Herpesviruses possess conserved proteins for interaction with Nedd4 family ubiquitin E3 ligases
Autor: | Tetsuo Koshizuka, Takahiro Kobayashi, Tatsuo Suzutani, Ken Ishioka |
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Jazyk: | angličtina |
Rok vydání: | 2018 |
Předmět: |
0301 basic medicine
CD3 Complex Nedd4 Ubiquitin Protein Ligases Ubiquitin-Protein Ligases viruses Protein domain lcsh:Medicine NEDD4 Plasma protein binding macromolecular substances Article Viral Proteins 03 medical and health sciences Retrovirus Protein Domains Ubiquitin Cell Line Tumor Humans lcsh:Science Herpesviridae Binding Sites Multidisciplinary 030102 biochemistry & molecular biology biology lcsh:R biology.organism_classification Cell biology Repressor Proteins HEK293 Cells 030104 developmental biology Membrane protein biology.protein lcsh:Q HeLa Cells Protein Binding |
Zdroj: | Scientific Reports, Vol 8, Iss 1, Pp 1-10 (2018) Scientific Reports |
ISSN: | 2045-2322 |
Popis: | Nedd4 is a family of ubiquitin E3 ligases that regulate numerous cellular processes. In this report, we showed that alpha- and beta-herpesviruses have membrane proteins that regulate the function of the Nedd4 family members. Although the homology search score was quite low, UL56 of herpes simplex virus type 1 and 2, ORF0 of varicella-zoster virus, UL42 of human cytomegalovirus, and U24 of human herpesvirus 6A, 6B, and 7 all possess at least one PPxY (PY) motif in their cytoplasmic domain, and are able to bind with Itch, a member of the Nedd4 family. These viral proteins altered the localization of Itch and decreased Itch expression in co-expressing cells. In addition, these viral proteins reduced the production of retrovirus vectors through the regulation of the Nedd4 family of proteins. U24, but not the other proteins, effectively reduced CD3ε expression on the T cell surface. These viral molecules are thought to contribute to the specific function of each virus through the regulation of Nedd4 family activity. |
Databáze: | OpenAIRE |
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