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Romisch K (2006) Cdc48p is UBX-linked to ER ubiquitin ligases. Trends Biochem Sci 31(1):24-5
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.
| Status: Published | Type: Journal Article | PubMed ID: 16316751 |
Topics addressed in this paper
Number of different genes curated to this paper: 6
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