Ectromelia virus BTB/kelch proteins, EVM150 and EVM167, interact with cullin-3-based ubiquitin ligases

Brianne A. Wilton, Stephanie Campbell, Nicholas Van Buuren, Robyn Garneau, Manabu Furukawa, Yue Xiong, Michele Barry

Research output: Contribution to journalArticle

32 Scopus citations

Abstract

Cellular proteins containing BTB and kelch domains have been shown to function as adapters for the recruitment of substrates to cullin-3-based ubiquitin ligases. Poxviruses are the only family of viruses known to encode multiple BTB/kelch proteins, suggesting that poxviruses may modulate the ubiquitin pathway through interaction with cullin-3. Ectromelia virus encodes four BTB/kelch proteins and one BTB-only protein. Here we demonstrate that two of the ectromelia virus-encoded BTB/kelch proteins, EVM150 and EVM167, interacted with cullin-3. Similar to cellular BTB proteins, the BTB domain of EVM150 and EVM167 was necessary and sufficient for cullin-3 interaction. During infection, EVM150 and EVM167 localized to discrete cytoplasmic regions, which co-localized with cullin-3. Furthermore, EVM150 and EVM167 co-localized and interacted with conjugated ubiquitin, as demonstrated by confocal microscopy and co-immunoprecipitation. Our findings suggest that the ectromelia virus-encoded BTB/kelch proteins, EVM150 and EVM167, interact with cullin-3 potentially functioning to recruit unidentified substrates for ubiquitination.

Original languageEnglish (US)
Pages (from-to)82-99
Number of pages18
JournalVirology
Volume374
Issue number1
DOIs
StatePublished - Apr 25 2008

Keywords

  • BTB/kelch
  • Cullin-3
  • Ectromelia
  • Poxvirus
  • Ubiquitination

ASJC Scopus subject areas

  • Virology

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    Wilton, B. A., Campbell, S., Van Buuren, N., Garneau, R., Furukawa, M., Xiong, Y., & Barry, M. (2008). Ectromelia virus BTB/kelch proteins, EVM150 and EVM167, interact with cullin-3-based ubiquitin ligases. Virology, 374(1), 82-99. https://doi.org/10.1016/j.virol.2007.11.036