Molecular basis of ubiquitin recognition by the autophagy receptor CALCOCO2.
Shanghai, China. In Autophagy, Nov 2015
The autophagy receptor CALCOCO2/NDP52 functions as a bridging adaptor and plays an essential role in the selective autophagic degradation of invading pathogens by specifically recognizing ubiquitin-coated intracellular pathogens and subsequently targeting them to the autophagic machinery; thereby it is required for innate immune defense against a range of infectious pathogens in mammals.
Emerging themes in bacterial autophagy.
Toronto, Canada. In Curr Opin Microbiol, Feb 2015
We review the importance of bacterial targeting by ubiquitination, diacylglycerol (DAG) or proteins such as Nod1, Nod2, NDP52, p62, NBR1, optineurin, LRSAM1 and parkin in the process of xenophagy.
Dual function of CALCOCO2/NDP52 during xenophagy.
Lyon, France. In Autophagy, 2014
In infected cells, the autophagy receptor CALCOCO2/NDP52 targets Salmonella Typhimurium to the phagophore membrane by concomitantly interacting with LC3C and binding to ubiquitinated cytosolic bacteria or to LGALS8/GALECTIN 8 adsorbed on damaged vacuoles that contain bacteria.
Myosin VI and its cargo adaptors - linking endocytosis and autophagy.
Cambridge, United Kingdom. In J Cell Sci, 2013
In addition, myosin VI has been shown to be a regulator of the autophagy pathway, because of its ability to link the endocytic and autophagic pathways through interactions with the ESCRT-0 protein Tom1 and the autophagy adaptor proteins T6BP, NDP52 and optineurin.
The role of 'eat-me' signals and autophagy cargo receptors in innate immunity.
Cambridge, United Kingdom. In Curr Opin Microbiol, 2013
The autophagy cargo receptors p62, NDP52 and Optineurin detect incoming bacteria that have become associated with specific 'eat-me' signals such as Galectin-8 and poly-ubiquitin and feed them into the autophagy pathway via interactions with phagophore-associated ATG8-like proteins.
Selective autophagy degrades DICER and AGO2 and regulates miRNA activity.
Zürich, Switzerland. In Nat Cell Biol, 2012
Here, we show that the miRNA-processing enzyme, DICER (also known as DICER1), and the main miRNA effector, AGO2 (also known as eukaryotic translation initiation factor 2C, 2 (EIF2C2)), are targeted for degradation as miRNA-free entities by the selective autophagy receptor NDP52 (also known as calcium binding and coiled-coil domain 2 (CALCOCO2)).