complex associates with the Cullin-4 ubiquitin ligase (CRL4) and a second ubiquitin ...Transcription factor ubiquitination is a decisive regulator of growth and development. The DET1-DDB1-DDA1 (DDD) complex associates with the Cullin-4 ubiquitin ligase (CRL4) and a second ubiquitin ligase, COP1, to control ubiquitination of transcription factors involved in neurological, metabolic, and immune cell development. Here, we report the structure of the human DDD complex, revealing a specific segment of DET1 that can recruit ubiquitin-conjugating (E2) enzymes. Structural variability analysis, mass spectrometry, and mutagenesis based on AlphaFold predictions suggest that dynamic closure of DET1, stabilized by DDA1, underlies coordinated recruitment of E2 enzymes and COP1. Biochemical assays suggest that the E2 acts as a recruitment factor to bring COP1 to DET1 for more effective substrate ubiquitination, which parallels a catalytically inactive E2 enzyme (COP10) in plant DDD complexes. This work provides a clear architecture for regulation and cooperative CRL4 complex assembly, which can affect degradation of diverse targets by COP1 complexes.
External linksSci Adv / PubMed:40009677 / PubMed Central
MethodsEM (single particle)
Resolution2.83 Å
Structure data

44638

9bjz

EMDB-44638, PDB-9bjz:
Structure of the human DDD-Ube2e2 complex
Method: EM (single particle) / Resolution: 2.83 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN BINDING / DDB1 / DDA1 / DET1 / DCAF / ubiquitin conjugating enzyme

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