The biological functions of Naa10 - From amino-terminal acetylation to human disease.
The biological functions of Naa10 - From amino-terminal acetylation to human disease.
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DOI：
10.1016/j.gene.2015.04.085
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发表时间：
2015-08-10
期刊：
影响因子：
3.5
通讯作者：
Lyon GJ
中科院分区：
文献类型：
--
作者：
Dörfel MJ;Lyon GJ
n端乙酰化（NTA）是已知最丰富的蛋白质修饰之一，而n端乙酰转移酶（NAT）机制在所有真核生物中都是保守的。在过去的50年里，NTA的功能已经开始慢慢被阐明，这包括蛋白质-蛋白质相互作用的调节，蛋白质稳定性，蛋白质功能和蛋白质靶向特定的细胞区室。许多这些功能已经在Naa10/NatA的范围内进行了研究；然而，我们才刚刚开始真正理解这幅图景的全部复杂性。大约40%的人类蛋白质是Naa10的底物，这种修饰的影响只对其中的一些进行了研究。除了在NatA复合体中作为NAT外，最近还发现了其他与Naa10有关的功能，包括翻译后NTA、赖氨酸乙酰化和NAT/ kat无关的功能。此外，最近的出版物将Naa10的突变与各种疾病联系起来，强调了人类Naa10研究的重要性。最近设计和合成的第一种双底物抑制剂可以有效和选择性地抑制NatA/Naa10复合物、单体Naa10和hNaa50，进一步增加了分析Naa10功能的工具集。
N-terminal acetylation (NTA) is one of the most abundant protein modifications known, and the N-terminal acetyltransferase (NAT) machinery is conserved throughout all Eukarya. Over the past 50 years, the function of NTA has begun to be slowly elucidated, and this includes the modulation of protein–protein interaction, protein-stability, protein function, and protein targeting to specific cellular compartments. Many of these functions have been studied in the context of Naa10/NatA; however, we are only starting to really understand the full complexity of this picture. Roughly, about 40% of all human proteins are substrates of Naa10 and the impact of this modification has only been studied for a few of them. Besides acting as a NAT in the NatA complex, recently other functions have been linked to Naa10, including post-translational NTA, lysine acetylation, and NAT/KAT-independent functions. Also, recent publications have linked mutations in Naa10 to various diseases, emphasizing the importance of Naa10 research in humans. The recent design and synthesis of the first bisubstrate inhibitors that potently and selectively inhibit the NatA/Naa10 complex, monomeric Naa10, and hNaa50 further increases the toolset to analyze Naa10 function.
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