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Updated: Aug 14, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
Published on: May 14, 2021
Cdc48p is UBX-linked to ER ubiquitin ligases
1University of Cambridge, Cambridge Institute for Medical Research and Department of Clinical Biochemistry, Hills Road, Cambridge CB2 2XY, UK. kbr20@cam.ac.uk
Abstract:
Proteasome-mediated turnover of misfolded secretory and transmembrane proteins at the cytoplasmic face of the endoplasmic reticulum (ER) membrane is dependent on a AAA-ATPase complex formed by the ubiquitin-selective chaperone Cdc48p in Saccharomyces cerevisiae and mammals by the Cdc48p homologue p97. Two new papers reveal that the Ubx2 protein physically links ER-membrane-integrated ubiquitin ligases to Cdc48p, and that it is essential for degradation of substrates that are ubiquitylated at the cytoplasmic face of the ER.
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