School of Biochemistry, Medical Research Council Centre for Synaptic Plasticity, Medical Sciences Building, University of Bristol, University Walk, Bristol, BS8 1TD, UK.
Biomolecules. 2012 May 14;2(2):256-68. doi: 10.3390/biom2020256.
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.
蛋白质的翻译后修饰对于细胞功能至关重要。SUMO（小泛素样修饰物）的共价修饰在多种细胞过程中发挥作用，包括转录调控、DNA 损伤修复、蛋白质定位和运输。影响蛋白质定位和运输的因素在神经元中尤为重要，因为神经元具有极化、形态复杂性和功能专业化。SUMOylation 已成为参与生物钟、细胞凋亡和蛋白质降解等关键途径的蛋白质在核内和核质间易位的主要介质。此外，需要 SUMO 调节的核外蛋白质的重新定位来维持神经元的兴奋性和突触传递。因此，SUMOylation 是神经元活力和功能的关键仲裁者。在这里，我们概述了我们对 SUMO 调节神经元蛋白质定位和易位的理解的最新进展，并强调了正在进行的令人兴奋的研究领域。
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