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首页> 外文期刊>Cellular Signalling >Epstein-Barr virus latent membrane protein 1 mediates phosphorylation and nuclear translocation of annexin A2 by activating PKC pathway
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Epstein-Barr virus latent membrane protein 1 mediates phosphorylation and nuclear translocation of annexin A2 by activating PKC pathway

机译:爱泼斯坦-巴尔病毒潜伏膜蛋白1通过激活PKC途径介导膜联蛋白A2的磷酸化和核易位

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We have previously combined phosphorylation enrichment with proteomics technology to elucidate the novel phosphoproteins in the signaling pathways triggered by Epstein-Barr virus (EBV)-encoded latent membrane protein 1 (LMP1) and shown that LMP1 can increase the phosphorylation level of annexin A2. Here, we further showed that LMP1 increased the serine, but not tyrosine, phosphorylation of annexin A2 by activating a novel signaling pathway, the protein kinase C (PKC) signaling pathway. However, LMP1 did not affect the level of annexin A2 expression. In addition, we found that LMP1 induced the nuclear entry of annexin A2 in an energy- and temperature-dependent manner, suggesting that the nuclear entry of annexin A2 is an active process. Treatment of LMP1-expressing cells with the PKC inhibitor myr-psi PKC resulted in annexin A2 being present almost exclusively at cell surface, instead of within the nucleus, suggesting that the nuclear entry of annexin A2 was associated with serine phosphorylation mediated by PKC. (c) 2006 Elsevier Inc. All rights reserved.
机译:我们之前已将磷酸化富集与蛋白质组学技术结合起来,阐明了由爱泼斯坦-巴尔病毒(EBV)编码的潜伏膜蛋白1(LMP1)触发的信号传导途径中的新型磷酸化蛋白,并表明LMP1可以增加膜联蛋白A2的磷酸化水平。在这里,我们进一步表明,LMP1通过激活新的信号传导途径,即蛋白激酶C(PKC)信号传导途径,增加了膜联蛋白A2的丝氨酸而非酪氨酸磷酸化。但是,LMP1不会影响膜联蛋白A2表达的水平。此外,我们发现LMP1以能量和温度依赖性方式诱导膜联蛋白A2的核进入,这表明膜联蛋白A2的核进入是一个活跃的过程。用PKC抑制剂myr-psi PKC处理表达LMP1的细胞导致膜联蛋白A2几乎仅存在于细胞表面,而不是存在于细胞核内,这表明膜联蛋白A2的核进入与PKC介导的丝氨酸磷酸化有关。 (c)2006 Elsevier Inc.保留所有权利。

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