Metabolism leaves its mark on the powerhouse: recent progress in post-translational modifications of lysine in mitochondria.
Metabolism leaves its mark on the powerhouse: recent progress in post-translational modifications of lysine in mitochondria.
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DOI：
10.3389/fphys.2014.00301
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发表时间：
2014
影响因子：
4
通讯作者：
Foster DB
中科院分区：
文献类型：
--
作者：
Papanicolaou KN;O'Rourke B;Foster DB
赖氨酸修饰在细胞核中被广泛研究，它们在基因调控中起着关键作用，是表观遗传学的支柱之一。在细胞质中，它们对蛋白质的稳定至关重要。然而，在过去的十年中，我们也见证了线粒体作为赖氨酸翻译后修饰（PTM）的主要位点的出现，这在很大程度上要归功于不断发展的蛋白质组学技术。在这里，我们回顾了最近关于赖氨酸残基与代谢硫酯辅酶A中间体直接反应产生的PTM的研究进展，包括乙酰化、琥珀酰化、丙二醛化和戊二酰化。我们强调进化守恒，动力学，化学计量学，以及这一新兴家族成员之间的串扰。我们研究了线粒体sirtuins对靶蛋白功能和调控的影响。最后，我们关注心脏和心脏线粒体的工作，并考虑乙酰化和其他新发现的修饰可能在心脏病中发挥的作用。
Lysine modifications have been studied extensively in the nucleus, where they play pivotal roles in gene regulation and constitute one of the pillars of epigenetics. In the cytoplasm, they are critical to proteostasis. However, in the last decade we have also witnessed the emergence of mitochondria as a prime locus for post-translational modification (PTM) of lysine thanks, in large measure, to evolving proteomic techniques. Here, we review recent work on evolving set of PTM that arise from the direct reaction of lysine residues with energized metabolic thioester-coenzyme A intermediates, including acetylation, succinylation, malonylation, and glutarylation. We highlight the evolutionary conservation, kinetics, stoichiometry, and cross-talk between members of this emerging family of PTMs. We examine the impact on target protein function and regulation by mitochondrial sirtuins. Finally, we spotlight work in the heart and cardiac mitochondria, and consider the roles acetylation and other newly-found modifications may play in heart disease.
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影响因子：
56.9
作者：
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通讯作者：
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