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 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.
Römisch
Karin
K
University of Cambridge, Cambridge Institute for Medical Research and Department of Clinical Biochemistry, Hills Road, Cambridge CB2 2XY, UK. kbr20@cam.ac.uk
D000251:Adenosine Triphosphatases; D018797:Cell Cycle Proteins / Q000378:metabolism*; D003593:Cytoplasm / Q000201:enzymology; D004721:Endoplasmic Reticulum / Q000201:enzymology*; D007700:Kinetics; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D029701:Saccharomyces cerevisiae Proteins; D013379:Substrate Specificity; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism*; D000074405:Valosin Containing Protein
D018797:Cell Cycle Proteins; D029701:Saccharomyces cerevisiae Proteins; D044767:Ubiquitin-Protein Ligases; D000251:Adenosine Triphosphatases; C000614177:CDC48 protein, S cerevisiae; D000074405:Valosin Containing Protein