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Gene Review

CeHV15gEBNA-3C  -  EBNA-3C

Macacine herpesvirus 4

 
 
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Disease relevance of CeHV15gEBNA-3C

  • Function, as measured by in vitro assays, also appears to be conserved with the EBV genes, since the rhesus LCV EBNA-3s can interact with the transcription factor RBP-Jkappa and the rhesus LCV EBNA-3C encodes a Q/P-rich domain with transcriptional activation properties [1].
  • To better understand the contribution of these interactions to EBNA-3C function and EBV latency, we examined whether they are conserved in the homologous proteins of nonhuman primate lymphocryptoviruses (LCVs), which bear a strong genetic and biological similarity to EBV [2].
  • Cell migration assays geared towards determining the effect of EBNA3C on Nm23-H1 antimetastatic function suggests that EBNA3C suppresses the effects of NM23-H1 on the motility of breast carcinoma as well as Burkitt's lymphoma cells [3].
 

High impact information on CeHV15gEBNA-3C

 

Biological context of CeHV15gEBNA-3C

  • The conservation of these functional motifs despite poor overall homology among the LCV 3C proteins strongly suggests that the interactions of EBNA-3C with J kappa and Spi do indeed play significant roles in the life cycle of EBV [2].
  • Although genetic and biochemical data indicate that the cell protein RBPJkappa is a mediator of EBNA-2 and EBNA-3C effects on transcriptional regulatory elements, the extent of association of these Epstein-Barr virus nuclear proteins with RBPJkappa in transformed B lymphocytes has not been determined [7].
  • These results suggest that Rhesus LCV restriction from human B cell immortalization is independent of the conserved cell cycle regulatory functions of the EBNA3C protein [8].
  • The Epstein Barr nuclear antigen EBNA3C regulates transcription, cell transformation and cell migration [3].
  • The interaction of EBNA3C with ProTalpha as well as the histone acetylase p300 suggested a possible role in modulation of histone acetylation and chromatin remodeling [3].
 

Associations of CeHV15gEBNA-3C with chemical compounds

References

  1. Structural, functional, and genetic comparisons of Epstein-Barr virus nuclear antigen 3A, 3B, and 3C homologues encoded by the rhesus lymphocryptovirus. Jiang, H., Cho, Y.G., Wang, F. J. Virol. (2000) [Pubmed]
  2. Transcriptional regulatory properties of Epstein-Barr virus nuclear antigen 3C are conserved in simian lymphocryptoviruses. Zhao, B., Dalbiès-Tran, R., Jiang, H., Ruf, I.K., Sample, J.T., Wang, F., Sample, C.E. J. Virol. (2003) [Pubmed]
  3. The Epstein Barr nuclear antigen EBNA3C regulates transcription, cell transformation and cell migration. Subramanian, C., Knight, J.S., Robertson, E.S. Front. Biosci. (2002) [Pubmed]
  4. Modulation of histone acetyltransferase activity through interaction of epstein-barr nuclear antigen 3C with prothymosin alpha. Cotter, M.A., Robertson, E.S. Mol. Cell. Biol. (2000) [Pubmed]
  5. EBNA-3B- and EBNA-3C-Regulated Cellular Genes in Epstein-Barr Virus-Immortalized Lymphoblastoid Cell Lines. Chen, A., Zhao, B., Kieff, E., Aster, J.C., Wang, F. J. Virol. (2006) [Pubmed]
  6. A cyclin-binding motif within the amino-terminal homology domain of EBNA3C binds cyclin A and modulates cyclin A-dependent kinase activity in Epstein-Barr virus-infected cells. Knight, J.S., Sharma, N., Kalman, D.E., Robertson, E.S. J. Virol. (2004) [Pubmed]
  7. EBNA-2 and EBNA-3C extensively and mutually exclusively associate with RBPJkappa in Epstein-Barr virus-transformed B lymphocytes. Johannsen, E., Miller, C.L., Grossman, S.R., Kieff, E. J. Virol. (1996) [Pubmed]
  8. Conserved cell cycle regulatory properties within the amino terminal domain of the Epstein-Barr virus nuclear antigen 3C. Sharma, N., Knight, J.S., Robertson, E.S. Virology (2006) [Pubmed]
 
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