[HTML][HTML] Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP
N Hosokawa, I Wada, K Nagasawa, T Moriyama… - Journal of Biological …, 2008 - ASBMB
The recognition of terminally misfolded proteins in the endoplasmic reticulum (ER) and the
extraction of these proteins to the cytoplasm for proteasomal degradation are determined by
a quality control mechanism in the ER. In yeast, Yos9p, an ER lectin containing a mannose 6-
phosphate receptor homology (MRH) domain, enhances ER-associated degradation
(ERAD) of glycoproteins. We show here that human XTP3-B (hXTP3-B), an ER lectin
containing two MRH domains, has two transcriptional variants, and both isoforms retard …
extraction of these proteins to the cytoplasm for proteasomal degradation are determined by
a quality control mechanism in the ER. In yeast, Yos9p, an ER lectin containing a mannose 6-
phosphate receptor homology (MRH) domain, enhances ER-associated degradation
(ERAD) of glycoproteins. We show here that human XTP3-B (hXTP3-B), an ER lectin
containing two MRH domains, has two transcriptional variants, and both isoforms retard …
