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2010-08-11Zeitschriftenartikel DOI: 10.1099/vir.0.024638-0
Mumps virus small hydrophobic protein targets ataxin-1 ubiquitin-like interacting protein (ubiquilin 4)
Woznik, Maria
Rödner, Claudia
Lemon, Ken
Rima, Bert
Mankertz, Annette
Finsterbusch, Tim
The small hydrophobic (SH) protein of mumps virus has been reported to interfere with innate immunity by inhibiting tumour necrosis factor alpha-mediated apoptosis. In a yeast two-hybrid screen we have identified the ataxin-1 ubiquitin-like interacting protein (A1Up) as a cellular target of the SH protein. A1Up contains an amino-terminal ubiquitin-like (UbL) domain, a carboxyterminal ubiquitin-associated (UbA) domain and two stress-inducible heat shock chaperoninbinding (Sti1) motifs. This places it within the ubiquitin-like protein family that is involved in proteasome-mediated activities. Co-immunoprecipitation confirmed the binding of SH and A1Up and demonstrates that a truncated protein fragment corresponding to aa 136–270 of A1Up, which represents the first Sti1-like repeat and an adjacent hydrophobic region, was sufficient for interaction, whereas neither the UbL nor the UbA domains were required for interaction. The ectopic expression of A1Up leads to a redistribution of SH to punctate structures that co-localize with the 20S proteasome in transfected or infected mammalian cells.
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DOI
10.1099/vir.0.024638-0
Permanent URL
https://doi.org/10.1099/vir.0.024638-0
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<a href="https://doi.org/10.1099/vir.0.024638-0">https://doi.org/10.1099/vir.0.024638-0</a>