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, Hyun Kyu Song

Research output: Contribution to journalArticle

43 Citations (Scopus)

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.

Original languageEnglish
Article number1613
JournalNature Communications
Volume4
DOIs
Publication statusPublished - 2013 Apr 11

Fingerprint

Galectins
sugars
Sugars
carbohydrates
nicotinamide
Autophagy
pathogens
adenines
determinants
bacteria
upstream
peptides
molecules
Carbohydrates
Molecules
Pathogens
crystal structure
NAD
cells
Bacteria

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Chemistry(all)
  • Physics and Astronomy(all)

Cite this

Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8. / Kim, Byeong Won; Beom Hong, Seung; Hoe Kim, Jun; Hoon Kwon, Do; Song, Hyun Kyu.

In: Nature Communications, Vol. 4, 1613, 11.04.2013.

Research output: Contribution to journalArticle

Kim, Byeong Won ; Beom Hong, Seung ; Hoe Kim, Jun ; Hoon Kwon, Do ; Song, Hyun Kyu. / Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8. In: Nature Communications. 2013 ; Vol. 4.
@article{512176c55d3f48eeb3327e4e023e55fc,
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.",
author = "Kim, {Byeong Won} and {Beom Hong}, Seung and {Hoe Kim}, Jun and {Hoon Kwon}, Do and Song, {Hyun Kyu}",
year = "2013",
month = "4",
day = "11",
doi = "10.1038/ncomms2606",
language = "English",
volume = "4",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",

}

TY - JOUR

T1 - Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8

AU - Kim, Byeong Won

AU - Beom Hong, Seung

AU - Hoe Kim, Jun

AU - Hoon Kwon, Do

AU - Song, Hyun Kyu

PY - 2013/4/11

Y1 - 2013/4/11

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84875908545&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84875908545&partnerID=8YFLogxK

U2 - 10.1038/ncomms2606

DO - 10.1038/ncomms2606

M3 - Article

C2 - 23511477

AN - SCOPUS:84875908545

VL - 4

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 1613

ER -