ASIA unversity:Item 310904400/8201
English  |  正體中文  |  简体中文  |  全文笔数/总笔数 : 93288/109022 (86%)
造访人次 : 20900355      在线人数 : 268
RC Version 6.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
搜寻范围 查询小技巧:
  • 您可在西文检索词汇前后加上"双引号",以获取较精准的检索结果
  • 若欲以作者姓名搜寻,建议至进阶搜寻限定作者字段,可获得较完整数据
  • 进阶搜寻


    题名: Phosphorylation of ARD1 by IKK beta contributes to its destabilization and degradation
    作者: Hsu-Ping Kuo;Dung-Fang Lee;Weiya Xia;Chien-Chen Lai;Long-Yuan Li;Mien-Chie Hung
    贡献者: Department of Biotechnology
    关键词: Phosphorylation;Arrest-defective protein 1;I kappa B kinase beta
    日期: 2009-11
    上传时间: 2010-03-26 10:28:59 (UTC+8)
    出版者: Asia University
    摘要: I kappa B kinase beta (IKK beta), a major kinase downstream of various proinflammatory signals, mediates multiple cellular functions through phosphorylation and regulation of its substrates. On the basis of protein sequence analysis, we identified arrest-defective protein 1 (ARD1), a protein involved in apoptosis and cell proliferation processes in many human cancer cells, as a new IKK beta substrate. We provided evidence showing that ARD1 is indeed a bona. de substrate of IKK beta. IKK beta physically associated with ARD1 and phosphorylated it at Ser209. Phosphorylation by IKK beta destabilized ARD1 and induced its proteasome-mediated degradation. Impaired growth suppression was observed in ARD1 phosphorylation-mimic mutant (S209E)-transfected cells as compared with ARD1 non-phosphorylatable mutant (S209A)-transfected cells. Our findings of molecular interactions between ARD1 and IKK beta may enable further understanding of the upstream regulation mechanisms of ARD1 and of the diverse functions of IKK beta. (C) 2009 Elsevier Inc. All rights reserved.
    显示于类别:[生物科技學系] 期刊論文


    档案 描述 大小格式浏览次数
    17.doc51KbMicrosoft Word432检视/开启


    DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - 回馈