2mxp
Solution structure of NDP52 ubiquitin-binding zinc finger
Structural highlights
FunctionCACO2_HUMAN May play a role in ruffle formation and actin cytoskeleton organization. Seems to negatively regulate constitutive secretion.[1] Publication Abstract from PubMedThe 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. Molecular basis of ubiquitin recognition by the autophagy receptor CALCOCO2.,Xie X, Li F, Wang Y, Wang Y, Lin Z, Cheng X, Liu J, Chen C, Pan L Autophagy. 2015;11(10):1775-89. doi: 10.1080/15548627.2015.1082025. PMID:26506893[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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