Free and N-linked oligomannosides as markers of the quality control of newly synthesized glycoproteins.
It appears increasingly evident that the oligomannoside type N-glycans play important roles in the fate of newly synthesized glycoproteins in the rough endoplasmic reticulum. The variety of protein-bound oligomannoside isomers are involved in the quality control of glycoprotein, in their transport into the Golgi and probably as a degradation signal. A prerequisite of the degradation in the cytosol by the proteasome pathway is the release of the glycans as free oligomannosides. These oligomannosides are further processed in the cytosol into a peculiar isomer of Man5GlcNAc1 which enters into the lysosome to be further degraded into monosaccharides. In this review, we will illustrate how the different species of N-linked and free oligomannosides either are involved or are markers of the quality control and fate of newly synthesized glycoproteins.
Cacan
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R
Laboratoire de Chimie Biologique, UMR n degrees 111 du CNRS, Université des Sciences et Technologies de Lille, Villeneuve d'Ascq Cedex, 59655, France.
Verbert
A
A
D015415:Biomarkers; D018870:Endoplasmic Reticulum, Rough / Q000378:metabolism*; D006023:Glycoproteins / Q000096:biosynthesis*; D006868:Hydrolysis; D009844:Oligosaccharides / Q000378:metabolism*; D017510:Protein Folding; D011499:Protein Processing, Post-Translational; D011786:Quality Control
D015415:Biomarkers; D006023:Glycoproteins; D009844:Oligosaccharides; C028569:oligomannoside