|
|||||
|
|
Human receptor for activated protein kinase C1 associates with polyglutamine aggregates and modulates polyglutamine toxicity |
|
| Authors: | Lam Wun Chan Wing Man Lo Tsz Wai Wong Azaria Kam Yan Wu Chi Chung Chan Ho Yin Edwin |
| Institution: | a Laboratory of Drosophila Research, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR, China b Molecular Biotechnology Programme, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR, China c Department of Biochemistry (Science), The Chinese University of Hong Kong, Laboratory of Drosophila Research, Molecular Biotechnology Programme, Room 509B, Mong Man Wai Building, Shatin, N.T., Hong Kong SAR, China |
| 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. |
| Keywords: | Drosophila Machado Joseph Disease RACK1 WD domain |
| 本文献已被 ScienceDirect PubMed 等数据库收录！ | |