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
1. Verfasser:	Römisch, Karin
Format:	Artikel
Sprache:	eng
Schlagworte:	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
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Beschreibung
Zusammenfassung:	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.
ISSN:	0968-0004 1362-4326
DOI:	10.1016/j.tibs.2005.11.004