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PMID: 21506607 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Review

The expanding horizons of asparagine-linked glycosylation.

Biochemistry ·Vol. 50 ·No. 21 ·2011-05-31 ·Pages 4411-26

Larkin A, Imperiali B

Abstract

Asparagine-linked glycosylation involves the sequential assembly of an oligosaccharide onto a polyisoprenyl donor, followed by the en bloc transfer of the glycan to particular asparagine residues within acceptor proteins. These N-linked glycans play a critical role in a wide variety of biological processes, such as protein folding, cellular targeting and motility, and the immune response. In the past decade, research in the field of N-linked glycosylation has achieved major advances, including the discovery of new carbohydrate modifications, the biochemical characterization of the enzymes involved in glycan assembly, and the determination of the biological impact of these glycans on target proteins. It is now firmly established that this enzyme-catalyzed modification occurs in all three domains of life. However, despite similarities in the overall logic of N-linked glycoprotein biosynthesis among the three kingdoms, the structures of the appended glycans are markedly different and thus influence the functions of elaborated proteins in various ways. Though nearly all eukaryotes produce the same nascent tetradecasaccharide (Glc(3)Man(9)GlcNAc(2)), heterogeneity is introduced into this glycan structure after it is transferred to the protein through a complex series of glycosyl trimming and addition steps. In contrast, bacteria and archaea display diversity within their N-linked glycan structures through the use of unique monosaccharide building blocks during the assembly process. In this review, recent progress toward gaining a deeper biochemical understanding of this modification across all three kingdoms will be summarized. In addition, a brief overview of the role of N-linked glycosylation in viruses will also be presented.

MeSH Terms
Asparagine/chemistry Bacteria/metabolism Carbohydrate Sequence Glycosylation Models, Molecular Molecular Sequence Data Viruses/metabolism
Chemicals
Asparagine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Larkin Angelyn
Department of Chemistry Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
Imperiali Barbara
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Article Info
Journal
Biochemistry
Abbr.
Biochemistry
ISSN
1520-4995
DOI
10.1021/bi200346n
Published
2011-05-31
Epub
2011-00-04
Pages
4411-26
Language
English
Region
United States
NLM ID
0370623
PMCID
PMC3101296
Subset
IM
Grants
NIGMS NIH HHS · R01 GM039334 · United States
NIGMS NIH HHS · R01 GM039334-24 · United States
NIGMS NIH HHS · GM039334 · United States
External Links
PubMed source DOI: 10.1021/bi200346n PMC Full Text View journal details
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