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Tsutomu Fujimori, Yukiko Kamiya, Kazuhiro Nagata, Koichi Kato and Nobuko Hosokawa Endoplasmic reticulum lectin XTP3-B inhibits endoplasmic reticulum-associated degradation of a misfolded α1-antitrypsin variant The FEBS Journal 280

Version of Record online: 28 FEB 2013 | DOI: 10.1111/febs.12157

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Mammalian XTP3-B is an endoplasmic reticulum (ER)-resident lectin that contains two mannose 6-phosphate receptor homology (MRH) domains, which recognize sugar moieties, and is involved in ER-associated degradation (ERAD). XTP3-B did not enhance the degradation of misfolded glycoproteins, but instead inhibited the degradation of NHK bearing M9 oligosaccharides, unlike its homologue OS-9. We propose that XTP3-B acts as a negative regulator of ERAD.

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