Journal
JOURNAL OF NEUROCHEMISTRY
Volume 94, Issue 4, Pages 1040-1053Publisher
WILEY
DOI: 10.1111/j.1471-4159.2005.03257.x
Keywords
CDCrel-1; cell death; parkin; Parkinson's disease; Septin 5
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Funding
- NIEHS NIH HHS [ES 012337] Funding Source: Medline
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Septin 5, a parkin substrate, is a vesicle- and membrane-associated protein that plays a significant role in inhibiting exocytosis. The regulatory function of Septin 5 in dopaminergic (DAergic) neurons of substantia nigra (SN), maintained at relatively low levels, has not yet been delineated. As loss of function mutations of parkin are the principal cause of a familial Parkinson's disease, a prevailing hypothesis is that the loss of parkin activity results in accumulation of Septin 5 which confers neuron-specific toxicity in SN-DAergic neurons. In vitro and in vivo models were used to support this hypothesis. In our well-characterized DAergic SN4741 cell model, acute accumulation of elevated levels of Septin 5, but not synphilin-1 ( another parkin substrate), resulted in cytotoxic cell death that was markedly reduced by parkin co-transfection. A transgenic
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