| Item Type: | Article | 
|---|---|
| Title: | Epstein-Barr virus-encoded EBNA-5 binds to Epstein-Barr virus-induced Fte1/S3a protein | 
| Creators Name: | Kashuba, E., Yurchenko, M., Szirak, K., Stahl, J., Klein, G. and Szekely, L. | 
| Abstract: | Epstein-Barr virus (EBV) transforms resting human B cells into immortalized immunoblasts. EBV-encoded nuclear antigens EBNA-5 (also called EBNA-LP) is one of the earliest viral proteins expressed in freshly infected B cells. We have recently shown that EBNA-5 binds p14ARF, a nucleolar protein that regulates the p53 pathway. Here, we report the identification of another protein with partially nucleolar localization, the v-fos transformation effector Fte-1 (Fte-1/S3a), as an EBNA-5 binding partner. In transfected cells, Fte-1/S3a and EBNA-5 proteins showed high levels of colocalization in extranucleolar inclusions. Fte-1/S3a has multiple biological functions. It enhances v-fos-mediated cellular transformation and is part of the small ribosomal subunit. It also interacts with the transcriptional factor CHOP and apoptosis regulator poly(ADP-ribose) polymerase (PARP). Fte-1/S3a is regularly expressed at high levels in both tumors and cancer cell lines. Its high expression favors the maintenance of malignant phenotype and undifferentiated state, whereas its down-regulation is associated with cellular differentiation and growth arrest. Here, we show that EBV-induced B cell transformation leads to the up-regulation of Fte-1/S3a. We suggest that EBNA-5 through binding may influence the growth promoting, differentiation inhibiting, or apoptosis regulating functions of Fte-1/S3a. | 
| Keywords: | Cell Transformation, EBNA-5, Epstein-Barr Virus, Fte-1/S3a Ribosomal Protein, Yeast Two-Hybrid System | 
| Source: | Experimental Cell Research | 
| ISSN: | 0014-4827 | 
| Publisher: | Elsevier | 
| Volume: | 303 | 
| Number: | 1 | 
| Page Range: | 47-55 | 
| Date: | 1 January 2005 | 
| Official Publication: | https://doi.org/10.1016/j.yexcr.2004.08.025 | 
| PubMed: | View item in PubMed | 
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