ArticleProtein science : a publication of the Protein Society2016
Interaction mode between catalytic and regulatory subunits in glucosidase II involved in ER glycoprotein quality control.
Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 21 citations in OpenAlex.
- Identification and validation of endoplasmic reticulum autophagy-related potential biomarkers in periodontitis.Scientific reports · 2025Article
- PRKCSH serves as a potential immunological and prognostic biomarker in pan-cancer.Scientific reports · 2024Article
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- Insight into broad substrate specificity and synergistic contribution of a fungal α-glucosidase in Chinese Nong-flavor daqu.Microbial cell factories · 2023Article
- Novel GANAB variants associated with polycystic liver disease.Orphanet journal of rare diseases · 2020Article
- PRKCSH contributes to tumorigenesis by selective boosting of IRE1 signaling pathway.Nature communications · 2019Article
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5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The glycoside hydrolase family 31 (GH31) α-glucosidases play vital roles in catabolic and regulated degradation, including the α-subunit of glucosidase II (GIIα), which catalyzes trimming of the terminal glucose residues of N-glycan in glycoprotein processing coupled with quality control in the endoplasmic reticulum (ER). Among the known GH31 enzymes, only GIIα functions with its binding partner, regulatory β-subunit (GIIβ), which harbors a lectin domain for substrate recognition. Although the structural data have been reported for GIIα and the GIIβ lectin domain, the interaction mode between GIIα and GIIβ remains unknown. Here, we determined the structure of a complex formed between GIIα and the GIIα-binding domain of GIIβ, thereby providing a structural basis underlying the functional extension of this unique GH31 enzyme.
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