Journal
NEURODEGENERATIVE DISEASES
Volume 13, Issue 2-3, Pages 110-113Publisher
KARGER
DOI: 10.1159/000355654
Keywords
Autophagy; Parkinson's disease; Heat shock protein; Mitochondria; Endoplasmic reticulum; Stress
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Funding
- NIEHS NIH HHS [R01 ES020395] Funding Source: Medline
- NIH HHS [P40 OD010440] Funding Source: Medline
- NINDS NIH HHS [NS06082, R01 NS060872] Funding Source: Medline
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Background: Mutations in LRRK2 (leucine-rich repeat kinase 2) are a common cause of familial Parkinson's disease. However, the mechanisms through which LRRK2 mutations contribute to neurodegeneration are poorly understood. Objective:We investigated the effects of WT, G2019S (GS), R1441C (RC) and kinase dead LRRK2 across multiple different cellular compartments in order to gain insight into the breadth of LRRK2 effects on cellular function. Methods: Nematodes expressing lgg-1::RFP, hsp1::GFP, hsp4::GFP and hsp6::GFP were crossed to nematode lines expressing WT, GS, RC or kinase dead LRRK2. Results: We observed that GS and RC LRRK2 inhibited autophagy, while WT, GS and RC LRRK2 increased the response of the mitochondrial hsp6 reporter to stress. The response of the hsp reporters under basal conditions was more nuanced. Conclusion: These results support a putative role of LRRK2 in the autophagic and mitochondrial systems. (C) 2013 S. Karger AG, Basel
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