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Goldoni, S., Humphries, A., Nyström, A., Sattar, S., Owens, R.T., McQuillan, D.J., Ireton, K., and Iozzo, R.V. 2009. Decorin is a novel antagonistic ligand of the Met receptor. J. Cell Biol. 185:743-754.
This paper provided a major contribution to the field of proteoglycan signaling and receptor biology by identifying decorin as the only known antagonistic ligand of the Met receptor. It also classifies Met as the primary receptor for decorin-mediated bioactivities. This article was selected by the Faculty of 1000.
Buraschi, S., Neill, T., Goyal, A., Poluzzi, C., Smythies, J., Owens, R.T, Schaefer, L., Torres, A. and Iozzo, R.V. 2013. Decorin causes autophagy in endothelial cells via Peg3. Proc. Natl. Acad. Sci. USA 110: E2582-E2591
Discovery that decorin evokes a protracted autophagic program in endothelial cells downstream of VEGFR2 and a poorly understood tumor suppressor gene known as Peg3. We found that Peg3 is required for decorin evoked autophagy and functions to maintain basal levels of Beclin 1, a major autophagic regulator. This discovery represents a major contribution to the field of proteoglycans demonstrating one of their core properties is autophagic regulation. This article was selected by the Faculty of 1000.
Poluzzi, C., Casulli, J., Goyal, A., Mercer, T.J., Neill, T., and Iozzo, R.V. 2014. Endorepellin evokes autophagy in endothelial cells. J.Biol. Chem. 289:1614-1628.
This paper identifies that endorepellin, the C-terminal cleavage fragment of perlecan, evokes autophagy in endothelial cells via VEGFR2 and Peg3. This article continues the emergent properties of matrix-derived molecules as being autophagic effectors. This article was selected by the Faculty of 1000.
Gubbiotti, M.A., Neill, T., Frey, H., Schaefer, L., and Iozzo, R.V. 2015. Decorin is an autophagy-inducible proteoglycan and is required for proper in vivo autophagy. Matrix Biol. 48:14-25.
Decorin not only evokes autophagy, but decorin itself is an autophagy-inducible gene. Moreover, decorin knockout mice have impaired autophagic responses and flux.
Neill, T., Buraschi, S., Goyal, A., Sharpe, C., Natkanski, E., Schaefer, L., Morrione, A., and Iozzo, R.V. 2016. EphA2 is a functional receptor for the growth factor progranulin. J. Cell Biol. 15:687-703.
A functional receptor for the growth factor progranulin has remained elusive for several decades. Here, we identify EphA2 as an authentic and functional signaling receptor for progranulin. We found that EphA2 coordinates progranulin-mediated activation of MAPK and Akt. EphA2 was also required for progranulin-mediated capillary morphogenesis as well as progranulin auto-regulation.