ArticleVirology journal2010
Herpes simplex virus UL56 interacts with and regulates the Nedd4-family ubiquitin ligase Itch.
Article in Virology journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 28 citations in OpenAlex.
- HSV-1 UL56 protein recruits cellular NEDD4-family ubiquitin ligases to suppress CD1d expression and NKT cell function.Journal of virology · 2025Article
- DR5 is a restriction factor for human herpesviruses.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- HSV-1 employs UL56 to antagonize expression and function of cGAMP channels.Cell reports · 2024Article
- Article
- Genetic variation in NDFIP1 modifies the metabolic patterns in immune cells of multiple sclerosis patients.Scientific reports · 2021Article
- Motor Skills: Recruitment of Kinesins, Myosins and Dynein during Assembly and Egress of Alphaherpesviruses.Viruses · 2021Review
- "Non-Essential" Proteins of HSV-1 with Essential Roles In Vivo: A Comprehensive Review.Viruses · 2020Review
- ITCH as a potential therapeutic target in human cancers.Seminars in cancer biology · 2020Review
- Host BAG3 Is Degraded by Pseudorabies Virus pUL56 C-TerminalInternational journal of molecular sciences · 2020Article
- Seeking Closure: How Do Herpesviruses Recruit the Cellular ESCRT Apparatus?Journal of virology · 2019Review
- HSV-2 Cellular Programming Enables Productive HIV Infection in Dendritic Cells.Frontiers in immunology · 2019Article
- Article
- Time-resolved Global and Chromatin Proteomics during Herpes Simplex Virus Type 1 (HSV-1) Infection.Molecular & cellular proteomics : MCP · 2017Article
- The Mouse Cytomegalovirus Gene m42 Targets Surface Expression of the Protein Tyrosine Phosphatase CD45 in Infected Macrophages.PLoS pathogens · 2016Article
- Asna1/TRC40 that mediates membrane insertion of tail-anchored proteins is required for efficient release of Herpes simplex virus 1 virions.Virology journal · 2016Article
- The pseudorabies virus protein, pUL56, enhances virus dissemination and virulence but is dispensable for axonal transport.Virology · 2016Article
- Major histocompatibility complex class I downregulation induced by equine herpesvirus type 1 pUL56 is through dynamin-dependent endocytosis.Journal of virology · 2014Article
- Differential microRNA profile and post-transcriptional regulation exist in systemic lupus erythematosus patients with distinct autoantibody specificities.Journal of clinical immunology · 2014Article
- Identification and characterization of equine herpesvirus type 1 pUL56 and its role in virus-induced downregulation of major histocompatibility complex class I.Journal of virology · 2012Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundHerpes simplex virus type 2 (HSV-2) is one of many viruses that exploits and modifies the cellular ubiquitin system. HSV-2 expresses the tegument protein UL56 that has been implicated in cytoplasmic transport and/or release of virions, and is a putative regulatory protein of Nedd4 ubiquitin ligase. In order to elucidate the biological function of UL56, this study examined the interaction of UL56 with the Nedd4-family ubiquitin ligase Itch and its role in the regulation of Itch. Additionally, we assessed the similarity between UL56 and regulatory proteins of Itch and Nedd4, Nedd4-family-interactins proteins (Ndfip).
resultsUL56 interacted with Itch, independent of additional viral proteins, and mediated more striking degradation of Itch, compared to Nedd4. Moreover, it was suggested that the lysosome pathway as well as the proteasome pathway was involved in the degradation of Itch. Other HSV-2 proteins with PY motifs, such as VP5 and VP16, did not mediate the degradation of endogenous Itch. Ndfip1 and Ndfip2 were similar in subcellular distribution patterns to UL56 and colocalized with UL56 in co-transfected cells.
conclusionsWe believe that this is the first report demonstrating the interaction of a HSV-specific protein and Itch. Thus, UL56 could function as a regulatory protein of Itch. The mechanism, function and significance of regulating Itch in HSV-2 infection remain unclear and warrant further investigation.
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