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首页> 外文期刊>EMBO Journal >CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein
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CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein

机译：芯片是chaperone-dependent E3连接酶ubiquitylates展开的蛋白质

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摘要

The ubiquitin-proteasome system catalyses the immediate destruction of misfolded or impaired proteins generated in cells, but how this proteolytic machinery recognizes abnormality of cellular proteins for selective elimination remains elusive. Here, we report that the C-terminus of Hsc70-interacting protein (CHIP) with a U-box domain is an E3 ubiquitin-ligase collaborating with molecular chaperones Hsp90 and 1 Hsc70. Thermally denatured firefly luciferase was multiubiquitylated by CHIP in the presence of E1 and E2 (Ubc4 or UbcH5c) in vitro, only when the unfolded substrate was captured by Hsp90 or Hsc70 and Hsp40. No ubiquitylating activity was detected in CHIP lacking the U-box region. CHIP efficiently ubiquitylated denatured luciferase trapped by the C-terminal region of Hsp90, which contains a CHIP binding site. CHIP also showed self-ubiquitylating activity independent of target ubiquitylation. Our results indicate that CHIP can be regarded as 'a quality-control E3' that selectively ubiquitylates unfolded protein(s) by collaborating with molecular chaperones.
机译：ubiquitin-proteasome体系催化作用立即销毁错误折叠或受损细胞内蛋白质生成,但如何蛋白水解机器识别异常的细胞蛋白质选择性消除仍然是难以捉摸的。糖基的Hsc70-interacting蛋白(芯片)域是一个E3 ubiquitin-ligase U-box与分子伴侣’以及合作1 Hsc70。是由芯片multiubiquitylated的存在吗E1和E2 (Ubc4或UbcH5c)体外,只有当展开基体由一半或被捕Hsc70 Hsp40。在芯片缺乏U-box地区检测到。有效ubiquitylated变性荧光素酶的一半被c端地区包含一个芯片结合位点。self-ubiquitylating活动独立于目标ubiquitylation。芯片可以被视为“质量控制E3”,有选择地ubiquitylates展开蛋白(s)与分子合作监护人。

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