Disruption of α-mannosidase processing induces non-canonical hybrid-type glycosylation

被引:14
作者
Crispin, Max
Aricescu, A. Radu
Chang, Veronica T.
Jones, E. Yvonne
Stuart, David I.
Dwek, Raymond A.
Davis, Simon J.
Harvey, David J.
机构
[1] Univ Oxford, Div Struct Biol, Wellcome Trust Ctr Human Genet, Oxford OX3 7BN, England
[2] Univ Oxford, Nuffield Dept Clin Med, Oxford OX3 9DS, England
[3] John Radcliffe Hosp, MRC, Human Immunol Unit, Weatherall Inst Mol Med, Oxford OX3 9DS, England
[4] Univ Oxford, Dept Biochem, Glycobiol Inst, Oxford OX1 3QU, England
基金
英国医学研究理事会; 英国惠康基金;
关键词
hybrid-type glycosylation; GlcNAc transferase I; electrospray ionization mass spectrometry; swainsonine; golgi alpha-mannosidase II;
D O I
10.1016/j.febslet.2007.04.020
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
Golgi alpha-mannosidase 11 is essential for the efficient formation of complex-type glycosylation. Here, we demonstrate that the disruption of Golgi a-mannosidase 11 activity by swainsonine in human embryonic kidney cells is capable of inducing a novel class of hybrid-type glycosylation containing a partially processed mannose moiety. The discovery of 'Man(6)-based' hybrid-type glycans reveals a broader in vivo specificity of Nacetylglucosaminyltransferase 1, further defines the arm-specific tolerance of core alpha 1-6 fucosyltransferase to terminal a1-2 mannose residues, and suggests that disruption of Golgi a-mannosidase 11 activity is capable of inducing potentially 'non-self' structures. (C) 2007 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
引用
收藏
页码:1963 / 1968
页数:6
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