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100+ datasets found
  1. R

    Data from: Asparagine N-linked glycosylation

    • reactome.org
    biopax2, biopax3 +5
  2. o

    Data from: Site-specific N-glycosylation of HeLa cell glycoproteins

    • www.omicsdi.org
    xml
  3. e

    N-glycosylation protein EOS1

    • www.ebi.ac.uk
    Updated Mar 4, 2012
  4. Data from: Glycosylation of a CNS-specific extracellular matrix...

    • researchdata.edu.au
    Updated Jun 26, 2012
  5. Data from: An Enzymatic Deglycosylation Scheme Enabling Identification of...

    • figshare.com
    • acs.figshare.com
    xls
    Updated Apr 2, 2020
  6. o

    Data from: Chemical labeling for fine mapping of IgG N-glycosylation by...

    • www.omicsdi.org
    xml
  7. o

    Data from: Quantitative Profiling of N-linked Glycosylation Machinery in...

    • www.omicsdi.org
    • www.ebi.ac.uk
    xml
    Updated May 19, 2021
  8. R

    Data from: Diseases of glycosylation

    • reactome.org
    biopax2, biopax3 +5
  9. s

    O-GLYCBASE

    • scicrunch.org
    Updated Jan 1, 1999
  10. e

    Data from: An integrated strategy reveals complex glycosylation of...

    • www.ebi.ac.uk
    Updated Jun 14, 2021
  11. o

    1. Site-specific O-glycosylation analysis of SARS-CoV-2 spike protein...

    • www.omicsdi.org
    xml
  12. o

    Data from: O-linked glycosylation sites profiling in Mycobacterium...

    • www.omicsdi.org
    xml
  13. e

    Data from: The Glycosylation Design Space for Recombinant Lysosomal...

    • www.ebi.ac.uk
    • www.omicsdi.org
  14. o

    Data from: Functional analysis of the Helicobacter pullorum N-linked protein...

    • www.omicsdi.org
    xml
  15. o

    Data from: N-glycosylation Profiling of Colorectal Cancer Cell Lines Reveals...

    • www.omicsdi.org
    xml
  16. Data from: Separation and characterization of the two Asn-linked...

    • researchdata.edu.au
    Updated Jun 26, 2012
  17. o

    Data from: The metacaspase Mca1p restricts O-glycosylation during...

    • www.omicsdi.org
    • www.ebi.ac.uk
    xml
  18. a

    congenital disorder of glycosylation In

    • www.alliancegenome.org
    Updated Sep 4, 2019
  19. e

    Site-specific N-glycosylation Characterization of Recombinant SARS-CoV-2...

    • www.ebi.ac.uk
    • covid-19.openaire.eu
    • +1more
    Updated Apr 22, 2021
  20. e

    Data from: O-glycan initiation directs distinct biological pathways and...

    • www.ebi.ac.uk
    • www.omicsdi.org
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Giovanni Dall'Olio, Asparagine N-linked glycosylation [Dataset]. https://reactome.org/content/detail/R-HSA-446203

Data from: Asparagine N-linked glycosylation

Related Article
sbml, owl, sbgn, biopax2, docx, biopax3, pdfAvailable download formats
Authors
Giovanni Dall'Olio
License

Attribution 4.0 (CC BY 4.0)https://creativecommons.org/licenses/by/4.0/
License information was derived automatically

Description

N-linked glycosylation is the most important form of post-translational modification for proteins synthesized and folded in the Endoplasmic Reticulum (Stanley et al. 2009). An early study in 1999 revealed that about 50% of the proteins in the Swiss-Prot database at the time were N-glycosylated (Apweiler et al. 1999). It is now established that the majority of the proteins in the secretory pathway require glycosylation in order to achieve proper folding.
The addition of an N-glycan to a protein can have several roles (Shental-Bechor & Levy 2009). First, glycans enhance the solubility and stability of the proteins in the ER, the golgi and on the outside of the cell membrane, where the composition of the medium is strongly hydrophilic and where proteins, that are mostly hydrophobic, have difficulty folding properly. Second, N-glycans are used as signal molecules during the folding and transport process of the protein: they have the role of labels to determine when a protein must interact with a chaperon, be transported to the golgi, or targeted for degradation in case of major folding defects. Third, and most importantly, N-glycans on completely folded proteins are involved in a wide range of processes: they help determine the specificity of membrane receptors in innate immunity or in cell-to-cell interactions, they can change the properties of hormones and secreted proteins, or of the proteins in the vesicular system inside the cell.
All N-linked glycans are derived from a common 14-sugar oligosaccharide synthesized in the ER, which is attached co-translationally to a protein while this is being translated inside the reticulum. The process of the synthesis of this glycan, known as Synthesis of the N-glycan precursor or LLO, constitutes one of the most conserved pathways in eukaryotes, and has been also observed in some eubacteria. The attachment usually happens on an asparagine residue within the consensus sequence asparagine-X-threonine by an complex called oligosaccharyl transferase (OST).
After being attached to an unfolded protein, the glycan is used as a label molecule in the folding process (also known as Calnexin/Calreticulin cycle) (Lederkremer 2009). The majority of the glycoproteins in the ER require at least one glycosylated residue in order to achieve proper folding, even if it has been shown that a smaller portion of the proteins in the ER can be folded without this modification.
Once the glycoprotein has achieved proper folding, it is transported via the cis-Golgi through all the Golgi compartments, where the glycan is further modified according to the properties of the glycoprotein. This process involves relatively few enzymes but due to its combinatorial nature, can lead to several millions of different possible modifications. The exact topography of this network of reactions has not been established yet, representing one of the major challenges after the sequencing of the human genome (Hossler et al. 2006).
Since N-glycosylation is involved in an great number of different processes, from cell-cell interaction to folding control, mutations in one of the genes involved in glycan assembly and/or modification can lead to severe development problems (often affecting the central nervous system). All the diseases in genes involved in glycosylation are collectively known as Congenital Disorders of Glycosylation (CDG) (Sparks et al. 2003), and classified as CDG type I for the genes in the LLO synthesis pathway, and CDG type II for the others.

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