Preferred Name | Interaction of ISG15 with NEDD4 and inhibition of Ebola virus budding | |
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Definitions |
Ebola virus VP40 virus-like particles (VLPs) requires the interaction of overlapping L-domains in the VP40 protein with host NEDD4 protein for efficient budding. Mono-ubiquitination of VP40 mediated by the NEDD4 E3 ligase is thought to be required for virus budding and release. ISG15 interacts with NEDD4 and inhibits the transfer of ubiquitin from the E2 enzyme to NEDD4. This prevents NEDD4-mediated ubiquitination of Ebola virus VP40 which is required for virion release. Authored: Garapati, P V, 2011-01-18 Reviewed: Zhang, DE, 2011--0-2- Edited: Garapati, P V, 2011-01-18 |
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ID |
http://purl.obolibrary.org/obo/HINO_0007153 |
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comment |
Ebola virus VP40 virus-like particles (VLPs) requires the interaction of overlapping L-domains in the VP40 protein with host NEDD4 protein for efficient budding. Mono-ubiquitination of VP40 mediated by the NEDD4 E3 ligase is thought to be required for virus budding and release. ISG15 interacts with NEDD4 and inhibits the transfer of ubiquitin from the E2 enzyme to NEDD4. This prevents NEDD4-mediated ubiquitination of Ebola virus VP40 which is required for virion release. Authored: Garapati, P V, 2011-01-18 Reviewed: Zhang, DE, 2011--0-2- Edited: Garapati, P V, 2011-01-18 |
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definition source |
Pubmed12525615 Reactome, http://www.reactome.org Pubmed18287095 Pubmed20153823 Pubmed11095724 Pubmed18305167 |
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label |
Interaction of ISG15 with NEDD4 and inhibition of Ebola virus budding |
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prefixIRI |
HINO:0007153 |
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prefLabel |
Interaction of ISG15 with NEDD4 and inhibition of Ebola virus budding |
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seeAlso |
ReactomeREACT_115975 Reactome Database ID Release 431169399 |
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subClassOf |