Cysteine availability tunes ubiquitin signaling via inverse stability of LRRC58 E3 ligase and its substrate CDO1
Gisele 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, , Brenda Arlene Schulman
The paper identifies LRRC58 as a cysteine-responsive E3 ligase that regulates CDO1 stability via ubiquitylation, revealing a mechanism linking cysteine availability to proteasomal turnover.
Nature Communications · May 7, 2026Peer-reviewedBiochemistry