Suppr超能文献

剪接体完整性在运动神经元疾病 ALS 和 SMA 中存在缺陷。

Spliceosome integrity is defective in the motor neuron diseases ALS and SMA.

机构信息

Laboratory for Motor Neuron Disease, RIKEN Brain Science Institute, Wako, Saitama, Japan.

出版信息

EMBO Mol Med. 2013 Feb;5(2):221-34. doi: 10.1002/emmm.201202303. Epub 2013 Jan 25.

Abstract

Two motor neuron diseases, amyotrophic lateral sclerosis (ALS) and spinal muscular atrophy (SMA), are caused by distinct genes involved in RNA metabolism, TDP-43 and FUS/TLS, and SMN, respectively. However, whether there is a shared defective mechanism in RNA metabolism common to these two diseases remains unclear. Here, we show that TDP-43 and FUS/TLS localize in nuclear Gems through an association with SMN, and that all three proteins function in spliceosome maintenance. We also show that in ALS, Gems are lost, U snRNA levels are up-regulated and spliceosomal U snRNPs abnormally and extensively accumulate in motor neuron nuclei, but not in the temporal lobe of FTLD with TDP-43 pathology. This aberrant accumulation of U snRNAs in ALS motor neurons is in direct contrast to SMA motor neurons, which show reduced amounts of U snRNAs, while both have defects in the spliceosome. These findings indicate that a profound loss of spliceosome integrity is a critical mechanism common to neurodegeneration in ALS and SMA, and may explain cell-type specific vulnerability of motor neurons.

摘要

两种运动神经元疾病,肌萎缩性侧索硬化症(ALS)和脊髓性肌萎缩症(SMA),分别由涉及 RNA 代谢的不同基因,即 TDP-43 和 FUS/TLS,以及 SMN 引起。然而,这两种疾病的 RNA 代谢是否存在共同的缺陷机制尚不清楚。在这里,我们表明 TDP-43 和 FUS/TLS 通过与 SMN 结合定位于核 Gems 中,并且这三种蛋白质都在剪接体维持中发挥作用。我们还表明,在 ALS 中,Gems 丢失,U snRNA 水平上调,剪接体 U snRNPs 异常且广泛地在运动神经元核中积累,但不在 FTLD 伴 TDP-43 病理的颞叶中积累。在 ALS 运动神经元中,U snRNAs 的这种异常积累与 SMA 运动神经元形成鲜明对比,后者显示 U snRNAs 减少,而两者的剪接体都有缺陷。这些发现表明,剪接体完整性的严重丧失是 ALS 和 SMA 神经退行性变的共同关键机制,并可能解释运动神经元的细胞类型特异性易感性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c83a/3569639/00b65733bd08/emmm0005-0221-f1.jpg

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验