ArticleJournal of virology2008
Interaction between simian virus 40 large T antigen and insulin receptor substrate 1 is disrupted by the K1 mutation, resulting in the loss of large T antigen-mediated phosphorylation of Akt.
Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 36 citations in OpenAlex.
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- Replication of JC Virus DNA in the G144 Oligodendrocyte Cell Line Is Dependent Upon Akt.Journal of virology · 2017Article
- ACSS2-mediated acetyl-CoA synthesis from acetate is necessary for human cytomegalovirus infection.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The Human Papillomavirus 16 E7 Oncoprotein Attenuates AKT Signaling To Promote Internal Ribosome Entry Site-Dependent Translation and Expression of c-MYC.Journal of virology · 2016Article
- Molecular Determinants for the Inactivation of the Retinoblastoma Tumor Suppressor by the Viral Cyclin-dependent Kinase UL97.The Journal of biological chemistry · 2015Article
- Transformation with oncogenic Ras and the simian virus 40 T antigens induces caspase-dependent sensitivity to fatty acid biosynthetic inhibition.Journal of virology · 2015Article
- Novel mutations in the RB1 gene from Chinese families with a history of retinoblastoma.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015Article
- Polyomavirus T antigens activate an antiviral state.Virology · 2015Article
- Inhibition of Cullin-RING E3 ubiquitin ligase 7 by simian virus 40 large T antigen.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- ChREBP, a glucose-responsive transcriptional factor, enhances glucose metabolism to support biosynthesis in human cytomegalovirus-infected cells.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Pulmonary tumors associated with the JC virus T-antigen in a transgenic mouse model.Oncology reports · 2013Article
- PKR-like endoplasmic reticulum kinase is necessary for lipogenic activation during HCMV infection.PLoS pathogens · 2013Article
- Dynein mediates the localization and activation of mTOR in normal and human cytomegalovirus-infected cells.Genes & development · 2012Article
- HijAkt: The PI3K/Akt pathway in virus replication and pathogenesis.Progress in molecular biology and translational science · 2012Review
- Activation of the PI3K/AKT pathway in Merkel cell carcinoma.PloS one · 2012Article
- Human cytomegalovirus induces multiple means to combat reactive oxygen species.Journal of virology · 2011Article
- Human cytomegalovirus infection maintains mTOR activity and its perinuclear localization during amino acid deprivation.Journal of virology · 2011Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The cellular kinase Akt is a key controller of cellular metabolism, growth, and proliferation. Many viruses activate Akt due to its beneficial effects on viral replication. We previously showed that wild-type (WT) simian virus 40 (SV40) large T antigen (TAg) inhibits apoptosis via the activation of PI3K/Akt signaling. Here we show that WT TAg expressed from recombinant adenoviruses in U2OS cells induced the phosphorylation of Akt at both T308 and S473. In contrast, Akt phosphorylation was eliminated by the K1 mutation (E107K) within the retinoblastoma protein (Rb) binding motif of TAg. This suggested that Akt phosphorylation may depend on TAg binding to Rb or one of its family members. However, in Rb-negative SAOS2 cells depleted of p107 and p130 by using small hairpin RNAs (shRNAs), WT TAg still mediated Akt phosphorylation. These results suggested that the K1 mutation affects another TAg function. WT-TAg-mediated phosphorylation of Akt was inhibited by a PI3K inhibitor, suggesting that the effects of TAg originated upstream of PI3K; thus, we examined the requirement for insulin receptor substrate 1 (IRS1), which binds and activates PI3K. Depletion of IRS1 by shRNAs abolished the WT-TAg-mediated phosphorylation of Akt. Immunoprecipitation studies showed that the known interaction between TAg and IRS1 is significantly weakened by the K1 mutation. These data indicate that the K1 mutation disrupts not only Rb binding but also IRS1 binding, contributing to the loss of activation of PI3K/Akt signaling.
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