Generation and degradation of free asparagine-linked glycans

Cellular and Molecular Life Sciences : CMLS
Yoichiro HaradaTadashi Suzuki

Abstract

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.

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Citations

Aug 13, 2015·Bioscience, Biotechnology, and Biochemistry·Tanim Jabid HossainTadashi Suzuki
Apr 18, 2016·Molecular Aspects of Medicine·Ian LokeMorten Thaysen-Andersen
Apr 8, 2017·Omics : a Journal of Integrative Biology·Eric AduaWei Wang
Sep 6, 2018·Proceedings of the National Academy of Sciences of the United States of America·Hua LuMark A Lehrman
Dec 8, 2019·International Journal of Molecular Sciences·Yoichiro HaradaNaoyuki Taniguchi
Sep 28, 2020·FEBS Open Bio·Jianxiu ZhangKeqiong Ye
Oct 15, 2020·Cell Reports·Yoichiro HaradaIkuro Maruyama
Sep 8, 2021·The FEBS Journal·Yoichiro HaradaNaoyuki Taniguchi
Sep 29, 2021·Journal of Biochemistry·Haruhiko FujihiraTadashi Suzuki

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