Institute of Neuropathology, RWTH Aachen University Medical School, Pauwelsstr. 30, 52074, Aachen, Germany.
EURON - European Graduate School of Neuroscience, Maastricht, The Netherlands.
Cell Death Dis. 2021 May 10;12(5):466. doi: 10.1038/s41419-021-03710-y.
Mutations in RNA binding proteins (RBPs) and in genes regulating autophagy are frequent causes of familial amyotrophic lateral sclerosis (fALS). The P56S mutation in vesicle-associated membrane protein-associated protein B (VAPB) leads to fALS (ALS8) and spinal muscular atrophy (SMA). While VAPB is primarily involved in the unfolded protein response (UPR), vesicular trafficking and in initial steps of the autophagy pathway, the effect of mutant P56S-VAPB on autophagy regulation in connection with RBP homeostasis has not been explored yet. Examining the muscle biopsy of our index ALS8 patient of European origin revealed globular accumulations of VAPB aggregates co-localised with autophagy markers LC3 and p62 in partially atrophic and atrophic muscle fibres. In line with this skin fibroblasts obtained from the same patient showed accumulation of P56S-VAPB aggregates together with LC3 and p62. Detailed investigations of autophagic flux in cell culture models revealed that P56S-VAPB alters both initial and late steps of the autophagy pathway. Accordingly, electron microscopy complemented with live cell imaging highlighted the impaired fusion of accumulated autophagosomes with lysosomes in cells expressing P56S-VAPB. Consistent with these observations, neuropathological studies of brain and spinal cord of P56S-VAPB transgenic mice revealed signs of neurodegeneration associated with altered protein quality control and defective autophagy. Autophagy and RBP homeostasis are interdependent, as demonstrated by the cytoplasmic mis-localisation of several RBPs including pTDP-43, FUS, Matrin 3 which often sequestered with P56S-VAPB aggregates both in cell culture and in the muscle biopsy of the ALS8 patient. Further confirming the notion that aggregation of the RBPs proceeds through the stress granule (SG) pathway, we found persistent G3BP- and TIAR1-positive SGs in P56S-VAPB expressing cells as well as in the ALS8 patient muscle biopsy. We conclude that P56S-VAPB-ALS8 involves a cohesive pathomechanism of aberrant RBP homeostasis together with dysfunctional autophagy.
RNA 结合蛋白 (RBPs) 和自噬调节基因的突变是家族性肌萎缩侧索硬化症 (fALS) 的常见原因。囊泡相关膜蛋白结合蛋白 B (VAPB) 的 P56S 突变导致 fALS (ALS8) 和脊髓性肌萎缩症 (SMA)。虽然 VAPB 主要参与未折叠蛋白反应 (UPR)、囊泡运输以及自噬途径的初始步骤,但突变型 P56S-VAPB 对与 RBP 动态平衡相关的自噬调节的影响尚未得到探索。对我们的欧洲起源的指数 ALS8 患者的肌肉活检显示,VAPB 聚集体的球状聚集物与自噬标记物 LC3 和 p62 在部分萎缩和萎缩的肌肉纤维中共同定位。与此一致的是,从同一患者获得的皮肤成纤维细胞显示 P56S-VAPB 聚集体与 LC3 和 p62 一起积累。在细胞培养模型中对自噬通量的详细研究表明,P56S-VAPB 改变了自噬途径的初始和晚期步骤。因此,电子显微镜结合活细胞成像突出了表达 P56S-VAPB 的细胞中积累的自噬体与溶酶体融合受损。与这些观察结果一致,P56S-VAPB 转基因小鼠的大脑和脊髓神经病理学研究显示与蛋白质质量控制改变和自噬缺陷相关的神经退行性变迹象。自噬和 RBP 动态平衡是相互依赖的,这一点可以通过包括 pTDP-43、FUS 和 Matrin 3 在内的几种 RBPs 的细胞质定位异常来证明,这些 RBPs 通常与 P56S-VAPB 聚集体一起在细胞培养和 ALS8 患者的肌肉活检中被隔离。进一步证实了 RBPs 聚集通过应激颗粒 (SG) 途径进行的观点,我们发现在表达 P56S-VAPB 的细胞以及 ALS8 患者的肌肉活检中存在持续的 G3BP- 和 TIAR1-阳性 SG。我们得出的结论是,P56S-VAPB-ALS8 涉及异常 RBP 动态平衡与功能失调的自噬之间的凝聚病理机制。