Nonenzymatic protein acylation as a carbon stress regulated by sirtuin deacylases.
Nonenzymatic protein acylation as a carbon stress regulated by sirtuin deacylases.
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DOI：
10.1016/j.molcel.2014.03.027
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发表时间：
2014-04-10
期刊：
影响因子：
16
通讯作者：
Hirschey, Matthew D.
中科院分区：
文献类型：
--
作者：
Wagner, Gregory R.;Hirschey, Matthew D.
细胞蛋白质被广泛的乙酰基和其他酰基修饰修饰。许多研究表明乙酰转移酶和脱乙酰酶对位点特异性乙酰化的调节作用。酰化是一种新型的赖氨酸修饰，但对其整体调控作用知之甚少。此外，赖氨酸酰化的机制，它与蛋白质乙酰化的重叠，以及它如何影响细胞功能是该领域的主要未回答的问题。在这篇综述中，我们讨论了已知的乙酰转移酶和脱乙酰酶的作用，和sirtuins作为一个保守的NAD+依赖性蛋白脱酰酶家族，是重要的细胞应激和稳态的反应。我们还考虑了一个新兴的想法，非酶蛋白酰化的证据。最后，我们提出了蛋白质酰化是蛋白质“碳应激”的一种形式的假设，即脱酰酶作为全球蛋白质质量控制网络的一部分进化而去除。
Cellular proteins are decorated with a wide range of acetyl and other acyl modifications. Many studies have demonstrated regulation of site-specific acetylation by acetyltransferases and deacetylases. Acylation is emerging as a new type of lysine modification, but less is known about its overall regulatory role. Furthermore, the mechanisms of lysine acylation, its overlap with protein acetylation, and how it influences cellular function are major unanswered questions in the field. In this review, we discuss the known roles of acetyltransferases and deacetylases, and the sirtuins as a conserved family of NAD+-dependent protein deacylases that are important for response to cellular stress and homeostasis. We also consider the evidence for an emerging idea of non-enzymatic protein acylation. Finally, we put forward the hypothesis that protein acylation is a form of protein “carbon stress”, that the deacylases evolved to remove as a part of a global protein quality control network.
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影响因子：
56.9
作者：
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通讯作者：
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影响因子：
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DOI：
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发表时间：
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影响因子：
3.1
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影响因子：
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通讯作者：
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