Mutations in SEC63 cause autosomal dominant polycystic liver disease
S Davila, L Furu, AG Gharavi, X Tian, T Onoe, Q Qian… - Nature …, 2004 - nature.com
Nature genetics, 2004•nature.com
Mutations in PRKCSH, encoding the β-subunit of glucosidase II, an N-linked glycan-
processing enzyme in the endoplasmic reticulum (ER), cause autosomal dominant
polycystic liver disease. We found that mutations in SEC63, encoding a component of the
protein translocation machinery in the ER, also cause this disease. These findings are
suggestive of a role for cotranslational protein-processing pathways in maintaining epithelial
luminal structure and implicate noncilial ER proteins in human polycystic disease.
processing enzyme in the endoplasmic reticulum (ER), cause autosomal dominant
polycystic liver disease. We found that mutations in SEC63, encoding a component of the
protein translocation machinery in the ER, also cause this disease. These findings are
suggestive of a role for cotranslational protein-processing pathways in maintaining epithelial
luminal structure and implicate noncilial ER proteins in human polycystic disease.
Abstract
Mutations in PRKCSH, encoding the β-subunit of glucosidase II, an N-linked glycan-processing enzyme in the endoplasmic reticulum (ER), cause autosomal dominant polycystic liver disease. We found that mutations in SEC63, encoding a component of the protein translocation machinery in the ER, also cause this disease. These findings are suggestive of a role for cotranslational protein-processing pathways in maintaining epithelial luminal structure and implicate noncilial ER proteins in human polycystic disease.
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