Literature DB >> 11269317

Intracellular functions of N-linked glycans.

A Helenius1, M Aebi.   

Abstract

N-linked oligosaccharides arise when blocks of 14 sugars are added cotranslationally to newly synthesized polypeptides in the endoplasmic reticulum (ER). These glycans are then subjected to extensive modification as the glycoproteins mature and move through the ER via the Golgi complex to their final destinations inside and outside the cell. In the ER and in the early secretory pathway, where the repertoire of oligosaccharide structures is still rather small, the glycans play a pivotal role in protein folding, oligomerization, quality control, sorting, and transport. They are used as universal "tags" that allow specific lectins and modifying enzymes to establish order among the diversity of maturing glycoproteins. In the Golgi complex, the glycans acquire more complex structures and a new set of functions. The division of synthesis and processing between the ER and the Golgi complex represents an evolutionary adaptation that allows efficient exploitation of the potential of oligosaccharides.

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Year:  2001        PMID: 11269317     DOI: 10.1126/science.291.5512.2364

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  635 in total

1.  Ricin A chain without its partner B chain is degraded after retrotranslocation from the endoplasmic reticulum to the cytosol in plant cells.

Authors:  A Di Cola; L Frigerio; J M Lord; A Ceriotti; L M Roberts
Journal:  Proc Natl Acad Sci U S A       Date:  2001-12-04       Impact factor: 11.205

Review 2.  A novel lectin in the secretory pathway. An elegant mechanism for glycoprotein elimination.

Authors:  I Braakman
Journal:  EMBO Rep       Date:  2001-08       Impact factor: 8.807

3.  Uncovering secretory secrets: inhibition of endoplasmic reticulum (ER) glucosidases suggests a critical role for ER quality control in plant growth and development.

Authors:  A Vitale
Journal:  Plant Cell       Date:  2001-06       Impact factor: 11.277

4.  A role for N-glycanase in the cytosolic turnover of glycoproteins.

Authors:  Christian Hirsch; Daniël Blom; Hidde L Ploegh
Journal:  EMBO J       Date:  2003-03-03       Impact factor: 11.598

5.  Outside-in signaling of cellulose synthesis by a spore coat protein in Dictyostelium.

Authors:  Christopher M West; Ping Zhang; Aiko C McGlynn; Lee Kaplan
Journal:  Eukaryot Cell       Date:  2002-04

Review 6.  Plant lectins: occurrence, biochemistry, functions and applications.

Authors:  H Rüdiger; H J Gabius
Journal:  Glycoconj J       Date:  2001-08       Impact factor: 2.916

Review 7.  Protein aggregation in disease: a role for folding intermediates forming specific multimeric interactions.

Authors:  Arthur Horwich
Journal:  J Clin Invest       Date:  2002-11       Impact factor: 14.808

Review 8.  Emerging technologies for making glycan-defined glycoproteins.

Authors:  Lai-Xi Wang; Joseph V Lomino
Journal:  ACS Chem Biol       Date:  2011-12-14       Impact factor: 5.100

9.  Revisiting the substrate specificity of mammalian α1,6-fucosyltransferase reveals that it catalyzes core fucosylation of N-glycans lacking α1,3-arm GlcNAc.

Authors:  Qiang Yang; Roushu Zhang; Hui Cai; Lai-Xi Wang
Journal:  J Biol Chem       Date:  2017-07-20       Impact factor: 5.157

10.  Quantitative liquid chromatography-mass spectrometry-multiple reaction monitoring (LC-MS-MRM) analysis of site-specific glycoforms of haptoglobin in liver disease.

Authors:  Miloslav Sanda; Petr Pompach; Zuzana Brnakova; Jing Wu; Kepher Makambi; Radoslav Goldman
Journal:  Mol Cell Proteomics       Date:  2013-02-06       Impact factor: 5.911

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