Cdc48p is UBX-linked to ER ubiquitin ligases
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 p9...
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| Veröffentlicht in: | Trends in biochemical sciences (Amsterdam. Regular ed.) 2006, Vol.31 (1), p.24-25 |
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| container_title | Trends in biochemical sciences (Amsterdam. Regular ed.) |
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| creator | Römisch, Karin |
| description | 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. |
| doi_str_mv | 10.1016/j.tibs.2005.11.004 |
| format | Article |
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| fulltext | fulltext |
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| ispartof | Trends in biochemical sciences (Amsterdam. Regular ed.), 2006, Vol.31 (1), p.24-25 |
| issn | 0968-0004 1362-4326 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_70728704 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Adenosine Triphosphatases Cell Cycle Proteins - metabolism Cytoplasm - enzymology Endoplasmic Reticulum - enzymology Kinetics Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae Proteins Substrate Specificity Ubiquitin-Protein Ligases - metabolism Valosin Containing Protein |
| title | Cdc48p is UBX-linked to ER ubiquitin ligases |
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