爱泼斯坦-巴尔病毒转化蛋白LMP1与肿瘤坏死因子受体家族的信号蛋白结合。
The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family.
作者信息
Mosialos G, Birkenbach M, Yalamanchili R, VanArsdale T, Ware C, Kieff E
机构信息
Department of Medicine, Harvard Medical School, Boston, Massachusetts 02115.
出版信息
Cell. 1995 Feb 10;80(3):389-99. doi: 10.1016/0092-8674(95)90489-1.
The cytoplasmic C-terminus of Epstein-Barr virus (EBV) latent infection membrane protein 1 (LMP1) is essential for B lymphocyte growth transformation and is now shown to interact with a novel human protein (LMP1-associated protein 1 [LAP1]). LAP1 is homologous to a murine protein, tumor necrosis factor receptor-associated factor 2 (TRAF2), implicated in growth signaling from the p80 TNFR. A second novel protein (EBI6), induced by EBV infection, is the human homolog of a second murine TNFR-associated protein (TRAF1). LMP1 expression causes LAP1 and EBI6 to localize to LMP1 clusters in lymphoblast plasma membranes, and LMP1 coimmunoprecipitates with these proteins. LAP1 binds to the p80 TNFR, CD40, and the lymphotoxin-beta receptor, while EBI6 associates with the p80 TNFR. The interaction of LMP1 with these TNFR family-associated proteins is further evidence for their role in signaling and links LMP1-mediated transformation to signal transduction from the TNFR family.
爱泼斯坦-巴尔病毒（EBV）潜伏感染膜蛋白1（LMP1）的胞质C末端对于B淋巴细胞生长转化至关重要，现已证明它能与一种新型人类蛋白（LMP1相关蛋白1 [LAP1]）相互作用。LAP1与一种小鼠蛋白肿瘤坏死因子受体相关因子2（TRAF2）同源，TRAF2参与p80肿瘤坏死因子受体（TNFR）的生长信号传导。EBV感染诱导产生的另一种新型蛋白（EBI6）是另一种小鼠TNFR相关蛋白（TRAF1）的人类同源物。LMP1的表达导致LAP1和EBI6定位于淋巴母细胞膜中的LMP1簇，并且LMP1与这些蛋白进行共免疫沉淀。LAP1与p80 TNFR、CD40以及淋巴毒素-β受体结合，而EBI6与p80 TNFR相关联。LMP1与这些TNFR家族相关蛋白的相互作用进一步证明了它们在信号传导中的作用，并将LMP1介导的转化与TNFR家族的信号转导联系起来。
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