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VCP recruitment to mitochondria causes mitophagy impairment and neurodegeneration in models of Huntington's disease.

Abstract：

:Mutant Huntingtin (mtHtt) causes neurodegeneration in Huntington's disease (HD) by evoking defects in the mitochondria, but the underlying mechanisms remains elusive. Our proteomic analysis identifies valosin-containing protein (VCP) as an mtHtt-binding protein on the mitochondria. Here we show that VCP is selectively translocated to the mitochondria, where it is bound to mtHtt in various HD models. Mitochondria-accumulated VCP elicits excessive mitophagy, causing neuronal cell death. Blocking mtHtt/VCP mitochondrial interaction with a peptide, HV-3, abolishes VCP translocation to the mitochondria, corrects excessive mitophagy and reduces cell death in HD mouse- and patient-derived cells and HD transgenic mouse brains. Treatment with HV-3 reduces behavioural and neuropathological phenotypes of HD in both fragment- and full-length mtHtt transgenic mice. Our findings demonstrate a causal role of mtHtt-induced VCP mitochondrial accumulation in HD pathogenesis and suggest that the peptide HV-3 might be a useful tool for developing new therapeutics to treat HD.

journal_name

Nat Commun

journal_title

Nature communications

authors

Guo X,Sun X,Hu D,Wang YJ,Fujioka H,Vyas R,Chakrapani S,Joshi AU,Luo Y,Mochly-Rosen D,Qi X

doi

10.1038/ncomms12646

subject

Has Abstract

pub_date

2016-08-26 00:00:00

pages

12646

issn

2041-1723

pii

ncomms12646

journal_volume

7

pub_type

杂志文章

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