ArticleVirus genes2006
Association of two membrane proteins encoded by herpes simplex virus type 2, UL11 and UL56.
Article in Virus genes, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Review
- Features and Functions of the Conserved Herpesvirus Tegument Protein UL11 and Its Binding Partners.Frontiers in microbiology · 2022Review
- "Non-Essential" Proteins of HSV-1 with Essential Roles In Vivo: A Comprehensive Review.Viruses · 2020Review
- Article
- Protein interactions and consensus clustering analysis uncover insights into herpesvirus virion structure and function relationships.PLoS biology · 2019Article
- The first genome sequence of a metatherian herpesvirus: Macropodid herpesvirus 1.BMC genomics · 2016Article
- The pseudorabies virus protein, pUL56, enhances virus dissemination and virulence but is dispensable for axonal transport.Virology · 2016Article
- Role of the nuclease activities encoded by herpes simplex virus 1 UL12 in viral replication and neurovirulence.Journal of virology · 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
- Article
- Herpes simplex virus UL56 interacts with and regulates the Nedd4-family ubiquitin ligase Itch.Virology journal · 2010Article
- Herpesvirus systematics.Veterinary microbiology · 2010Article
- Differences in the regulatory and functional effects of the Us3 protein kinase activities of herpes simplex virus 1 and 2.Journal of virology · 2009Article
- Herpes simplex virus type 2 tegument protein UL56 relocalizes ubiquitin ligase Nedd4 and has a role in transport and/or release of virions.Virology journal · 2009Article
- Herpes simplex virus type 2 UL56 interacts with the ubiquitin ligase Nedd4 and increases its ubiquitination.Journal of virology · 2008Article
- Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Herpes simplex virus (HSV) acquires envelope by budding into trans-Golgi network (TGN)-derived vesicles. Previous studies showed that the UL11 gene product enables efficient virion envelopment and export from infected cells and is incorporated into virions as tegument protein. At its N-terminus, UL11 is dually acylated by myristoic and palmitoic acids. Fatty acylation of UL11 provides both membrane binding strength and Golgi-targeting specificity. We show here that UL11 interacts with UL56 protein, a tail-anchored type II membrane protein encoded by HSV, which associated with the Golgi apparatus and cytoplasmic vesicles. We previously showed that UL56 is involved in vesicular transport in infected cells. The UL11-UL56 complex localized to the perinuclear region of the cytoplasm in infected cells. Fatty acylation of UL11 was important for the formation of the UL11-UL56 protein complex. Taken together, our results identify a novel interaction between two HSV proteins facilitated by mutual interactions with Golgi-derived vesicles.
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Registered trials
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