Control of mRNA export by adenovirus E4orf6 and E1B55K proteins during productive infection requires E4orf6 ubiquitin ligase activity

Journal of Virology
Paola BlanchetteT Dobner

Abstract

During the adenovirus infectious cycle, the early proteins E4orf6 and E1B55K are known to perform several functions. These include nuclear export of late viral mRNAs, a block of nuclear export of the bulk of cellular mRNAs, and the ubiquitin-mediated degradation of selected proteins, including p53 and Mre11. Degradation of these proteins occurs via a cellular E3 ubiquitin ligase complex that is assembled through interactions between elongins B and C and BC boxes present in E4orf6 to form a cullin 5-based ligase complex. E1B55K, which has been known for some time to associate with the E4orf6 protein, is thought to bind to specific substrate proteins to bring them to the complex for ubiquitination. Earlier studies with E4orf6 mutants indicated that the interaction between the E4orf6 and E1B55K proteins is optimal only when E4orf6 is able to form the ligase complex. These and other observations suggested that most if not all of the functions ascribed to E4orf6 and E1B55K during infection, including the control of mRNA export, are achieved through the degradation of specific substrates by the E4orf6 ubiquitin ligase activity. We have tested this hypothesis through the generation of a virus mutant in which the E4orf6 product is unab...Continue Reading

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Citations

Jul 11, 2008·Journal of Virology·Rachel A SchwartzMatthew D Weitzman
Jan 9, 2009·Journal of Virology·Michael A ThomasDavid A Ornelles
Dec 3, 2010·Journal of Virology·Gayatri YatherajamS J Flint
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Oct 13, 2017·Journal of Virology·Ana QuintasYolanda Revilla
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Dec 29, 2020·Virus Research·Samuel HofmannSabrina Schreiner

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