ArticleThe Journal of biological chemistry2010
Free oligosaccharides to monitor glycoprotein endoplasmic reticulum-associated degradation in Saccharomyces cerevisiae.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 96 citations in OpenAlex.
- Cytosolic Peptide: N-Glycanase (NGLY1)-from Basic Biology to Genetic Disorder, NGLY1 Deficiency.Advances in experimental medicine and biology · 2026Review
- Structural characterization of zebrafish Ngly2, an ovary-enriched acid PNGase required for egg-free glycan production.The Journal of biological chemistry · 2025Article
- Development of a fluorescence and quencher-based FRET assay for detection of endogenous peptide:N-glycanase/NGLY1 activity.The Journal of biological chemistry · 2024Article
- Mitotic phosphorylation inhibits the Golgi mannosidase MAN1A1.Cell reports · 2022Article
- Comprehensive and Comparative Structural Glycome Analysis in Mouse Epiblast-like Cells.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Article
- Protocol for analyzing the biosynthesis and degradation of N-glycan precursors in mammalian cells.STAR protocols · 2021Article
- A defined glycosylation regulatory network modulates total glycome dynamics during pluripotency state transition.Scientific reports · 2021Article
- Uncoupling the hydrolysis of lipid-linked oligosaccharide from the oligosaccharyl transfer reaction by point mutations in yeast oligosaccharyltransferase.The Journal of biological chemistry · 2020Article
- Cryo-EM structure of fission yeast tetrameric α-mannosidase Ams1.FEBS open bio · 2020Article
- Free glycans derived fromThe Journal of biological chemistry · 2019Article
- Letting go ofThe Journal of biological chemistry · 2019Article
- Protein quality control in the secretory pathway.The Journal of cell biology · 2019Review
- A bioactive mammalian disaccharide associated with autoimmunity activates STING-TBK1-dependent immune response.Nature communications · 2019Article
- Non-lysosomal Degradation of Singly Phosphorylated Oligosaccharides Initiated by the Action of a Cytosolic Endo-β-N-acetylglucosaminidase.The Journal of biological chemistry · 2016Article
- The cytoplasmic peptide:N-glycanase (NGLY1) - Structure, expression and cellular functions.Gene · 2016Review
- Article
- GalNAc-T4 putatively modulates the estrogen regulatory network through FOXA1 glycosylation in human breast cancer cells.Molecular and cellular biochemistry · 2016Article
- Glycosylation-directed quality control of protein folding.Nature reviews. Molecular cell biology · 2015Review
- Article
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Authors and funding
5 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
In eukaryotic cells, N-glycosylation has been recognized as one of the most common and functionally important co- or post-translational modifications of proteins. "Free" forms of N-glycans accumulate in the cytosol of mammalian cells, but the precise mechanism for their formation and degradation remains unknown. Here, we report a method for the isolation of yeast free oligosaccharides (fOSs) using endo-beta-1,6-glucanase digestion. fOSs were undetectable in cells lacking PNG1, coding the cytoplasmic peptide:N-glycanase gene, suggesting that almost all fOSs were formed from misfolded glycoproteins by Png1p. Structural studies revealed that the most abundant fOS was M8B, which is not recognized well by the endoplasmic reticulum-associated degradation (ERAD)-related lectin, Yos9p. In addition, we provide evidence that some of the ERAD substrates reached the Golgi apparatus prior to retrotranslocation to the cytosol. N-Glycan structures on misfolded glycoproteins in cells lacking the cytosol/vacuole alpha-mannosidase, Ams1p, was still quite diverse, indicating that processing of N-glycans on misfolded glycoproteins was more complex than currently envisaged. Under ER stress, an increase in fOSs was observed, whereas levels of M7C, a key glycan structure recognized by Yos9p, were unchanged. Our method can thus provide valuable information on the molecular mechanism of glycoprotein ERAD in Saccharomyces cerevisiae.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.