期刊
VIROLOGY
卷 359, 期 1, 页码 37-45出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2006.09.001
关键词
STP-A11; Herpesvirus saimiri; IKK; NIK; canonical NF-kappa B; non-canonical NF-kappa B; NF-kappa B2; p52 protein; p100 processing
类别
Although Saimiri Transforming Protein (STP)-A11 an oncoprotein of Herpesvirus saimiri, has been known to activate NF-kappa B signaling pathway, the detailed mechanism has not been reported yet. We herein report that STP-A11 activates non-canonical NF-kappa B pathway, resulting in p100 processing to p52. In addition, translocation of p52 protein (NF-kappa B2) into the nucleus is observed by the expression of STP-A11. STP-A11-mediated processing of p100 to p52 protein requires proteosome-mediated proteolysis because MG132 treatment clearly blocked p52 production in spite of the expression of STP-A11. Analysis of STP-A11 mutants to activate NF-kappa B2 pathway discloses the requirement of TRAF6-binding site not Src-binding site for STP-A11-mediated NF-kappa B2 pathway. Blockage of STP-A11-mediated p52 production using siRNA against p52 enhanced a chemotherapeutic drug-mediated cell death, suggesting that p52 production induced by the expression of STP-A11 would contribute to cellular transformation, which results from a resistance to cell death. (c) 2006 Elsevier Inc. All rights reserved.
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