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• W2055239738 endingPage "9807" @default.
• W2055239738 startingPage "9803" @default.
• W2055239738 abstract "The ubiquitin-proteasome pathway plays a critical role in the degradation of short-lived and regulatory proteins in a variety of cellular processes. The F-box proteins are part of the ubiquitin-ligase complexes, which mediate ubiquitination and proteasome-dependent degradation of phosphorylated proteins. We previously identified NFB42, an F-box protein that is highly enriched in the nervous system, as a binding partner for the herpes simplex virus 1 UL9 protein, the viral replication-initiator protein, in a yeast two-hybrid screen. In the present work, we find that coexpression of NFB42 and UL9 genes in 293T cells leads to a significant decrease in the level of UL9 protein. Treatment with the 26S-proteasome inhibitor MG132 restores the UL9 protein to normal levels. We have observed also that the UL9 protein is polyubiquitinated in vivo and that the interaction between NFB42 and the UL9 protein is dependent upon phosphorylation of the UL9 protein. These results suggest that the interaction of the UL9 protein with NFB42 results in its polyubiquitination and subsequent degradation by the 26S proteasome. They suggest further a mechanism by which latency of herpes simplex virus 1 can be established in neuronal cells." @default.
• W2055239738 created "2016-06-24" @default.
• W2055239738 creator A5029607367 @default.
• W2055239738 creator A5053216536 @default.
• W2055239738 date "2003-08-06" @default.
• W2055239738 modified "2023-09-27" @default.
• W2055239738 title "Replication-initiator protein (UL9) of the herpes simplex virus 1 binds NFB42 and is degraded via the ubiquitin–proteasome pathway" @default.
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• W2055239738 doi "https://doi.org/10.1073/pnas.1733876100" @default.
• W2055239738 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/187846" @default.
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