ArticleJournal of virology1998
Phosphorylation of the human cytomegalovirus 86-kilodalton immediate-early protein IE2.
Article in Journal of virology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
47 citing papers in PubMed, 68 citations in OpenAlex.
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- Human Cytomegalovirus Decreases Major Histocompatibility Complex Class II by Regulating Class II Transactivator Transcript Levels in a Myeloid Cell Line.Journal of virology · 2020Article
- Bright and Early: Inhibiting Human Cytomegalovirus by Targeting Major Immediate-Early Gene Expression or Protein Function.Viruses · 2020Review
- Casein kinase-2-mediated phosphorylation increases the SUMO-dependent activity of the cytomegalovirus transactivator IE2.The Journal of biological chemistry · 2019Article
- Inhibition of diverse opportunistic viruses by structurally optimized retrograde trafficking inhibitors.Bioorganic & medicinal chemistry · 2019Article
- A tumor-specific endogenous repetitive element is induced by herpesviruses.Nature communications · 2019Article
- Nonenvelopment Role for the ESCRT-III Complex during Human Cytomegalovirus Infection.Journal of virology · 2018Article
- RO0504985 is an inhibitor of CMGC kinase proteins and has anti-human cytomegalovirus activity.Antiviral research · 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
- Potent Inhibition of Human Cytomegalovirus by Modulation of Cellular SNARE Syntaxin 5.Journal of virology · 2017Article
- 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
- PKR-like endoplasmic reticulum kinase is necessary for lipogenic activation during HCMV infection.PLoS pathogens · 2013Article
- Phosphorylation events during viral infections provide potential therapeutic targets.Reviews in medical virology · 2012Article
- Human cytomegalovirus infection induces adipocyte-like lipogenesis through activation of sterol regulatory element binding protein 1.Journal of virology · 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
- The changing role of mTOR kinase in the maintenance of protein synthesis during human cytomegalovirus infection.Journal of virology · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
We have investigated the phosphorylation state of the human cytomegalovirus 86-kDa immediate-early (IE) protein IEP86 from transfected and infected cells. We show that multiple domains of IEP86 are phosphorylated by cellular kinases, both in vitro and in vivo. Our data suggest that serum-inducible kinases play a significant role in cell-mediated IE protein phosphorylation and that a member of the mitogen-activated protein (MAP) kinase (MAPK) family, extracellular regulated kinase 2 (ERK2), phosphorylates several domains of IEP86 in vitro. Alanine substitution mutagenesis was performed on specific serines or threonines (T27, S144, T233/S234, and T555) found in consensus MAP kinase motifs. Analysis of these mutations showed that T27 and T233/S234 are the major sites for serum-inducible kinases and are the major ERK2 sites in vitro. S144 appeared to be phosphorylated in a serum-independent manner in vitro. All of the mutations except T555 eliminated specific phosphorylation in vivo. In transient transfection analyses, IEP86 isoforms containing mutations in S144 and, especially, T233/S234 displayed increased transcriptional activation relative to the wild type, suggesting that phosphorylation at these sites in wild-type IEP86 may result in reduction of its transcriptional activation ability.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.