Adenovirus E1B 19,000-Molecular-Weight Protein Activates c-Jun N-Terminal Kinase and c-Jun-Mediated Transcription

See, Raymond H.; Shi, Yang

doi:10.1128/mcb.18.7.4012

Cited by 26 publications

(30 citation statements)

References 71 publications

(104 reference statements)

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“…However, the situation bears some resemblance to the inhibition of apoptosis and SAPK activation associated with the E1B19K protein of adenovirus (33). This viral protein up-regulates SAPK activity but also inhibits Fas-mediated apoptosis by binding to BAX, APAF1, and FADD/caspase 8 in the signal transduction pathway (31,93).…”

Section: Discussionmentioning

confidence: 99%

“…Many viruses act to up-regulate SAPK activity to increase their survival (32). For example, adenovirus activates SAPK activity and c-JUN transcription via its E1B19K protein (33). The LMP1 protein of Epstein-Barr virus also activates SAPK, which may contribute to the transforming properties of this viral protein.…”

Section: Discussionmentioning

confidence: 99%

“…32). These include the E1B/19K protein of adenovirus (33), the TAT protein of human immunodeficiency virus (34), the LMP1 protein of Epstein-Barr virus, the TAX protein of HTLV-1, the angiogenic G protein receptor of Kaposi sarcoma virus, and the HBx protein of HBV (35,36). Cellular oncogenes such as TPL2 (tumor progression locus 2 protein) and BCR-ABL tyrosine kinase and the HER2/NEU gene product associated with many breast tumors, epidermal growth factor-stimulated proliferation, the RET oncoprotein, the MAS gene product, and the MET protein increase SAPK levels (32).…”

Section: Hepatitis B Virus (Hbv)mentioning

confidence: 99%

See 2 more Smart Citations

X Protein of Hepatitis B Virus Inhibits Fas-mediated Apoptosis and Is Associated with Up-regulation of the SAPK/JNK Pathway

Diao

Khine

Sarangi

et al. 2001

Journal of Biological Chemistry

157

121

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The X protein from a chronic strain of hepatitis B virus (HBx) was determined to inhibit Fas-mediated apoptosis and promote cell survival. Fas-mediated apoptosis is the major cause of hepatocyte damage during liver disease. Experiments demonstrated that cell death caused by anti-Fas antibodies was blocked by the expression of HBx in human primary hepatocytes and mouse embryo fibroblasts. This effect was also observed in mouse erythroleukemia cells that lacked p53, indicating that protection against Fas-mediated apoptosis was independent of p53. Components of the signal transduction pathways involved in this protection were studied. The SAPK/JNK pathway has previously been suggested to be a survival pathway for some cells undergoing Fasmediated apoptosis, and kinase assays showed that SAPK activity was highly up-regulated in cells expressing the HBx protein. Normal mouse fibroblasts expressing HBx were protected from death, whereas identical fibroblasts lacking the SEK1 component from the SAPK pathway succumbed to Fas-mediated apoptosis, whether HBx was present or not. Assays showed that caspase 3 and 8 activities and the release of cytochrome c from mitochondria were inhibited, in the presence of HBx, following stimulation with anti-Fas antibodies. Coprecipitation and confocal immunofluorescence microscopy experiments demonstrated that HBx localizes with a cytoplasmic complex containing MEKK1, SEK1, SAPK, and 14-3-3 proteins. Finally, mutational analysis of HBx demonstrated that a potential binding region for 14-3-3 proteins was essential for induction of SAPK/JNK activity and protection from Fas-mediated apoptosis.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Hepatitis B Virus (Hbv)mentioning

confidence: 99%

See 1 more Smart Citation

X Protein of Hepatitis B Virus Inhibits Fas-mediated Apoptosis and Is Associated with Up-regulation of the SAPK/JNK Pathway

Diao

Khine

Sarangi

et al. 2001

Journal of Biological Chemistry

157

121

View full text Add to dashboard Cite

show abstract

“…Some viruses show a dependence on the ERK signaling cascades for replication, and viral proteins inducing ERK activation have been identified (2,22,24,34,38,39). Virus-induced activation of two other MAPKs, JNK and p38, has also been described (9,18,20,36,40,48,53,58). However, to date, the signaling pathways induced by baculovirus infec- tion are largely unknown.…”

Section: Discussionmentioning

confidence: 99%

ERK- and JNK-Dependent Signaling Pathways Contribute to Bombyx mori Nucleopolyhedrovirus Infection

Katsuma

Mita

Shimada

2007

J Virol

110

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Mitogen-activated protein kinases (MAPKs) often play important roles in virus infection. To explore intracellular signaling pathways induced by baculovirus infection, we examined the involvement of MAPKs inBombyx mori nucleopolyhedrovirus (BmNPV) infection of BmN cells. We found that specific inhibitors of extracellular signal-regulated kinase (ERK) kinase and c-Jun NH 2 -terminal kinase (JNK) significantly reduced occlusion body (OB) formation and budded virus (BV) production. Next, we quantified OB and BV production after applying the inhibitors at different times postinfection (p.i.). The inhibitors significantly reduced OB and BV production to various extents when applied at 12 h p.i., indicating that the reduction of BmNPV infectivity by these inhibitors occurs at the late stage of infection. Also, we observed that these inhibitors markedly repressed or deregulated the expression of delayed early, late, and very late gene products. Western blot analysis using phospho-MAPK-specific antibodies showed that ERK and JNK were activated at the late stage of BmNPV infection. In addition, the magnitude and pattern of MAPK activation were dependent on the multiplicity of infection. To verify the effects of the inhibitors on BmNPV infection, we also attempted to knock down the B. mori genes BmErk and BmJnk, which encode ERK and JNK, respectively. Knockdown of BmErk and BmJnk resulted in the reduced production of OBs and BVs, confirming that BmERK and BmJNK are involved in the BmNPV infection process. Taken together, these results indicate that the activation of MAPK signaling pathways is required for efficient infection by BmNPV.

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“…Briefly, proliferating U20S cells were treated with either Me 2 SO solvent control or nocodazole at the indicated concentrations. Cell lysates were prepared 1 h post-treatment, and the activation of MEKK1 was analyzed by Western blotting with an anti-JNK1 antibody (SC-474, Santa Cruz Biotechnology) as described previously (39).…”

Section: Methodsmentioning

confidence: 99%

Stimulation of p300-mediated Transcription by the Kinase MEKK1

See

Calvo

Shi

et al. 2001

Journal of Biological Chemistry

Self Cite

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p300 and CREB-binding protein (CBP) are related transcriptional coactivators that possess histone acetyltransferase activity. Inactivation of p300/CBP is part of the mechanism by which adenovirus E1A induces oncogenic transformation of cells. Recently, the importance of p300/CBP has been demonstrated directly in several organisms including mouse, Drosophila, and Caenorhabditis elegans where p300/CBP play an indispensable role in differentiation, in patterning, and in cell fate determination and proliferation during development. CBP/p300s are modified by phosphorylation during F9 cell differentiation as well as adenovirus infection, suggesting that phosphorylation may play a role in the regulation of p300/CBP activity. Here we show that the mitogen-activated/extracellular response kinase kinase 1 (MEKK1) enhances p300-mediated transcription. We identify several domains within p300 that can respond to MEKK1-induced transcriptional activation. Interestingly, activation of p300-mediated transcription by MEKK1 does not appear to require the downstream kinase JNK and may involve either a direct phosphorylation of p300 by MEKK1 or by other non-JNK MEKK1-directed downstream kinases. Finally, we present evidence that p300 is important for MEKK1 to induce apoptosis. Taken together, these results identify MEKK1 as a kinase that is likely to be involved in the regulation of the transactivation potential of p300 and support a role of p300 in MEKK1-induced apoptosis.

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Adenovirus E1B 19,000-Molecular-Weight Protein Activates c-Jun N-Terminal Kinase and c-Jun-Mediated Transcription

Cited by 26 publications

References 71 publications

X Protein of Hepatitis B Virus Inhibits Fas-mediated Apoptosis and Is Associated with Up-regulation of the SAPK/JNK Pathway

X Protein of Hepatitis B Virus Inhibits Fas-mediated Apoptosis and Is Associated with Up-regulation of the SAPK/JNK Pathway

ERK- and JNK-Dependent Signaling Pathways Contribute to Bombyx mori Nucleopolyhedrovirus Infection

Stimulation of p300-mediated Transcription by the Kinase MEKK1

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