The expanding horizons of asparagine-linked glycosylation.
The expanding horizons of asparagine-linked glycosylation.
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DOI：
10.1021/bi200346n
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发表时间：
2011-05-31
期刊：
影响因子：
2.9
通讯作者：
Imperiali B
中科院分区：
文献类型：
--
作者：
Larkin A;Imperiali B
天冬酰胺连接的糖基化包括低聚糖在聚异戊二烯供体上的顺序组装，然后将多糖整体转移到受体蛋白中的特定天冬酰胺残基上。这些n链聚糖在多种生物过程中发挥着关键作用，如蛋白质折叠、细胞靶向和运动以及免疫反应。在过去的十年中，n -链糖基化领域的研究取得了重大进展，包括新的碳水化合物修饰的发现，参与聚糖组装的酶的生化表征，以及这些聚糖对靶蛋白的生物学影响。现在已经确定，这种酶催化的修饰发生在生命的所有三个领域。然而，尽管在这三个领域中，n链糖蛋白生物合成的整体逻辑相似，但附加聚糖的结构却明显不同，从而以各种方式影响合成蛋白的功能。虽然几乎所有的真核生物都产生相同的新生十四糖（Glc3Man9GlcNAc2），但在通过一系列复杂的糖基修剪和添加步骤转移到蛋白质后，这种糖基结构引入了异质性。相比之下，细菌和古细菌通过在组装过程中使用独特的单糖构建块，在其n链聚糖结构中表现出多样性。在这篇综述中，将总结最近在这三个王国中对这种修饰获得更深入的生化理解的进展。此外，还将简要介绍n -链糖基化在病毒中的作用。
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 last 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 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 amongst 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 transfer to 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.
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影响因子：
4.8
作者：
Bickel, T;Lehle, L;Jakob, CA
通讯作者：
Jakob, CA
DOI：
10.1073/pnas.1932838100
发表时间：
2003-09-30
影响因子：
11.1
作者：
Baar, C;Eppinger, M;Schuster, SC
通讯作者：
Schuster, SC
DOI：
10.1073/pnas.0500044102
发表时间：
2005-02-22
影响因子：
11.1
作者：
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通讯作者：
Aebi, M
影响因子：
4.1
作者：
BAUSE, E
通讯作者：
BAUSE, E
影响因子：
2.9
作者：
Chen, Mark M.;Glover, Kerney Jebrell;Imperiali, Barbara
通讯作者：
Imperiali, Barbara