Analysis of site-specific N-glycan remodeling in the endoplasmic reticulum and the Golgi

被引:57
作者
Hang, Ivan [1 ]
Lin, Chia-wei [1 ]
Grant, Oliver C. [3 ]
Fleurkens, Susanna [1 ]
Villiger, Thomas K. [2 ]
Soos, Miroslav [2 ]
Morbidelli, Massimo [2 ]
Woods, Robert J. [3 ]
Gauss, Robert [1 ]
Aebi, Markus [1 ]
机构
[1] Swiss Fed Inst Technol, Inst Microbiol, Dept Biol, CH-8093 Zurich, Switzerland
[2] Swiss Fed Inst Technol, Inst Chem & Bioengn, Dept Chem & Appl Biosci, CH-8093 Zurich, Switzerland
[3] Univ Georgia, Complex Carbohydrate Res Ctr, Athens, GA 30602 USA
基金
瑞士国家科学基金会; 美国国家卫生研究院;
关键词
endoplasmic reticulum glycosylation; Golgi; Golgi glycosylation; site-specific glycosylation; MOLECULAR-DYNAMICS SIMULATIONS; INDIVIDUAL GLYCOSYLATION SITES; CARBOHYDRATE INTERACTIONS; LINKED OLIGOSACCHARIDES; MATHEMATICAL-MODEL; ALPHA-MANNOSIDASES; CRYSTAL-STRUCTURE; RECOGNITION; SUGGESTS; MANNOSE;
D O I
10.1093/glycob/cwv058
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The hallmark of N-linked protein glycosylation is the generation of diverse glycan structures in the secretory pathway. Dynamic, non-template-driven processes of N-glycan remodeling in the endoplasmic reticulum and the Golgi provide the cellular setting for structural diversity. We applied newly developed mass spectrometry-based analytics to quantify site-specific N-glycan remodeling of the model protein Pdi1p expressed in insect cells. Molecular dynamics simulation, mutational analysis, kinetic studies of in vitro processing events and glycan flux analysis supported the defining role of the protein in N-glycan processing.
引用
收藏
页码:1335 / 1349
页数:15
相关论文
共 61 条
[1]   N-glycan structures: recognition and processing in the ER [J].
Aebi, Markus ;
Bernasconi, Riccardo ;
Clerc, Simone ;
Molinari, Maurizio .
TRENDS IN BIOCHEMICAL SCIENCES, 2010, 35 (02) :74-82
[2]   Dynamic metabolic flux analysis - tools for probing transient states of metabolic networks [J].
Antoniewicz, Maciek R. .
CURRENT OPINION IN BIOTECHNOLOGY, 2013, 24 (06) :973-978
[3]  
Case D.A., 2014, Amber 14, V14
[4]   PARTICLE MESH EWALD - AN N.LOG(N) METHOD FOR EWALD SUMS IN LARGE SYSTEMS [J].
DARDEN, T ;
YORK, D ;
PEDERSEN, L .
JOURNAL OF CHEMICAL PHYSICS, 1993, 98 (12) :10089-10092
[5]   A dynamic mathematical model for monoclonal antibody N-linked glycosylation and nucleotide sugar donor transport within a maturing Golgi apparatus [J].
del Val, Ioscani Jimenez ;
Nagy, Judit M. ;
Kontoravdi, Cleo .
BIOTECHNOLOGY PROGRESS, 2011, 27 (06) :1730-1743
[6]  
DELL A, 1994, METHOD ENZYMOL, V230, P108
[7]  
Dell Anne, 2010, Int J Microbiol, V2010, P148178, DOI 10.1155/2010/148178
[8]   ANALYSIS OF DERIVATIZED CERAMIDES AND NEUTRAL GLYCOSPHINGOLIPIDS BY HIGH-PERFORMANCE TANDEM MASS-SPECTROMETRY [J].
DOMON, B ;
VATH, JE ;
COSTELLO, CE .
ANALYTICAL BIOCHEMISTRY, 1990, 184 (01) :151-164
[9]   Site-specific glycosylation analysis of the bovine lysosomal α-mannosidase [J].
Faid, V ;
Evjen, G ;
Tollersrud, OK ;
Michalski, JC ;
Morelle, W .
GLYCOBIOLOGY, 2006, 16 (05) :440-461
[10]   Unique carbohydrate-carbohydrate interactions are required for high affinity binding between FcγRIII and antibodies lacking core fucose [J].
Ferrara, Claudia ;
Grau, Sandra ;
Jaeger, Christiane ;
Sondermann, Peter ;
Bruenker, Peter ;
Waldhauer, Inja ;
Hennig, Michael ;
Ruf, Armin ;
Rufer, Arne Christian ;
Stihle, Martine ;
Umana, Pablo ;
Benz, Joerg .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2011, 108 (31) :12669-12674