Molecular basis of ubiquitin recognition by the autophagy receptor CALCOCO2.
Molecular basis of ubiquitin recognition by the autophagy receptor CALCOCO2.
复制标题
自噬受体 CALCOCO2 识别泛素的分子基础。
DOI：
10.1080/15548627.2015.1082025
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发表时间：
2015
期刊：
影响因子：
13.3
通讯作者：
Pan Lifeng
中科院分区：
文献类型：
--
作者：
Xie Xingqiao;Li Faxiang;Wang Yuanyuan;Wang Yingli;Lin Zhijie;Cheng Xiaofang;Liu Jianping;Chen Changbin;Pan Lifeng
The autophagy receptor CALCOCO2/NDP52 functions as a bridging adaptor and plays an essential role in the selective autophagic degradation of invading pathogens by specifically recognizing ubiquitin-coated intracellular pathogens and subsequently targeting them to the autophagic machinery; thereby it is required for innate immune defense against a range of infectious pathogens in mammals. However, the mechanistic basis underlying CALCOCO2-mediated specific recognition of ubiqutinated pathogens is still unknown. Here, using biochemical and structural analyses, we demonstrated that the cargo-binding region of CALCOCO2 contains a dynamic unconventional zinc finger as well as a C2H2-type zinc-finger, and only the C2H2-type zinc finger specifically recognizes mono-ubiquitin or poly-ubiquitin chains. In addition to elucidating the specific ubiquitin recognition mechanism of CALCOCO2, the structure of the CALCOCO2 C2H2-type zinc finger in complex with mono-ubiquitin also uncovers a unique zinc finger-binding mode for ubiquitin. Our findings provide mechanistic insight into how CALCOCO2 targets ubiquitin-decorated pathogens for autophagic degradations.
