ArticleVirology2008
Ectromelia virus BTB/kelch proteins, EVM150 and EVM167, interact with cullin-3-based ubiquitin ligases.
Article in Virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
26 citing papers in PubMed, 43 citations in OpenAlex.
- Review
- Vaccinia virus BTB-Kelch proteins C2 and F3 inhibit NF-κB activation.The Journal of general virology · 2022Article
- An E3 Ubiquitin Ligase Scaffolding Protein Is Proviral during Chikungunya Virus Infection in Aedes aegypti.Microbiology spectrum · 2022Article
- Poxvirus Interactions with the Host Ubiquitin System.Pathogens (Basel, Switzerland) · 2021Review
- Article
- Progress on Poxvirus E3 Ubiquitin Ligases and Adaptor Proteins.Frontiers in immunology · 2021Review
- Molecular basis of cullin-3 (Cul3) ubiquitin ligase subversion by vaccinia virus protein A55.The Journal of biological chemistry · 2019Article
- Identification of Poxvirus Genome Uncoating and DNA Replication Factors with Mutually Redundant Roles.Journal of virology · 2018Article
- Pathogenicity-associated protein domains: The fiercely-conserved evolutionary signatures.Gene reports · 2017Review
- Comparative Proteomics Reveals Strain-Specific β-TrCP Degradation via Rotavirus NSP1 Hijacking a Host Cullin-3-Rbx1 Complex.PLoS pathogens · 2016Article
- Rotavirus NSP1 Associates with Components of the Cullin RING Ligase Family of E3 Ubiquitin Ligases.Journal of virology · 2016Article
- Cullin E3 ligases and their rewiring by viral factors.Biomolecules · 2014Review
- Vaccinia virus virulence factor N1 can be ubiquitylated on multiple lysine residues.The Journal of general virology · 2014Article
- EVM005: an ectromelia-encoded protein with dual roles in NF-κB inhibition and virulence.PLoS pathogens · 2014Article
- Ectromelia virus encodes a BTB/kelch protein, EVM150, that inhibits NF-κB signaling.Journal of virology · 2014Article
- Loss of cytoskeletal transport during egress critically attenuates ectromelia virus infection in vivo.Journal of virology · 2012Article
- Orthopoxvirus genes that mediate disease virulence and host tropism.Advances in virology · 2012Article
- Deerpox virus encodes an inhibitor of apoptosis that regulates Bak and Bax.Journal of virology · 2011Article
- Viral takeover of the host ubiquitin system.Frontiers in microbiology · 2011Article
- Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.