Glycosyltransferase complexes in eukaryotes: long-known, prevalent but still unrecognized.
Glycosyltransferase complexes in eukaryotes: long-known, prevalent but still unrecognized.
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DOI：
10.1007/s00018-015-2066-0
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发表时间：
2016-01
期刊：
影响因子：
--
通讯作者：
Glumoff T
中科院分区：
文献类型：
--
作者：
Kellokumpu S;Hassinen A;Glumoff T
糖基化是蛋白质和脂类最常见和最复杂的细胞修饰。它对多细胞生命至关重要，它的消失往往会导致一种毁灭性的疾病。然而，糖基化在健康和疾病中的潜在机制细节仍不清楚。这在一定程度上是由于多糖修饰的复杂性和动态性，以及不是所有的参与者都被考虑在内的事实。自20世纪60年代末以来，大量研究表明，糖基转移酶在酵母、植物和动物细胞中通常相互形成同分异构体复合体。为了宣传它们的接受性，我们将在这里总结它们的流行率和潜在的糖基化功能重要性的积累数据，主要集中在它们的相互作用，介导这些相互作用的蛋白质结构域，以及在形成复合体时发生的酶活性变化。最后，我们将重点介绍这些酶复合体的少数现有三维结构，以确定它们的个体性质，并强调它们的缺乏是更详细地了解这些酶复合体如何在真核细胞中相互作用和发挥作用的主要障碍。
Glycosylation is the most common and complex cellular modification of proteins and lipids. It is critical for multicellular life and its abrogation often leads to a devastating disease. Yet, the underlying mechanistic details of glycosylation in both health and disease remain unclear. Partly, this is due to the complexity and dynamicity of glycan modifications, and the fact that not all the players are taken into account. Since late 1960s, a vast number of studies have demonstrated that glycosyltransferases typically form homomeric and heteromeric complexes with each other in yeast, plant and animal cells. To propagate their acceptance, we will summarize here accumulated data for their prevalence and potential functional importance for glycosylation focusing mainly on their mutual interactions, the protein domains mediating these interactions, and enzymatic activity changes that occur upon complex formation. Finally, we will highlight the few existing 3D structures of these enzyme complexes to pinpoint their individual nature and to emphasize that their lack is the main obstacle for more detailed understanding of how these enzyme complexes interact and function in a eukaryotic cell.
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