Caspase-1 clipping causes complications for α-synuclein
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چکیده
منابع مشابه
Caspase-1 causes truncation and aggregation of the Parkinson's disease-associated protein α-synuclein.
The aggregation of α-synuclein (aSyn) leading to the formation of Lewy bodies is the defining pathological hallmark of Parkinson's disease (PD). Rare familial PD-associated mutations in aSyn render it aggregation-prone; however, PD patients carrying wild type (WT) aSyn also have aggregated aSyn in Lewy bodies. The mechanisms by which WT aSyn aggregates are unclear. Here, we report that inflamma...
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Parkinson's disease (PD) is a neurodegenerative disorder characterized by the selective loss of dopaminergic neurons and the presence of Lewy bodies. Many recent studies focused on the interaction between α-synuclein (α-syn) and dopamine in the pathogenesis of PD, and fluorescent anisotropy suggested that the C-terminal region of α-syn may be a target for modification by dopamine. However, it i...
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Early infantile epileptic encephalopathy (EIEE)-associated mutations in MUNC18-1 cause Munc18-1 misfolding and cellular aggregation. In this issue, Chai et al. (2016. J. Cell Biol http://dx.doi.org/10.1083/jcb.201512016) find that Munc18-1 is a molecular chaperone for α-synuclein and that aggregated Munc18-1 EIEE-causing mutants promote α-synuclein aggregation.
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641 The Rockefeller University Press $30.00 J. Cell Biol. Vol. 214 No. 6 641–643 www.jcb.org/cgi/doi/10.1083/jcb.201608060 Early infantile epileptic encephalopathy (EIEE), also known as Ohtahara syndrome, is a debilitating neurological disorder that results in early-onset tonic seizures and severe intellectual disability. Heterozygous mutations in MUNC18-1 (also known as syntaxin binding protei...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2016
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.1610993113