The BAG2 and BAG5 proteins inhibit the ubiquitination of pathogenic ataxin3-80Q.

Research paper by Xiang-Qian XQ Che, Bei-Sha BS Tang, Hong-Feng HF Wang, Xin-Xiang XX Yan, Hong H Jiang, Lu L Shen, Qian Q Xu, Guang-Hui GH Wang, Hai-Nan HN Zhang, Chun-Yu CY Wang, Ji-Feng JF Guo

Indexed on: 10 Jul '14Published on: 10 Jul '14Published in: The International journal of neuroscience


The expansion of a polyglutamine domain in the protein ataxin3 causes spinocerebellar ataxia type-3 (SCA3). However, there is little information to date about the upstream proteins in the ubiquitin-proteasome system of pathogenic ataxin3-80Q. Here, we report that BAG2 (Bcl-2 associated athanogene family protein 2) and BAG5 (Bcl-2-associated athanogene family protein 5) stabilise pathogenic ataxin3-80Q by inhibiting its ubiquitination as determined based on western blotting and co-immunofluorescence experiments. The association of the BAG2 and BAG5 proteins with pathogenic ataxin3-80Q strengthens the important roles of the BAG family in neurodegenerative diseases.