| First Author | Yoshida Y | Year | 2005 |
| Journal | EMBO Rep | Volume | 6 |
| Issue | 3 | Pages | 239-44 |
| PubMed ID | 15723043 | Mgi Jnum | J:96950 |
| Mgi Id | MGI:3573989 | Doi | 10.1038/sj.embor.7400351 |
| Citation | Yoshida Y, et al. (2005) Glycoprotein-specific ubiquitin ligases recognize N-glycans in unfolded substrates. EMBO Rep 6(3):239-44 |
| abstractText | Misfolded or unassembled polypeptides in the endoplasmic reticulum (ER) are retro-translocated into the cytosol and degraded by the ubiquitin-proteasome system. We reported previously that the SCF(Fbs1,2) ubiquitin-ligase complexes that contribute to ubiquitination of glycoproteins are involved in the ER-associated degradation pathway. Here we investigated how the SCF(Fbs1,2) complexes interact with unfolded glycoproteins. The SCF(Fbs1) complex was associated with p97/VCP AAA ATPase and bound to integrin-beta1, one of the SCF(Fbs1) substrates, in the cytosol in a manner dependent on p97 ATPase activity. Both Fbs1 and Fbs2 proteins interacted with denatured glycoproteins, which were modified with not only high-mannose but also complex-type oligosaccharides, more efficiently than native proteins. Given that Fbs proteins interact with innermost chitobiose in N-glycans, we propose that Fbs proteins distinguish native from unfolded glycoproteins by sensing the exposed chitobiose structure. |
