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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Deubiquitinating function of ataxin-3: insights from the solution structure of the Josephin domain.

Spinocerebellar ataxia type 3 is a human neurodegenerative disease resulting from polyglutamine tract expansion. The affected protein, ataxin-3, which contains an N-terminal Josephin domain followed by tandem ubiquitin (Ub)-interacting motifs (UIMs) and a polyglutamine stretch, has been implicated in the function of the Ub proteasome system. NMR-based structural analysis has now revealed that the Josephin domain binds Ub and has a papain-like fold that is reminiscent of that of other deubiquitinases, despite primary sequence divergence but consistent with its deubiqutinating activity. Mutation of the catalytic Cys enhances the stability of a complex between ataxin-3 and polyubiquitinated proteins. This effect depends on the integrity of the UIM region, suggesting that the UIMs are bound to the substrate polyubiquitin during catalysis. We propose that ataxin-3 functions as a polyubiquitin chain-editing enzyme.[1]

References

  1. Deubiquitinating function of ataxin-3: insights from the solution structure of the Josephin domain. Mao, Y., Senic-Matuglia, F., Di Fiore, P.P., Polo, S., Hodsdon, M.E., De Camilli, P. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
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