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Title 

Co-chaperone CHIP promotes aggregation of ataxin-1

Authors 

Jung Young ChoiJ H RyuH S KimSung Goo ParkKwang-Hee BaeSunghyun KangP K MyungS ChoByoung Chul ParkDo Hee Lee

Publisher 

Elsevier

Issue Date 

2007

Citation 

Molecular and Cellular Neuroscience, vol. 34, no. 1, pp. 69-79

Keywords 

aggregationataxin-1CHIPNeurodegenerationpolyglutamineubiquitinataxin 1ataxin 3BAG 1 proteinchaperone

Abstract 

Recent studies demonstrated that co-chaperone/E3 ligase CHIP (C-terminus of hsp70-interacting protein) mediates the ubiquitylation and suppresses the aggregation of polyglutamine (polyQ) proteins, such as huntingtin or ataxin-3. In this study, we investigated the effects of CHIP on the degradation of another polyQ protein ataxin-1. Interestingly CHIP associates not only with the polyQ-expanded ataxin-1 but also with the normal ataxin-1. Moreover, by enhancing ataxin-1 ubiquitylation, CHIP over-expression leads to a reduction in the solubility of ataxin-1 and thus increases the aggregate formation, especially that of polyQ-expanded ataxin-1. Domain analysis revealed that the TPR domain is required for the promotion of aggregation. By contrast, other co-chaperones or E3 ligases, such as BAG-1 or parkin, did not show similar effects on the aggregation of ataxin-1. Importantly, the effect of CHIP is impaired by the mutation of Ser776 of ataxin-1 whose phosphorylation is crucial for ataxin-1 aggregation. Our findings suggest that the role of CHIP in aggregation of polyQ proteins greatly varies depending on the context of full-length polyQ proteins.

ISSN 

1044-7431

Link 

http://dx.doi.org/10.1016/j.mcn.2006.10.002

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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