The Expanding Horizons of Asparagine-Linked Glycosylation
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 pr...
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| Format: | Article |
| Language: | en_US |
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American Chemical Society
2012
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| Online Access: | http://hdl.handle.net/1721.1/71649 https://orcid.org/0000-0002-5749-7869 |
| _version_ | 1826204490629382144 |
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| author | Larkin, Angelyn Imperiali, Barbara |
| author2 | Massachusetts Institute of Technology. Department of Biology |
| author_facet | Massachusetts Institute of Technology. Department of Biology Larkin, Angelyn Imperiali, Barbara |
| author_sort | Larkin, Angelyn |
| collection | MIT |
| description | 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 (Glc3Man9GlcNAc2), 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. |
| first_indexed | 2024-09-23T12:56:26Z |
| format | Article |
| id | mit-1721.1/71649 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T12:56:26Z |
| publishDate | 2012 |
| publisher | American Chemical Society |
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| spelling | mit-1721.1/716492022-09-28T10:59:14Z The Expanding Horizons of Asparagine-Linked Glycosylation Larkin, Angelyn Imperiali, Barbara Massachusetts Institute of Technology. Department of Biology Massachusetts Institute of Technology. Department of Chemistry Imperiali, Barbara Imperiali, Barbara Larkin, Angelyn 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 (Glc3Man9GlcNAc2), 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. National Institutes of Health (U.S.) (GM039334 ) 2012-07-17T14:31:03Z 2012-07-17T14:31:03Z 2011-04 2011-04 Article http://purl.org/eprint/type/JournalArticle 0006-2960 1520-4995 http://hdl.handle.net/1721.1/71649 Larkin, Angelyn, and Barbara Imperiali. “The Expanding Horizons of Asparagine-Linked Glycosylation.” Biochemistry 50.21 (2011): 4411–4426. Web. https://orcid.org/0000-0002-5749-7869 en_US http://dx.doi.org/10.1021/bi200346n Biochemistry Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. application/pdf American Chemical Society Prof. Imperiali via Erja Kajosalo |
| spellingShingle | Larkin, Angelyn Imperiali, Barbara The Expanding Horizons of Asparagine-Linked Glycosylation |
| title | The Expanding Horizons of Asparagine-Linked Glycosylation |
| title_full | The Expanding Horizons of Asparagine-Linked Glycosylation |
| title_fullStr | The Expanding Horizons of Asparagine-Linked Glycosylation |
| title_full_unstemmed | The Expanding Horizons of Asparagine-Linked Glycosylation |
| title_short | The Expanding Horizons of Asparagine-Linked Glycosylation |
| title_sort | expanding horizons of asparagine linked glycosylation |
| url | http://hdl.handle.net/1721.1/71649 https://orcid.org/0000-0002-5749-7869 |
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