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


Editor's Summary

Targeting Salmonella for Degradation
Salmonella infection damages host intracellular vesicle membranes, which exposes carbohydrates that are detected by galectins. Galectin-8 selectively recruits the cargo receptor NDP52 to stimulate autophagy, a process of intracellular degradation, of the damaged vesicular structures and associated bacteria. Li et al. solved the crystal structure of the binding domain of NDP52 in complex with the carbohydrate recognition domain of galectin-8. NDP52 formed a hooklike structure that bound to a hydrophobic pocket on galectin-8. Two adjacent amino acids in this pocket were critical for binding to NDP52. Amino acids in these positions were altered in other galectins, thereby explaining the selectivity of NDP52 for galectin-8 and how galectin-8 activates autophagy in Salmonella-infected cells.

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).

Read the Full Text

Cellular Self-Defense: How Cell-Autonomous Immunity Protects Against Pathogens.
F. Randow, J. D. MacMicking, and L. C. James (2013)
Science 340, 701-706
   Abstract »    Full Text »    PDF »
Science Signaling Podcast: 5 February 2013.
F. Randow and A. M. VanHook (2013)
Science Signaling 6, pc4
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