Regulation of Neuronal Protein Trafficking and Translocation by SUMOylation.
Regulation of Neuronal Protein Trafficking and Translocation by SUMOylation.
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DOI：
10.3390/biom2020256
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发表时间：
2012-05-14
期刊：
影响因子：
5.5
通讯作者：
Henley JM
中科院分区：
文献类型：
--
作者：
Berndt A;Wilkinson KA;Henley JM
蛋白质的翻译后修饰对于细胞功能是必不可少的。SUMO（small ubiquitin-like modifier，小泛素样修饰物）的共价修饰在转录调控、DNA损伤修复、蛋白质定位和运输等多个细胞过程中发挥作用。影响蛋白质定位和运输的因素在神经元中特别重要，因为它们的极化，形态复杂性和功能特化。SUMO化已经成为参与关键途径如昼夜节律、细胞凋亡和蛋白质降解的蛋白质的核内和核质易位的主要介质。此外，SUMO调节的细胞核蛋白的重新定位是维持神经元兴奋性和突触传递所必需的。因此，SUMO化是神经元活力和功能的关键仲裁者。在这里，我们提供了一个概述，我们了解的神经元蛋白定位和易位的调节SUMO和突出正在进行的研究令人兴奋的领域的最新进展。
Post-translational modifications of proteins are essential for cell function. Covalent modification by SUMO (small ubiquitin-like modifier) plays a role in multiple cell processes, including transcriptional regulation, DNA damage repair, protein localization and trafficking. Factors affecting protein localization and trafficking are particularly crucial in neurons because of their polarization, morphological complexity and functional specialization. SUMOylation has emerged as a major mediator of intranuclear and nucleo-cytoplasmic translocations of proteins involved in critical pathways such as circadian rhythm, apoptosis and protein degradation. In addition, SUMO-regulated re-localization of extranuclear proteins is required to sustain neuronal excitability and synaptic transmission. Thus, SUMOylation is a key arbiter of neuronal viability and function. Here, we provide an overview of recent advances in our understanding of regulation of neuronal protein localization and translocation by SUMO and highlight exciting areas of ongoing research.