caa a22 4500 606177426 CHVBK 20210128100752.0 cr unu---uuuuu 210128e20150701xx s 000 0 eng 10.1007/s00018-015-1881-7 doi (NATIONALLICENCE)springer-10.1007/s00018-015-1881-7 Generation and degradation of free asparagine-linked glycans [Elektronische Daten] [Yoichiro Harada, Hiroto Hirayama, Tadashi Suzuki] Asparagine (N)-linked protein glycosylation, which takes place in the eukaryotic endoplasmic reticulum (ER), is important for protein folding, quality control and the intracellular trafficking of secretory and membrane proteins. It is known that, during N-glycosylation, considerable amounts of lipid-linked oligosaccharides (LLOs), the glycan donor substrates for N-glycosylation, are hydrolyzed to form free N-glycans (FNGs) by unidentified mechanisms. FNGs are also generated in the cytosol by the enzymatic deglycosylation of misfolded glycoproteins during ER-associated degradation. FNGs derived from LLOs and misfolded glycoproteins are eventually merged into one pool in the cytosol and the various glycan structures are processed to a near homogenous glycoform. This article summarizes the current state of our knowledge concerning the formation and catabolism of FNGs. Springer Basel, 2015 Free N-glycan nationallicence Oligosaccharyltransferase nationallicence Pyrophosphatase nationallicence Peptide:N-glycanase nationallicence Yeast nationallicence Mammals nationallicence Harada Yoichiro Glycometabolome Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center, Global Research Cluster, RIKEN, 2-1 Hirosawa, 351-0198, Wako, Saitama, Japan aut Hirayama Hiroto Glycometabolome Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center, Global Research Cluster, RIKEN, 2-1 Hirosawa, 351-0198, Wako, Saitama, Japan aut Suzuki Tadashi Glycometabolome Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center, Global Research Cluster, RIKEN, 2-1 Hirosawa, 351-0198, Wako, Saitama, Japan aut Cellular and Molecular Life Sciences Springer Basel 72/13(2015-07-01), 2509-2533 1420-682X 72:13<2509 2015 72 18 https://doi.org/10.1007/s00018-015-1881-7 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00018-015-1881-7 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Harada Yoichiro Glycometabolome Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center, Global Research Cluster, RIKEN, 2-1 Hirosawa, 351-0198, Wako, Saitama, Japan aut NATIONALLICENCE 700 1- Hirayama Hiroto Glycometabolome Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center, Global Research Cluster, RIKEN, 2-1 Hirosawa, 351-0198, Wako, Saitama, Japan aut NATIONALLICENCE 700 1- Suzuki Tadashi Glycometabolome Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center, Global Research Cluster, RIKEN, 2-1 Hirosawa, 351-0198, Wako, Saitama, Japan aut NATIONALLICENCE 773 0- Cellular and Molecular Life Sciences Springer Basel 72/13(2015-07-01), 2509-2533 1420-682X 72:13<2509 2015 72 18