O-linked glycosylation - meaning and definition. What is O-linked glycosylation
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  3. O-linked glycosylation

What (who) is O-linked glycosylation - definition


O-linked glycosylation         
O-linked glycosylation is the attachment of a sugar molecule to the oxygen atom of serine (Ser) or threonine (Thr) residues in a protein. O-glycosylation is a post-translational modification that occurs after the protein has been synthesised.
https://en.wikipedia.org/wiki/O-linked_glycosylation
O-GlcNAc         
  • Chemoenzymatic labeling for the detection of ''O''-GlcNAc. GalT Y289L transfers GalNAz to ''O''-GlcNAc, providing a handle for click chemistry. Various probes can be conjugated via azide-alkyne cycloaddition. Attachment of a PEG5K mass tag allows for visualization of ''O''-GlcNAc stoichiometry.
  • FRET biosensor for ''O''-GlcNAc. Under high ''O''-GlcNAc conditions, GafD will bind the ''O''-GlcNAc group on the CKII peptide substrate, bringing CFP and YFP into proximity for FRET. Various localization sequences can be fused to localize the sensor to various cellular compartments, e.g., nucleus, cytoplasm, and plasma membrane.
  • Structure of IsoTaG probe. Probe consists of a biotin affinity tag (red), a linker (black), an acid-cleavable silane (blue), an isotope recoding motif (green), and an alkyne (purple).
  • Site-directed mutagenesis for manipulating ''O''-GlcNAc. S/T-to-A mutagenesis prevents ''O''-GlcNAc modification at that residue. S/T-to-C mutagenesis allows for generation of the ''S''-GlcNAc modification, a structural analogue of ''O''-GlcNAc that is not readily hydrolyzed by OGA.
  • ''O''-GlcNAcylation of serine and threonine residues is dynamically controlled by OGT and OGA.
  • GalT radiolabeling of cellular proteins with UDP-[<sup>3</sup>H]galactose followed by β-elimination yielded Galβ1-4GlcNAcitol, suggesting that the substrate for GalT was ''O''-GlcNAc. Radiolabeled [<sup>3</sup>H]galactose shown in red.
  • ''Left'': Model of full-length ncOGT in complex with CKII peptide substrate and UDP.<ref name=":5" /> Colors indicate TPR domain (gray), N-terminal region of catalytic domain (light pink), intervening domain (light green), C-terminal region of catalytic domain (light blue), CKII peptide substrate (green), and UDP (cyan). ''Right'': Structure of human OGA D175N dimer in complex with ''O''-GlcNAcylated TAB1 peptide substrate. Monomers shown in blue-white/light yellow with respective peptide substrates in blue/yellow. (PDB: 5VVU)
  • PDB]]: 4GYW)
  • doi-access=free}}</ref>
THE GLYCOSYLATION OF A PROTEIN BY ADDITION OF N-ACETYLGLUCOSAMINE VIA THE O3 ATOM OF PEPTIDYL-THREONINE, FORMING O3-N-ACETYLGLUCOSAMINE-L-THREONINE.
O-linked β-N-acetylglucosamine (O-GlcNAc); O-glcnac; O-linked beta-N-acetylglucosamine; O-Linked β-N-acetylglucosamine; O-GlcNAcylation; O GlcNAc; Oglcnac; O-linked glcnac
O-GlcNAc (short for O-linked GlcNAc or O-linked β-N-acetylglucosamine) is a reversible enzymatic post-translational modification that is found on serine and threonine residues of nucleocytoplasmic proteins. The modification is characterized by a β-glycosidic bond between the hydroxyl group of serine or threonine side chains and N-acetylglucosamine (GlcNAc).
https://en.wikipedia.org/wiki/O-GlcNAc
N-linked glycosylation         
  • Biosynthesis pathway of ''N''-linked glycoproteins: The synthesis of ''N''-linked glycan starts in the endoplasmic reticulum, continues in the Golgi and ends at the plasma membrane, where the ''N''-linked glycoproteins are either secreted or becomes embedded in the plasma membrane.
  • The difference between the glycan produced by humans and animal cells. Human cells lack the Neu5Gc cap.
  • Glycan processing in the ER and Golgi.
  • Step-by-step synthesis of the precursor oligosaccharide in the ER lumen during ''N''-linked glycosylation: the diagram illustrates the steps occurring in both the Phase I and Phase II as described in the table.
  • The three major types of glycans.
N-linked glycosylation, is the attachment of an oligosaccharide, a carbohydrate consisting of several sugar molecules, sometimes also referred to as glycan, to a nitrogen atom (the amide nitrogen of an asparagine (Asn) residue of a protein), in a process called N-glycosylation, studied in biochemistry. This type of linkage is important for both the structure and function of many eukaryotic proteins.
https://en.wikipedia.org/wiki/N-linked_glycosylation
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