| Literature DB >> 15133510 |
Sonia Davila1, Laszlo Furu, Ali G Gharavi, Xin Tian, Tamehito Onoe, Qi Qian, Airong Li, Yiqiang Cai, Patrick S Kamath, Bernard F King, Pablo J Azurmendi, Pia Tahvanainen, Helena Kääriäinen, Krister Höckerstedt, Olivier Devuyst, Yves Pirson, Rodolfo S Martin, Richard P Lifton, Esa Tahvanainen, Vicente E Torres, Stefan Somlo.
Abstract
Mutations in PRKCSH, encoding the beta-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.Entities:
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Year: 2004 PMID： 15133510 DOI： 10.1038/ng1357
Source DB: PubMed Journal: Nat Genet ISSN： 1061-4036 Impact factor: 38.330