Epstein-Barr virus-encoded EBNA-5 binds to Epstein-Barr virus-induced Fte1/S3a protein

Kashuba, Elena; Yurchenko, Mariya; Szirák, Krisztina; Stahl, Joachim; Klein, George; Szekeres, L.

doi:10.1016/j.yexcr.2004.08.025

Cited by 12 publications

(14 citation statements)

References 43 publications

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“…In particular, RPS3a is associated with EBV, an oncogenic virus [17]. Similar to HBx in our studies, EBNA-5, an EBV-encoded viral protein, binds with RPS3a and induces RPS3a expression, suggesting a role of RPS3a in EBV-induced tumorigenesis [17].…”

Section: Discussionsupporting

confidence: 76%

“…RPS3a, a component of the ribosomal small subunit (40S) [16], shows high sequence homology in mammalian cells and is localized in both the nucleus and cytoplasm [17]. RPS3a also has multiple biological functions unrelated with the ribosome.…”

Section: Introductionmentioning

confidence: 99%

“…Importantly, it is reported that Epstein-Barr virus (EBV)-induced B cell transformation leads to the up-regulation of RPS3a. Furthermore, EBV-encoded nuclear antigen, EBNA-5 is reported to bind RPS3a, suggesting a role for EBV-induced B cell transformation [17]. On the other hand, RPS3a has also been described as a regulator of apoptosis and transcription factors [27]–[29].…”

Section: Introductionmentioning

confidence: 99%

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RPS3a Over-Expressed in HBV-Associated Hepatocellular Carcinoma Enhances the HBx-Induced NF-κB Signaling via Its Novel Chaperoning Function

et al. 2011

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Hepatitis B virus (HBV) infection is one of the major causes of hepatocellular carcinoma (HCC) development. Hepatitis B virus X protein (HBx) is known to play a key role in the development of hepatocellular carcinoma (HCC). Several cellular proteins have been reported to be over-expressed in HBV-associated HCC tissues, but their role in the HBV-mediated oncogenesis remains largely unknown. Here, we explored the effect of the over-expressed cellular protein, a ribosomal protein S3a (RPS3a), on the HBx-induced NF-κB signaling as a critical step for HCC development. The enhancement of HBx-induced NF-κB signaling by RPS3a was investigated by its ability to translocate NF-κB (p65) into the nucleus and the knock-down analysis of RPS3a. Notably, further study revealed that the enhancement of NF-κB by RPS3a is mediated by its novel chaperoning activity toward physiological HBx. The over-expression of RPS3a significantly increased the solubility of highly aggregation-prone HBx. This chaperoning function of RPS3a for HBx is closely correlated with the enhanced NF-κB activity by RPS3a. In addition, the mutational study of RPS3a showed that its N-terminal domain (1–50 amino acids) is important for the chaperoning function and interaction with HBx. The results suggest that RPS3a, via extra-ribosomal chaperoning function for HBx, contributes to virally induced oncogenesis by enhancing HBx-induced NF-κB signaling pathway.

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Section: Discussionsupporting

confidence: 76%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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RPS3a Over-Expressed in HBV-Associated Hepatocellular Carcinoma Enhances the HBx-Induced NF-κB Signaling via Its Novel Chaperoning Function

et al. 2011

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“…EBNA-LP has also been shown to interact with several cellular proteins, including oncogenes and tumor suppressors (pRb, p53, p14ARF, and Fte1/S3a), heat shock proteins (hsp70 and hsp72/hsc73), molecules involved in cell cycle regulation (DNA-PKcs and HA95) and HAX-1, an antiapoptotic protein (6,9,14,15,27,45). However, the roles of most of these interactions remain to be established.…”

mentioning

confidence: 99%

Truncated Form of the Epstein-Barr Virus Protein EBNA-LP Protects against Caspase-Dependent Apoptosis by Inhibiting Protein Phosphatase 2A

Garibal

Hollville

Bell

et al. 2007

J Virol

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“…Cloning of GST2TK-EBNA-5 and pBabe-puro-EBNA-5 was described previously. 20 The EBNA-5 constructs contained four W 1 W 2 repeats and the unique C-terminal domain (Y). EBNA-5 containing four W 1 W 2 repeats and the Y domain was subcloned into pGEM (Sp6) vector at the BamH1/EcoRI sites.…”

Section: Plasmidsmentioning

confidence: 99%

Epstein‐Barr virus‐encoded EBNA‐5 forms trimolecular protein complexes with MDM2 and p53 and inhibits the transactivating function of p53

Kashuba

Yurchenko

Yenamandra

et al. 2010

Intl Journal of Cancer

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We report that MDM2, a negative regulator of p53, can bind to EBNA-5. Using GST pull-down assay, immunoprecipitation, surface plasmon resonance and immunostaining of lymphoblastoid cells, we found that trimolecular complexes are formed between EBNA-5, MDM2 and p53, where MDM2 serves as a bridge. The EBNA-5 binding to MDM2 counteracted destabilizing effect of the latter on the p53. In ubiquitination and degradation assays in vitro, EBNA-5 inhibited p53 polyubiquitination (but not monoubiquitination) in a concentration-dependent manner. This resembles the effect of p14ARF on p53. Moreover, EBNA-5 was found to inhibit the degradation of p53 in vitro. High levels of p53 expression were maintained in LCLs. The binding of EBNA-5 to MDM2 also could impair the functional activity of p53. The p53-dependent genes P21 and VDR were not induced in EBV-infected, in contrast to mitogen-activated cells. This may explain the tolerance of established LCLs to high levels of p53 without undergoing apoptosis.

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Epstein-Barr virus-encoded EBNA-5 binds to Epstein-Barr virus-induced Fte1/S3a protein

Cited by 12 publications

References 43 publications

RPS3a Over-Expressed in HBV-Associated Hepatocellular Carcinoma Enhances the HBx-Induced NF-κB Signaling via Its Novel Chaperoning Function

RPS3a Over-Expressed in HBV-Associated Hepatocellular Carcinoma Enhances the HBx-Induced NF-κB Signaling via Its Novel Chaperoning Function

Truncated Form of the Epstein-Barr Virus Protein EBNA-LP Protects against Caspase-Dependent Apoptosis by Inhibiting Protein Phosphatase 2A

Epstein‐Barr virus‐encoded EBNA‐5 forms trimolecular protein complexes with MDM2 and p53 and inhibits the transactivating function of p53

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