4.5 Article

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

Journal

FEBS LETTERS
Volume 581, Issue 10, Pages 1963-1968

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2007.04.020

Keywords

hybrid-type glycosylation; GlcNAc transferase I; electrospray ionization mass spectrometry; swainsonine; golgi alpha-mannosidase II

Funding

  1. Medical Research Council [G9900061, G0500365] Funding Source: researchfish
  2. Medical Research Council [G9900061, G0500365] Funding Source: Medline
  3. Wellcome Trust [081894] Funding Source: Medline
  4. MRC [G0500365, G9900061] Funding Source: UKRI

Ask authors/readers for more resources

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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.5
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available