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Human receptor for activated protein kinase C1 associates with polyglutamine aggregates and modulates polyglutamine toxicity.

Abstract：

:Formation of SDS-insoluble protein aggregates in affected neurons is a cellular pathological feature of polyglutamine (polyQ) disease. We identified a multi-WD-domain protein, receptor for activated protein kinase C1 (RACK1), as a novel polyQ aggregate component from a Drosophila transgenic polyQ disease model. We showed that WD domains were crucial determinants for the recruitment of RACK1 to polyQ aggregates. Over-expression of the human RACK1 protein suppressed polyQ-induced neurodegeneration in vivo. This is the first report to demonstrate the involvement of WD-domain proteins in polyQ pathogenesis, and the proteomic approach described here can be applied to the investigation of other protein aggregation disorders including Alzheimer's and Parkinson's diseases.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Lam W,Chan WM,Lo TW,Wong AKY,Wu CC,Chan HYE

doi

10.1016/j.bbrc.2008.10.057

subject

Has Abstract

pub_date

2008-12-12 00:00:00

pages

714-719

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(08)02024-X

journal_volume

377

pub_type

杂志文章

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