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TitleCysteine availability tunes ubiquitin signaling via inverse stability of LRRC58 E3 ligase and its substrate CDO1.
Journal, issue, pagesNat Commun, Vol. 17, Issue 1, Year 2026
Publish dateMay 7, 2026
AuthorsGisele A Andree / Luca J Stier / Kerstin Schmiederer / Alina S Thielen / Luis Schmid / Samuel A Maiwald / Karthik V Gottemukkala / Jiale Du / Susanne von Gronau / Claudia Strasser / Judith Müller / Lukas T Henneberg / Camille Guyot / Gary Kleiger / Matthias Mann / Peter J Murray / Brenda A Schulman /
PubMed AbstractCellular responses to amino acid fluctuations often hinge on ubiquitin-mediated control of metabolic enzymes, yet the underlying E3 ligase pathways remain poorly defined. Using quantitative ...Cellular responses to amino acid fluctuations often hinge on ubiquitin-mediated control of metabolic enzymes, yet the underlying E3 ligase pathways remain poorly defined. Using quantitative proteomics and active cullin-RING ligase (CRL) profiling, we identify LRRC58 as a cysteine-responsive substrate receptor whose stability increases sharply under cysteine starvation. Proteomics reveals an inverse relationship between LRRC58 and the metabolic enzyme cysteine dioxygenase 1 (CDO1), suggesting a cysteine-linked regulatory axis. Biochemical reconstitution and cryo-EM structures show that LRRC58 forms an active CUL2- or CUL5-based CRL that selectively positions CDO1 for ubiquitylation at Lys8. Disease mutant versions of CDO1 mapping to the LRRC58 interface and impaired for the endogenous ubiquitylation pathway were degraded through orthogonal targeting by a VHL-based degrader. Together, our proteomics-guided discovery pipeline, cellular stability studies, and structural analyses uncover a metabolically-tuned LRRC58-CDO1 pathway that links cysteine availability to selective proteasomal turnover, reveals principles of metabolite-regulated CRL activity, and showcases mechanisms distinguishing endogenous and targeted protein degradation.
External linksNat Commun / PubMed:42098103 / PubMed Central
MethodsEM (single particle)
Resolution2.91 - 3.7 Å
Structure data

EMDB-55652: Composite map of LRRC58- EloB/C-CDO1 in complex with neddylated CUL2-RBX1-ARIH1-Ub
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-55653: Consensus map of LRRC58- EloB/C-CDO1 in complex with neddylated CUL2-RBX1-ARIH1-Ub
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-55654: Focused map of LRRC58-CDO1 region from LRRC58- EloB/C-CDO1 in complex with neddylated CUL2-RBX1-ARIH1-Ub
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-55655: Focused map of CUL2-LRRC58-EloC interface region from LRRC58- EloB/C-CDO1 in complex with neddylated CUL2-RBX1-ARIH1-Ub
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-55656: Focused map of ARIH1-Ub region from LRRC58- EloB/C-CDO1 in complex with neddylated CUL2-RBX1-ARIH1-Ub
Method: EM (single particle) / Resolution: 3.6 Å

55658

9t7v

EMDB-55658, PDB-9t7v:
Structure of LRRC58-EloB/C-CDO1 in complex with NEDD8-CUL5-RBX2-ARIH2-Ub
Method: EM (single particle) / Resolution: 2.95 Å

EMDB-55659: Consensus Map of LRRC58-ELOB/C-CDO1 in complex with NEDD8-CUL5-RBX2-ARIH2-Ub
Method: EM (single particle) / Resolution: 2.91 Å

EMDB-55660: Focused map of LRRC58-CDO1 region from LRRC58-ELOB/C-CDO1-CUL5-RBX2-NEDD8-ARIH2-UB
Method: EM (single particle) / Resolution: 3.05 Å

Chemicals

ChemComp-FE:
Unknown entry

ChemComp-SY8:
5-azanylpentan-2-one

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsLIGASE / Cullin / E3 ligase / Ubiquitin

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