title: Interaction mode between catalytic and regulatory subunits in glucosidase II involved in ER glycoprotein quality control.
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.
authors: Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya, 467-8603, Japan. tadashisatoh@phar.nagoya-cu.ac.jp.|JST, PRESTO, 3-1 Tanabe-dori, Mizuho-ku, Nagoya, 467-8603, Japan. tadashisatoh@phar.nagoya-cu.ac.jp.
authors: Tadashi
authors: T
authors: Satoh
authors: Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya, 467-8603, Japan.|Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, Aichi, 444-8787, Japan.|Institute for Molecular Science, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, Aichi, 444-8787, Japan.
authors: Takayasu
authors: T
authors: Toshimori
authors: Department of Biotechnology, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka, 565-0871, Japan.
authors: Masanori
authors: M
authors: Noda
authors: Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, Aichi, 444-8787, Japan.|Department of Biotechnology, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka, 565-0871, Japan.
authors: Susumu
authors: S
authors: Uchiyama
authors: Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya, 467-8603, Japan. kkatonmr@ims.ac.jp.|Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, Aichi, 444-8787, Japan. kkatonmr@ims.ac.jp.|Institute for Molecular Science, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, Aichi, 444-8787, Japan. kkatonmr@ims.ac.jp.
authors: Koichi
authors: K
authors: Kato
mesh_terms: D020134:Catalytic Domain; D002597:Chaetomium / Q000737:chemistry / Q000201:enzymology*; D004721:Endoplasmic Reticulum / Q000201:enzymology*; D005656:Fungal Proteins / Q000737:chemistry*; D006801:Humans; D020836:Protein Structure, Quaternary; D000520:alpha-Glucosidases / Q000737:chemistry*
chemical_list: D005656:Fungal Proteins; C034251:4-nitrophenyl-alpha-glucosidase; D000520:alpha-Glucosidases
keywords: ER quality control; GH31; crystal structure; glucosidase II; regulatory subunit