期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 276, 期 22, 页码 19640-19647出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M011028200
关键词
-
We recently reported the identification of a RING finger-containing protein, HHARI (human homologue of Drosophiba ariadne), which binds to the human ubiquitin-conjugating enzyme UbcH7 in vitro, We now demonstrate that HHARI interacts and co-localizes with UbcH7 in mammalian cells, particularly in the perinuclear region, We have further defined a minimal interaction region of HHARI comprising residues 186-254, identified individual amino acid residues essential for the interaction, and determined that the distance between the RING1 finger and IBR (in between RING fingers) domains is critical to maintaining binding. We have also established that the RING1 finger of HHARI cannot be substituted for by the highly homologous RING finger domains of either of the ubiquitin-protein ligase components c-CBL or Parkin, despite their similarity in structure and their independent capabilities to bind UbcH7, Furthermore, mutation of the RING1 finger domain of HHARI from a RING-HC to a RING-HP type abolishes interaction with UbcH7. These studies demonstrate that very subtle changes to the domains that regulate recognition between highly conserved components of the ubiquitin pathway can dramatically affect their ability to interact.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据