Cysteine availability tunes ubiquitin signaling via inverse stability of LRRC58 E3 ligase and its substrate CDO1.
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| Title: | Cysteine availability tunes ubiquitin signaling via inverse stability of LRRC58 E3 ligase and its substrate CDO1. |
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| Authors: | Andree GA; Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany., Stier LJ; Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany.; Department of Chemistry, School of Natural Sciences, Technical University of Munich, Garching, Germany., Schmiederer K; Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany.; Department of Chemistry, School of Natural Sciences, Technical University of Munich, Garching, Germany., Thielen AS; Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany.; Department of Chemistry, School of Natural Sciences, Technical University of Munich, Garching, Germany., Schmid L; Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany., Maiwald SA; Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany.; Department of Chemistry, School of Natural Sciences, Technical University of Munich, Garching, Germany., Gottemukkala KV; Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany.; Department of Chemistry, School of Natural Sciences, Technical University of Munich, Garching, Germany., Du J; Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany., von Gronau S; Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany., Strasser C; Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany., Müller J; Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany., Henneberg LT; Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany.; Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany., Guyot C; Research Group of Immunoregulation, Max Planck Institute of Biochemistry, Martinsried, Germany., Kleiger G; Department of Chemistry and Biochemistry, University of Nevada, Las Vegas, Las Vegas, NV, USA., Mann M; Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany., Murray PJ; Research Group of Immunoregulation, Max Planck Institute of Biochemistry, Martinsried, Germany., Schulman BA; Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany. schulman@biochem.mpg.de.; Department of Chemistry, School of Natural Sciences, Technical University of Munich, Garching, Germany. schulman@biochem.mpg.de. |
| Source: | Nature communications [Nat Commun] 2026 May 07; Vol. 17 (1). Date of Electronic Publication: 2026 May 07. |
| Publication Type: | Journal Article |
| Journal Info: | Publisher: Nature Pub. Group Country of Publication: England NLM ID: 101528555 Publication Model: Electronic Cited Medium: Internet ISSN: 2041-1723 (Electronic) Linking ISSN: 20411723 NLM ISO Abbreviation: Nat Commun Subsets: MEDLINE |
| Database: | MEDLINE Ultimate |
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