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Sci. Signal., 5 February 2013
Vol. 6, Issue 261, p. ra9
[DOI: 10.1126/scisignal.2003730]

RESEARCH ARTICLES

Sterical Hindrance Promotes Selectivity of the Autophagy Cargo Receptor NDP52 for the Danger Receptor Galectin-8 in Antibacterial Autophagy

Sai Li1*, Michal P. Wandel2*, Fudong Li1, Zhonghua Liu1, Chao He1, Jihui Wu1, Yunyu Shi1{dagger}, and Felix Randow2{dagger}

1 Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China.
2 MRC Laboratory of Molecular Biology, Division of Protein and Nucleic Acid Chemistry, Hills Road, Cambridge CB2 0QH, UK.

* These authors contributed equally to this work.

Abstract: Autophagy, the process of lysosome-dependent degradation of cytosolic components, is a mechanism by which cells selectively engulf invading pathogens to protect themselves against infection. Galectin-8, a cytosolic protein with specificity for β-galactoside–containing glycans, binds endosomal and lysosomal membranes that have been damaged, for example, by pathogens, and selectively recruits the autophagy cargo receptor NDP52 to induce autophagy. We solved the crystal structure of the NDP52–galectin-8 complex to show how NDP52 exclusively binds galectin-8 and, consequently, why other galectins do not restrict the growth of Salmonella in human cells.

{dagger} To whom correspondence should be addressed. E-mail: yyshi{at}ustc.edu.cn (Y.S.); randow{at}mrc-lmb.cam.ac.uk (F.R.)

Citation: S. Li, M. P. Wandel, F. Li, Z. Liu, C. He, J. Wu, Y. Shi, F. Randow, Sterical Hindrance Promotes Selectivity of the Autophagy Cargo Receptor NDP52 for the Danger Receptor Galectin-8 in Antibacterial Autophagy. Sci. Signal. 6, ra9 (2013).

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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