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.

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

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