期刊
HUMAN MOLECULAR GENETICS
卷 23, 期 25, 页码 6732-6745出版社
OXFORD UNIV PRESS
DOI: 10.1093/hmg/ddu391
关键词
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资金
- Fundacao para a Ciencia e Tecnologia, Portugal [SFRH/BD/44446/2008]
- EMBO Installation Grant
- Marie Curie International Reintegration Grant (Neurofold)
- DFG Center for Nanoscale Microscopy and Molecular Physiology of the Brain
- Parkinson's UK [G-1203]
- Fundação para a Ciência e a Tecnologia [SFRH/BD/44446/2008] Funding Source: FCT
- Parkinson's UK [G-1203] Funding Source: researchfish
Alpha-synuclein (aSyn) misfolding and aggregation are pathological features common to several neurodegenerative diseases, including Parkinson's disease (PD). Mounting evidence suggests that aSyn can be secreted and transferred from cell to cell, participating in the propagation and spreading of pathological events. Rab11, a small GTPase, is an important regulator in both endocytic and secretory pathways. Here, we show that Rab11 is involved in regulating aSyn secretion. Rab11 knockdown or overexpression of either Rab11a wild-type (Rab11a WT) or Rab11a GDP-bound mutant (Rab11a S25N) increased secretion of aSyn. Furthermore, we demonstrate that Rab11 interacts with aSyn and is present in intracellular inclusions together with aSyn. Moreover, Rab11 reduces aSyn aggregation and toxicity. Our results suggest that Rab11 is involved in modulating the processes of aSyn secretion and aggregation, both of which are important mechanisms in the progression of aSyn pathology in PD and other synucleinopathies.
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