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Yoshida, Y. et al.

Yoshida, Adachi, Fukiya, Iwai, Tanaka,

Glycoprotein-specific ubiquitin ligases recognize N-glycans in unfolded substrates.

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.[1]

References

Glycoprotein-specific ubiquitin ligases recognize N-glycans in unfolded substrates. Yoshida, Y., Adachi, E., Fukiya, K., Iwai, K., Tanaka, K. EMBO Rep. (2005) [Pubmed]

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