Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8

Byeong-Won Kim, Seung Beom Hong, Jun Hoe Kim, Do Hoon Kwon and Hyun Kyu Song ()
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Byeong-Won Kim: School of Life Sciences and Biotechnology, Korea University, Anam-Dong, Seongbuk-Gu
Seung Beom Hong: School of Life Sciences and Biotechnology, Korea University, Anam-Dong, Seongbuk-Gu
Jun Hoe Kim: School of Life Sciences and Biotechnology, Korea University, Anam-Dong, Seongbuk-Gu
Do Hoon Kwon: School of Life Sciences and Biotechnology, Korea University, Anam-Dong, Seongbuk-Gu
Hyun Kyu Song: School of Life Sciences and Biotechnology, Korea University, Anam-Dong, Seongbuk-Gu

Nature Communications, 2013, vol. 4, issue 1, 1-8

Abstract: 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.

Date: 2013
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DOI: 10.1038/ncomms2606

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