Physiological and molecular functions of the cytosolic peptide:N-glycanase

被引：26

作者：

Hirayama, Hiroto ^{[1
]}

Hosomi, Akira ^{[1
]}

Suzuki, Tadashi ^{[1
]}

机构：

[1] RIKEN, Global Res Cluster, Max Planck Joint Ctr Syst Chem Biol, Syst Glycobiol Res Grp,Glycometabolome Team, Tokyo, Japan

来源：

SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY | 2015年 / 41卷

关键词：

Endoplasmic reticulum-associated degradation; Free oligosaccharides; N-glycosylation; Peptide:N-glycanase; Ubiquitin-proteasome system; Rad23; RETICULUM-ASSOCIATED DEGRADATION; NUCLEOTIDE EXCISION-REPAIR; N-LINKED GLYCANS; FREE POLYMANNOSE OLIGOSACCHARIDES; ER-ASSOCIATED DEGRADATION; ENDOPLASMIC-RETICULUM; SACCHAROMYCES-CEREVISIAE; CYTOPLASMIC PEPTIDE; CAENORHABDITIS-ELEGANS; ALPHA-MANNOSIDASE;

D O I：

10.1016/j.semcdb.2014.11.009

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Peptide:N-glycanase (PNGase) is a deglycosylating enzyme that acts on N-glycoproteins. A growing evidence exists to indicate that the cytosolic form of PNGase, which is ubiquitously distributed throughout eukaryotes, is not only implicated in the efficient degradation of misfolded glycoproteins destined for the proteasomal degradation but also in the generation of free oligosaccharides as the initial step in the non-lysosomal catabolism of N-glycans. This article summarizes the current state of our knowledge of the physiological and molecular functions of the cytosolic PNGase in a model organism, Saccharomyces cerevisiae, and also discusses the functional/structural diversities of this molecule within eukaryotes. (C) 2014 Elsevier Ltd. All rights reserved.

引用

页码：110 / 120

页数：11

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