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Sterical hindrance promotes selectivity of the autophagy cargo receptor NDP52 for the danger receptor galectin-8 in anti-bacterial autophagy
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 lectin with specificity for β-galactosides, binds endosomal and lysosomal membranes t...
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Published in: | Science signaling 2013-02, Vol.6 (261), p.ra9-ra9 |
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Main Authors: | , , , , , , , |
Format: | Article |
Language: | English |
Online Access: | Get full text |
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Summary: | 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 lectin with specificity for β-galactosides, binds endosomal and lysosomal membranes that have been damaged, for example by pathogens, and selectively recruits the autophagy cargo receptor NDP52 to induce autophagy. Here, 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. |
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ISSN: | 1937-9145 |
DOI: | 10.1126/scisignal.2003730 |