title: Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8.
abstract: Infectious bacteria are cleared from mammalian cells by host autophagy in combination with other upstream cellular components, such as the autophagic receptor NDP52 and sugar receptor galectin-8. However, the detailed molecular basis of the interaction between these two receptors remains to be elucidated. Here, we report the biochemical characterization of both NDP52 and galectin-8 as well as the crystal structure of galectin-8 complexed with an NDP52 peptide. The unexpected observation of nicotinamide adenine dinucleotide located at the carbohydrate-binding site expands our knowledge of the sugar-binding specificity of galectin-8. The NDP52-galectin-8 complex structure explains the key determinants for recognition on both receptors and defines a special orientation of N- and C-terminal carbohydrate recognition domains of galectin-8. Dimeric NDP52 forms a ternary complex with two monomeric galectin-8 molecules as well as two LC3C molecules. These results lay the groundwork for understanding how host cells target bacterial pathogens for autophagy.
authors.affiliation: Division of Life Sciences, School of Life Sciences and Biotechnology, Korea University, Anam-Dong, Seongbuk-Gu, Seoul, Korea.
authors.forename: Byeong-Won
authors.initials: BW
authors.lastname: Kim
authors.forename: Seung Beom
authors.initials: SB
authors.lastname: Hong
authors.forename: Jun Hoe
authors.initials: JH
authors.lastname: Kim
authors.forename: Do Hoon
authors.initials: DH
authors.lastname: Kwon
authors.forename: Hyun Kyu
authors.initials: HK
authors.lastname: Song
mesh_terms: D000595:Amino Acid Sequence; D001343:Autophagy; D018360:Crystallography, X-Ray; D019281:Dimerization; D004591:Electrophoresis, Polyacrylamide Gel; D037161:Galectins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016296:Mutagenesis; D009243:NAD; D009687:Nuclear Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
chemical_list: C094297:CALCOCO2 protein, human; D037161:Galectins; D009687:Nuclear Proteins; D009243:NAD