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Sel1p-Ubx2p participates in a distinct Cdc48p-dependent endoplasmic reticulum-associated degradation pathway-
Wilson JD, Liu Y, Bentivoglio CM, Barlowe C
Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA-
Abstract: The endoplasmic reticulum -ER- serves a critical role in the biogenesis of secretory proteins- Folding of nascent polypeptides occurs in the ER before anterograde transport through the secretory pathway, whereas terminally misfolded secretory proteins are recognized and eliminated by ER-associated degradation -ERAD-- Here, we investigated the role of the ubiquitin regulatory X -UBX- domain-containing protein Sel1p in ER quality control and transport- Mutant sel1Delta yeast displayed a constitutively active unfolded protein response and a mildly reduced rate of secretory protein transport from the ER- Immunoisolation of Sel1p from detergent-solubilized ER microsomes revealed a protein complex containing both Cdc48p and Npl4p and suggested a direct role for Sel1p in ERAD- In cells that lack Sel1p, we observed a reduction in the level of Cdc48p bound to ER membranes and a decrease in the turnover rate of two model ERAD substrates, carboxypeptidase Y* and Ste6*- In addition, we found that Sel1p and a second UBX domain-containing protein, Shp1p, associated with Cdc48p in a mutually exclusive manner- Interestingly, the association of Sel1p with Cdc48p was regulated by ATP, while the interaction of Shp1p with Cdc48p was not influenced by ATP- Based on these findings, we conclude that Sel1p operates in the ERAD pathway by coupling Cdc48p to ER membranes and that Shp1p acts in a distinct Cdc48p-dependent protein degradation pathway-
[PUBMED: 16919153]

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