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

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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)

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.

Suggested Citation

  • Byeong-Won Kim & Seung Beom Hong & Jun Hoe Kim & Do Hoon Kwon & Hyun Kyu Song, 2013. "Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8," Nature Communications, Nature, vol. 4(1), pages 1-8, June.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms2606
    DOI: 10.1038/ncomms2606
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    Cited by:

    1. Xinheng He & Lifen Zhao & Yinping Tian & Rui Li & Qinyu Chu & Zhiyong Gu & Mingyue Zheng & Yusong Wang & Shaoning Li & Hualiang Jiang & Yi Jiang & Liuqing Wen & Dingyan Wang & Xi Cheng, 2024. "Highly accurate carbohydrate-binding site prediction with DeepGlycanSite," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    2. Ália dos Santos & Daniel E. Rollins & Yukti Hari-Gupta & Hannah McArthur & Mingxue Du & Sabrina Yong Zi Ru & Kseniia Pidlisna & Ane Stranger & Faeeza Lorgat & Danielle Lambert & Ian Brown & Kevin Howl, 2023. "Autophagy receptor NDP52 alters DNA conformation to modulate RNA polymerase II transcription," Nature Communications, Nature, vol. 14(1), pages 1-24, December.
    3. Shuzhi Cui & Tian Xia & Jianjin Zhao & Xiaoyu Ren & Tingtao Wu & Mireille Kameni & Xiaoju Guo & Li He & Jingao Guo & Aléria Duperray-Susini & Florence Levillayer & Jean-Marc Collard & Jin Zhong & Life, 2023. "NDP52 mediates an antiviral response to hepatitis B virus infection through Rab9-dependent lysosomal degradation pathway," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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