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. 2010 Feb;6(2):288-9.
doi: 10.4161/auto.6.2.11118. Epub 2010 Feb 4.

NDP52, a novel autophagy receptor for ubiquitin-decorated cytosolic bacteria

Natalia von Muhlinen  1 , Teresa Thurston, Grigory Ryzhakov, Stuart Bloor, Felix Randow
Affiliations

NDP52, a novel autophagy receptor for ubiquitin-decorated cytosolic bacteria

Natalia von Muhlinen et al. Autophagy. 2010 Feb.

Abstract

Autophagy functions as a cell-autonomous effector mechanism of innate immunity by separating bacteria from cytosolic resources and delivering them for lysosomal destruction. How cytosolic bacteria are targeted for autophagy is incompletely understood. We recently discovered that Salmonella enterica serotype Typhimurium and Streptococcus pyogenes are detected by NDP52 (nuclear dot protein 52 kDa), after these bacteria enter the cytosol of human cells and become decorated with polyubiquitinated proteins. NDP52 binds the bacterial ubiquitin coat as well as ATG8/LC3 and delivers cytosolic bacteria into autophagosomes. In the absence of NDP52 ubiquitin-coated bacteria accumulate outside ATG8/LC3(+) autophagosomes. Cells lacking NDP52 fail to restrict bacterial proliferation, as do cells depleted of TBK1, an IKK family kinase colocalizing with NDP52 at the bacterial surface. Our findings demonstrate the existence of a receptor for the selective autophagy of cytosolic bacteria, suggesting that cells are able to differentiate between antibacterial and other forms of autophagy.

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