【摘 要】
：
The autophagy receptor NDP52 functions as a bridging adaptor and plays an essential role in the selective autophagic degradation of invaded pathogens by spe
【机 构】
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StateKeyLaboratoryofBioorganicChemistry,ShanghaiInstituteofOrganicChemistry,ChineseAcademyofSciences
【出 处】
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The 7th International Symposium on Autophagy 2015(第七届自噬国际研讨会
论文部分内容阅读
The autophagy receptor NDP52 functions as a bridging adaptor and plays an essential role in the selective autophagic degradation of invaded 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 NDP52-mediated specific recognition of ubiqutinated pathogens is still unknown.Here, using biochemical and structural analyses, we demonstrated that the cargo-binding region of NDP52 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 NDP52, the structure of the NDP52 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 NDP52 targets ubiquitin-decorated pathogens for autophagic degradations.
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