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- Title
Glycoprotein-specific ubiquitin ligases recognize N-glycans in unfolded substrates.
- Authors
Yukiko Yoshida; Eru Adachi; Kanako Fukiya; Kazuhiro Iwai; Keiji Tanaka
- Abstract
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 SCFFbs1,2 ubiquitin-ligase complexes that contribute to ubiquitination of glycoproteins are involved in the ER-associated degradation pathway. Here we investigated how the SCFFbs1,2 complexes interact with unfolded glycoproteins. The SCFFbs1 complex was associated with p97/VCP AAA ATPase and bound to integrin-ß1, one of the SCFFbs1 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.
- Publication
EMBO Reports, 2005, Vol 6, Issue 3, p239
- ISSN
1469-221X
- Publication type
Academic Journal
- DOI
10.1038/sj.embor.7400351