ArticleThe Biochemical journal2006
Man2C1, an alpha-mannosidase, is involved in the trimming of free oligosaccharides in the cytosol.
Article in The Biochemical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 89 citations in OpenAlex.
- Structural characterization of zebrafish Ngly2, an ovary-enriched acid PNGase required for egg-free glycan production.The Journal of biological chemistry · 2025Article
- Free oligosaccharides in serum.BBA advances · 2025Article
- Mechanism of high-mannose N-glycan breakdown and metabolism by Bifidobacterium longum.Nature chemical biology · 2023Article
- Impaired catabolism of free oligosaccharides due to MAN2C1 variants causes a neurodevelopmental disorder.American journal of human genetics · 2022Article
- N-Glycosylation.Advances in experimental medicine and biology · 2021Article
- Rapid and Accurate Visualization of Breast Tumors with a Fluorescent Probe Targeting α-Mannosidase 2C1.ACS central science · 2020Article
- Cryo-EM structure of fission yeast tetrameric α-mannosidase Ams1.FEBS open bio · 2020Article
- Cytosolic FreeFrontiers in plant science · 2020Article
- Free glycans derived fromThe Journal of biological chemistry · 2019Article
- Iminosugar antivirals: the therapeutic sweet spot.Biochemical Society transactions · 2017Review
- Occurrence of complex type free N-glycans with a single GlcNAc residue at the reducing termini in the fresh-water plant, Egeria densa.Glycoconjugate journal · 2017Article
- Non-lysosomal Degradation of Singly Phosphorylated Oligosaccharides Initiated by the Action of a Cytosolic Endo-β-N-acetylglucosaminidase.The Journal of biological chemistry · 2016Article
- Article
- Generation and degradation of free asparagine-linked glycans.Cellular and molecular life sciences : CMLS · 2015Review
- Interaction of platelet endothelial cell adhesion molecule (PECAM) with α2,6-sialylated glycan regulates its cell surface residency and anti-apoptotic role.The Journal of biological chemistry · 2014Article
- Accumulation of free oligosaccharides and tissue damage in cytosolic α-mannosidase (Man2c1)-deficient mice.The Journal of biological chemistry · 2014Article
- Characterisation of class I and II α-mannosidases from Drosophila melanogaster.Glycoconjugate journal · 2013Article
- Deficiency of α-glucosidase I alters glycoprotein glycosylation and lifespan in Caenorhabditis elegans.Glycobiology · 2013Article
- Basal autophagy is required for the efficient catabolism of sialyloligosaccharides.The Journal of biological chemistry · 2013Article
- Dual functions for cytosolic α-mannosidase (Man2C1): its down-regulation causes mitochondria-dependent apoptosis independently of its α-mannosidase activity.The Journal of biological chemistry · 2013Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The endoplasmic-reticulum-associated degradation of misfolded (glyco)proteins ensures that only functional, correctly folded proteins exit from the endoplasmic reticulum and that misfolded ones are degraded by the ubiquitin-proteasome system. During the degradation of misfolded glycoproteins, they are deglycosylated by the PNGase (peptide:N-glycanase). The free oligosaccharides released by PNGase are known to be further catabolized by a cytosolic alpha-mannosidase, although the gene encoding this enzyme has not been identified unequivocally. The findings in the present study demonstrate that an alpha-mannosidase, Man2C1, is involved in the processing of free oligosaccharides that are formed in the cytosol. When the human Man2C1 orthologue was expressed in HEK-293 cells, most of the enzyme was localized in the cytosol. Its activity was enhanced by Co2+, typical of other known cytosolic alpha-mannosidases so far characterized from animal cells. The down-regulation of Man2C1 activity by a small interfering RNA drastically changed the amount and structure of oligosaccharides accumulating in the cytosol, demonstrating that Man2C1 indeed is involved in free oligosaccharide processing in the cytosol. The oligosaccharide processing in the cytosol by PNGase, endo-beta-N-acetylglucosaminidase and alpha-mannosidase may represent the common 'non-lysosomal' catabolic pathway for N-glycans in animal cells, although the molecular mechanism as well as the functional importance of such processes remains to be determined.
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