溶酶体
细胞生物学
胞吐
自噬
内体
细胞外
生物
ATG16L1
蛋白质稳态
灯1
内吞作用
脂质双层融合
细胞内
化学
生物化学
膜
受体
细胞凋亡
酶
作者
Katarzyna M. Grochowska,Marit Sperveslage,Rajeev Raman,Antonio Virgilio Failla,Dawid Głów,Christian Schulze,Laura Laprell,Boris Fehse,Michael R. Kreutz
出处
期刊:Cell Reports
[Elsevier]
日期:2023-08-01
卷期号:42 (8): 112998-112998
被引量:4
标识
DOI:10.1016/j.celrep.2023.112998
摘要
The complex morphology of neurons poses a challenge for proteostasis because the majority of lysosomal degradation machinery is present in the cell soma. In recent years, however, mature lysosomes were identified in dendrites, and a fraction of those appear to fuse with the plasma membrane and release their content to the extracellular space. Here, we report that dendritic lysosomes are heterogeneous in their composition and that only those containing lysosome-associated membrane protein (LAMP) 2A and 2B fuse with the membrane and exhibit activity-dependent motility. Exocytotic lysosomes dock in close proximity to GluN2B-containing N-methyl-D-aspartate-receptors (NMDAR) via an association of LAMP2B to the membrane-associated guanylate kinase family member SAP102/Dlg3. NMDAR-activation decreases lysosome motility and promotes membrane fusion. We find that chaperone-mediated autophagy is a supplier of content that is released to the extracellular space via lysosome exocytosis. This mechanism enables local disposal of aggregation-prone proteins like TDP-43 and huntingtin.
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