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  • Title: Structural basis for recognition of the third SH3 domain of full-length R85 (R85FL)/ponsin by ataxin-7.
    Author: Jiang YJ, Zhou CJ, Zhou ZR, Wu M, Hu HY.
    Journal: FEBS Lett; 2013 Sep 17; 587(18):2905-11. PubMed ID: 23892081.
    Abstract:
    Ataxin-7 (Atx7) is a component of the nuclear transcription co-activator complex; its polyglutamine (polyQ) expansion may cause nuclear accumulation and recruit numerous proteins to the intranuclear inclusion bodies. Full-length R85 (R85FL) is such a protein sequestered by polyQ-expanded Atx7. Here, we report that Atx7 specifically interacts with the third SH3 domain (SH3C) of R85FL through its second portion of proline-rich region (PRR). NMR structural analysis of the SH3C domain and its complex with PRR revealed that SH3C contains a large negatively charged surface for binding with the RRTR motif of Atx7. Microscopy imaging demonstrated that sequestration of R85FL by the polyQ-expanded Atx7 in cell is mediated by this specific SH3C-PRR interaction, which is implicated in the pathogenesis of spinocerebellar ataxia 7.
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