| First Author | Minami R | Year | 2010 |
| Journal | J Cell Biol | Volume | 190 |
| Issue | 4 | Pages | 637-50 |
| PubMed ID | 20713601 | Mgi Jnum | J:168161 |
| Mgi Id | MGI:4887294 | Doi | 10.1083/jcb.200908092 |
| Citation | Minami R, et al. (2010) BAG-6 is essential for selective elimination of defective proteasomal substrates. J Cell Biol 190(4):637-50 |
| abstractText | BAG-6/Scythe/BAT3 is a ubiquitin-like protein that was originally reported to be the product of a novel gene located within the human major histocompatibility complex, although the mechanisms of its function remain largely obscure. Here, we demonstrate the involvement of BAG-6 in the degradation of a CL1 model defective protein substrate in mammalian cells. We show that BAG-6 is essential for not only model substrate degradation but also the ubiquitin-mediated metabolism of newly synthesized defective polypeptides. Furthermore, our in vivo and in vitro analysis shows that BAG-6 interacts physically with puromycin-labeled nascent chain polypeptides and regulates their proteasome-mediated degradation. Finally, we show that knockdown of BAG-6 results in the suppressed presentation of MHC class I on the cell surface, a procedure known to be affected by the efficiency of metabolism of defective ribosomal products. Therefore, we propose that BAG-6 is necessary for ubiquitin-mediated degradation of newly synthesized defective polypeptides. |
