文献知网节
  • 记笔记
摘要:The cellular endosomal sorting complex required for transport(ESCRT)was recently found to mediate important morphogenesis processes at the nuclear envelope(NE).We previously showed that the Epstein-Barr virus(EBV)BFRF1 protein recruits the ESCRT-associated protein Alix to modulate NE structure and promote EBV nuclear egress.Here,we uncover new cellular factors and mechanisms involved in this process.BFRF1-induced NE vesicles are similar to those observed following EBV reactivation.BFRF1 is ubiquitinated and elimination of ubiquitination with either lysine mutations or fusion of a de-ubiquitinase hampers NE-derived vesicle formation and virus maturation.BFRF1 selectively binds the ubiquitin ligase Itch through a.a.181-313 sequence.Itch associates with an Alix-BFRF1 complex and is required for BFRF1-induced nucleocytoplasmic transport of EBV genomes.Our data demonstrate that Itch,ubiquitin and Alix control the BFRF1-mediated modulation of the NE and EBV maturation,uncovering novel regulatory mechanisms of ESCRT-induced nuclear egress of viral nucleocapsids.
会议名称:

2016 Membrane Shaping and Remodeling by Proteins(MSRP) Conference

会议时间:

2016-05-19

会议地点:

中国四川成都

  • 专辑:

    基础科学

  • 专题:

    生物学

  • 分类号:

    Q939.4

  • 手机阅读
    即刻使用手机阅读
    第一步

    扫描二维码下载

    "移动知网-全球学术快报"客户端

    第二步

    打开“全球学术快报”

    点击首页左上角的扫描图标

    第三步

    扫描二维码

    手机同步阅读本篇文献

  • HTML阅读
  • CAJ下载
  • PDF下载

下载手机APP用APP扫此码同步阅读该篇文章

下载:3 页码:37 页数:1 大小:146k

引文网络
  • 参考文献
  • 引证文献
  • 共引文献
  • 同被引文献
  • 二级参考文献
  • 二级引证文献
  • 批量下载
相关推荐
  • 相似文献
  • 读者推荐
  • 相关基金文献
  • 相关法规
  • 关联作者
  • 相关视频