Cytoplasmic peptide:N-glycanase and catabolic pathway for free N-glycans in the cytosol |
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Authors: | Tadashi Suzuki |
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Institution: | aDepartment of Biochemistry, 21st Center of Excellence Program (COE), Osaka University Graduate School of Medicine, Japan;bCore Research for Evolutionary Science and Technology (CREST), Japan Science and Technology Agency (JST), Japan |
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Abstract: | Peptide:N-glycanase (PNGase) releases N-glycans from glycoproteins/glycopeptides. Cytoplasmic PNGase is widely recognized as a component of machinery for ER-associated degradation (ERAD), i.e. proteasomal degradation of misfolded, newly synthesized (glyco)proteins that have been exported from the ER. The enzyme belongs to the “transglutaminase superfamily” that contains a putative catalytic triad of cysteine, histidine, and aspartic acid. The mammalian orthologues of PNGase contain the N-terminal PUB domain that serves as the protein–protein interaction domain. The C-terminus of PNGase was recently found to be a novel carbohydrate-binding domain. Taken together, these observations indicate that C-terminus of mammalian PNGase is important for recognition of the substrates while N-terminus of this enzyme is involved in assembly of a degradation complex. |
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Keywords: | Peptide:N-glycanase ER-associated degradation Free oligosaccharide PUB domain |
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