Structural highlights
Function
LEG8_HUMAN Lectin with a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans.[1]
Publication Abstract from PubMed
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 beta-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.
Sterical hindrance promotes selectivity of the autophagy cargo receptor NDP52 for the danger receptor galectin-8 in antibacterial autophagy.,Li S, Wandel MP, Li F, Liu Z, He C, Wu J, Shi Y, Randow F Sci Signal. 2013 Feb 5;6(261):ra9. doi: 10.1126/scisignal.2003730. PMID:23386746[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ideo H, Matsuzaka T, Nonaka T, Seko A, Yamashita K. Galectin-8-N-domain recognition mechanism for sialylated and sulfated glycans. J Biol Chem. 2011 Apr 1;286(13):11346-55. Epub 2011 Feb 2. PMID:21288902 doi:10.1074/jbc.M110.195925
- ↑ Li S, Wandel MP, Li F, Liu Z, He C, Wu J, Shi Y, Randow F. Sterical hindrance promotes selectivity of the autophagy cargo receptor NDP52 for the danger receptor galectin-8 in antibacterial autophagy. Sci Signal. 2013 Feb 5;6(261):ra9. doi: 10.1126/scisignal.2003730. PMID:23386746 doi:http://dx.doi.org/10.1126/scisignal.2003730
