Department of Biochemistry and Molecular Medicine, University of California Davis, School of Medicine, One Shields Ave, Davis, CA, USA.
Genome Center, University of California Davis, Davis, California, USA.
Acta Neuropathol Commun. 2019 Sep 3;7(1):143. doi: 10.1186/s40478-019-0796-1.
Fragile X-associated tremor/ataxia syndrome (FXTAS) is a neurodegenerative disorder associated with a premutation repeat expansion (55-200 CGG repeats) in the 5' noncoding region of the FMR1 gene. Solitary intranuclear inclusions within FXTAS neurons and astrocytes constitute a hallmark of the disorder, yet our understanding of how and why these bodies form is limited. Here, we have discovered that FXTAS inclusions emit a distinct autofluorescence spectrum, which forms the basis of a novel, unbiased method for isolating FXTAS inclusions by preparative fluorescence-activated cell sorting (FACS). Using a combination of autofluorescence-based FACS and liquid chromatography/tandem mass spectrometry (LC-MS/MS)-based proteomics, we have identified more than two hundred proteins that are enriched within the inclusions relative to FXTAS whole nuclei. Whereas no single protein species dominates inclusion composition, highly enriched levels of conjugated small ubiquitin-related modifier 2 (SUMO 2) protein and p62/sequestosome-1 (p62/SQSTM1) protein were found within the inclusions. Many additional proteins involved with RNA binding, protein turnover, and DNA damage repair were enriched within inclusions relative to total nuclear protein. The current analysis has also allowed the first direct detection, through peptide sequencing, of endogenous FMRpolyG peptide, the product of repeat-associated non-ATG (RAN) translation of the FMR1 mRNA. However, this peptide was found only at extremely low levels and not within whole FXTAS nuclear preparations, raising the question whether endogenous RAN products exist at quantities sufficient to contribute to FXTAS pathogenesis. The abundance of the inclusion-associated ubiquitin- and SUMO-based modifiers supports a model for inclusion formation as the result of increased protein loads and elevated oxidative stress leading to maladaptive autophagy. These results highlight the need to further investigate FXTAS pathogenesis in the context of endogenous systems.
脆性 X 相关震颤/共济失调综合征(FXTAS)是一种与 FMR1 基因 5'非编码区的前突变重复扩展(55-200 CGG 重复)相关的神经退行性疾病。FXTAS 神经元和星形胶质细胞中的孤立核内包涵体构成该疾病的标志,但我们对这些体如何以及为何形成的理解有限。在这里,我们发现 FXTAS 包涵体发出独特的自发荧光光谱,这为通过制备性荧光激活细胞分选(FACS)分离 FXTAS 包涵体提供了一种新的、无偏的方法。我们使用基于自发荧光的 FACS 和基于液相色谱/串联质谱(LC-MS/MS)的蛋白质组学相结合的方法,已经鉴定出超过 200 种在包涵体中相对于 FXTAS 全核富集的蛋白质。虽然没有单一的蛋白质种类主导包涵体的组成,但在包涵体中发现了高度富集的共轭小泛素相关修饰物 2(SUMO 2)蛋白和 p62/自噬体-1(p62/SQSTM1)蛋白。与总核蛋白相比,许多参与 RNA 结合、蛋白质周转和 DNA 损伤修复的额外蛋白质也在包涵体中富集。当前的分析还通过肽测序首次直接检测到内源性 FMRpolyG 肽,即 FMR1 mRNA 重复相关非 ATG(RAN)翻译的产物。然而,这种肽仅以极低的水平存在,并且不在整个 FXTAS 核制剂中,这引发了一个问题,即内源性 RAN 产物是否以足以导致 FXTAS 发病机制的数量存在。包涵体相关泛素和 SUMO 修饰物的丰度支持包涵体形成的模型,即由于蛋白质负荷增加和氧化应激升高导致适应性自噬。这些结果强调需要在内源性系统的背景下进一步研究 FXTAS 的发病机制。