背根神经节神经元轴突生长锥中核糖体蛋白的动态及其与肌动蛋白丝和局部翻译的关联

IF 3.7 3区 医学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Neurochemical Research Pub Date : 2024-07-08 DOI:10.1007/s11064-024-04195-9
Osamu Hoshi, Nobuyuki Takei
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引用次数: 0

摘要

生长锥中的局部翻译在对轴突导向线索等细胞外刺激的反应中起着至关重要的作用。我们以前的研究表明,脑源性神经营养因子通过激活背根神经节神经元生长锥中的哺乳动物雷帕霉素复合体 1 信号靶激活翻译并增强新蛋白合成。在这项研究中,我们重点研究了 40S 核糖体蛋白 S6 (RPS6)、60S 核糖体蛋白 P0/1/2 (RPP0/1/2) 和肌动蛋白丝,以确定核糖体蛋白的定位如何随着神经营养素诱导的整体蛋白质合成而发生变化。我们利用免疫细胞化学和超分辨率显微镜进行的定量分析表明,在没有刺激的情况下,RPS6、RPP0/1/2 和肌动蛋白倾向于共定位,而当局部蛋白质合成增强时,这些核糖体蛋白倾向于与肌动蛋白分离并相互结合。我们认为这是因为刺激会导致核糖体亚基相互结合,形成活跃翻译的核糖体(多聚体)。这项研究进一步阐明了细胞骨架成分在生长锥局部翻译中的作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

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Ribosomal Protein Dynamics and Its Association with Actin Filaments and Local Translation in Axonal Growth Cones of Dorsal Root Ganglia Neurons

Local translation in growth cones plays a critical role in responses to extracellular stimuli, such as axon guidance cues. We previously showed that brain-derived neurotrophic factor activates translation and enhances novel protein synthesis through the activation of mammalian target of rapamycin complex 1 signaling in growth cones of dorsal root ganglion neurons. In this study, we focused on 40S ribosomal protein S6 (RPS6), 60S ribosomal protein P0/1/2 (RPP0/1/2), and actin filaments to determine how localization of ribosomal proteins changes with overall protein synthesis induced by neurotrophins. Our quantitative analysis using immunocytochemistry and super-resolution microscopy indicated that RPS6, RPP0/1/2, and actin tend to colocalize in the absence of stimulation, and that these ribosomal proteins tend to dissociate from actin and associate with each other when local protein synthesis is enhanced. We propose that this is because stimulation causes ribosomal subunits to associate with each other to form actively translating ribosomes (polysomes). This study further clarifies the role of cytoskeletal components in local translation in growth cones.

Graphical Abstract

Schematic representation of ribosomal protein localization in the the growth cone. a Ribosomal proteins RPS6 and RP0/1/2 are associated with actin in the absence of stimulation. b Upon stimulation by neurotrophins, these two subunit proteins dissociate from actin and bind to each other to form the 80S ribosome initiation complex

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来源期刊
Neurochemical Research
Neurochemical Research 医学-神经科学
CiteScore
7.70
自引率
2.30%
发文量
320
审稿时长
6 months
期刊介绍: Neurochemical Research is devoted to the rapid publication of studies that use neurochemical methodology in research on nervous system structure and function. The journal publishes original reports of experimental and clinical research results, perceptive reviews of significant problem areas in the neurosciences, brief comments of a methodological or interpretive nature, and research summaries conducted by leading scientists whose works are not readily available in English.
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