Listeria monocytogenes ActA-mediated escape from autophagic recognition
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Williams, A. et al. Aggregate-prone proteins are cleared from the cytosol by autophagy: therapeutic implications. Curr. Top. Dev. Biol. 76, 89–101 (2006).
Deretic, V. & Levine, B. Autophagy, immunity, and microbial adaptations. Cell Host Microbe. 5, 527–549 (2009).
Py, B. F., Lipinski, M. M. & Yuan, J. Autophagy limits Listeria monocytogenes intracellular growth in the early phase of primary infection. Autophagy 3, 117–125 (2007).
Birmingham, C. L. et al. Listeria monocytogenes evades killing by autophagy during colonization of host cells. Autophagy 3, 442–451 (2007).
Ikeda, H. et al. Expanded polyglutamine in the Machado-Joseph disease protein induces cell death in vitro and in vivo. Nature Genet. 13, 196–202 (1996).
Fu, L. et al. Nuclear aggresomes form by fusion of PML-associated aggregates. Mol. Biol. Cell 16, 4905–4917 (2005).
Klionsky, D. J. & Emr, S. D. Autophagy as a regulated pathway of cellular degradation. Science 290, 1717–1721 (2000).
Nakagawa, I. et al. Autophagy defends cells against invading group A Streptococcus. Science 306, 1037–1040 (2004).
Gutierrez, M. G. et al. Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages. Cell 119, 753–766 (2004).
Deretic, V. et al. Mycobacterium tuberculosis inhibition of phagolysosome biogenesis and autophagy as a host defence mechanism. Cell. Microbiol. 8, 719–727 (2006).
Otto, G. P. et al. Macroautophagy is dispensable for intracellular replication of Legionella pneumophila in Dictyostelium discoideum. Mol. Microbiol. 51, 63–72 (2004).
Gutierrez, M. G. et al. Autophagy induction favours the generation and maturation of the Coxiella-replicative vacuoles. Cell. Microbiol. 7, 981–993 (2005).
Dorn, B. R., Dunn, W. A., Jr. & Progulske-Fox, A. Porphyromonas gingivalis traffics to autophagosomes in human coronary artery endothelial cells. Infect. Immun. 69, 5698–5708 (2001).
Kocks, C. et al. L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein. Cell 68, 521–531 (1992).
Stevens, J. M., Galyov, E. E. & Stevens, M. P. Actin-dependent movement of bacterial pathogens. Nature Rev. Microbiol. 4, 91–101 (2006).
Rich, K. A., Burkett, C. & Webster, P. Cytoplasmic bacteria can be targets for autophagy. Cell. Microbiol. 5, 455–468 (2003).
Birmingham, C. L. et al. Listeriolysin O allows Listeria monocytogenes replication in macrophage vacuoles. Nature 451, 350–354 (2008).
Welch, M. D., Iwamatsu, A. & Mitchison, T. J. Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. Nature 385, 265–269 (1997).
Chakraborty, T. et al. A focal adhesion factor directly linking intracellularly motile Listeria monocytogenes and Listeria ivanovii to the actin-based cytoskeleton of mammalian cells. EMBO J. 14, 1314–1321 (1995).
Footer, M. J., Lyo, J. K. & Theriot, J. A. Close packing of Listeria monocytogenes ActA, a natively unfolded protein, enhances F-actin assembly without dimerization. J. Biol. Chem. 283, 23852–23862 (2008).
Portnoy, D. A., Chakraborty, T., Goebel, W. & Cossart, P. Molecular determinants of Listeria monocytogenes pathogenesis. Infect. Immun. 60, 1263–1267 (1992).
Pistor, S. et al. Mutations of arginine residues within the 146-KKRRK-150 motif of the ActA protein of Listeria monocytogenes abolish intracellular motility by interfering with the recruitment of the Arp2/3 complex. J. Cell Sci. 113 (Pt 18), 3277–3287 (2000).
Kuma, A. et al. The role of autophagy during the early neonatal starvation period. Nature 432, 1032–1036 (2004).
Bjorkoy, G. et al. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J. Cell Biol. 171, 603–614 (2005).
Komatsu, M. et al. Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice. Cell 131, 1149–1163 (2007).
Gal, J., Strom, A. L., Kilty, R., Zhang, F. & Zhu, H. p62 accumulates and enhances aggregate formation in model systems of familial amyotrophic lateral sclerosis. J. Biol. Chem. 282, 11068–11077 (2007).
Pankiv, S. et al. p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitylated protein aggregates by autophagy. J. Biol. Chem. 282, 24131–24145 (2007).
Long, J. et al. Ubiquitin recognition by the UBA domain of p62 involves a novel conformational switch. J. Biol. Chem. 283, 5427–5440 (2008).
Van Troys, M. et al. The actin propulsive machinery: the proteome of Listeria monocytogenes tails. Biochem. Biophys. Res. Commun. 375, 194–199 (2008).