Synaptic Function Section, National Institute of Neurological Disorders and Stroke, National Institutes of Health, 35 Convent Drive, Bethesda, MD 20892-3706, USA.
Biosci Rep. 2011 Apr;31(2):151-8. doi: 10.1042/BSR20100110.
The autophagy-lysosomal pathway is an intracellular degradation process essential for maintaining neuronal homoeostasis. Defects in this pathway have been directly linked to a growing number of neurodegenerative disorders. We recently revealed that Snapin plays a critical role in co-ordinating dynein-driven retrograde transport and late endosomal-lysosomal trafficking, thus maintaining efficient autophagy-lysosomal function. Deleting snapin in neurons impairs lysosomal proteolysis and reduces the clearance of autolysosomes. The role of the autophagy-lysosomal system in neuronal development is, however, largely uncharacterized. Here, we report that snapin deficiency leads to developmental defects in the central nervous system. Embryonic snapin-/- mouse brain showed reduced cortical plates and intermediate zone cell density, increased apoptotic death in the cortex and third ventricle, enhanced membrane-bound LC3-II staining associated with autophagic vacuoles and an accumulation of polyubiquitinated proteins in the cortex and hippocampus. Thus our results provide in vivo evidence for the essential role of late endocytic transport and autophagy-lysosomal function in maintaining neuronal survival and development of the mammalian central nervous system. In addition, our study supports the existence of a functional interplay between the autophagy-lysosome and ubiquitin-proteasome systems in the protein quality-control process.
自噬溶酶体途径是一种细胞内降解过程,对维持神经元内稳态至关重要。该途径的缺陷与越来越多的神经退行性疾病直接相关。我们最近发现 Snapin 在协调动力蛋白驱动的逆行运输和晚期内体溶酶体运输方面起着关键作用,从而维持有效的自噬溶酶体功能。在神经元中删除 snapin 会损害溶酶体蛋白水解,并减少自噬溶酶体的清除。然而,自噬溶酶体系统在神经元发育中的作用在很大程度上尚未得到表征。在这里,我们报告 snapin 缺陷导致中枢神经系统发育缺陷。胚胎 snapin-/- 小鼠大脑显示皮质板和中间区细胞密度降低,皮质和第三脑室中的细胞凋亡死亡增加,与自噬小体相关的膜结合 LC3-II 染色增强,以及皮质和海马体中多聚泛素化蛋白的积累。因此,我们的研究结果为晚期内吞运输和自噬溶酶体功能在维持哺乳动物中枢神经系统神经元存活和发育中的重要作用提供了体内证据。此外,我们的研究支持自噬溶酶体和泛素-蛋白酶体系统在蛋白质质量控制过程中存在功能相互作用。