Pathogen–endoplasmic-reticulum interactions: in through the out door (original) (raw)
Bonifacino, J. S. & Glick, B. S. The mechanisms of vesicle budding and fusion. Cell116, 153–166 (2004). CASPubMed Google Scholar
Altan-Bonnet, N., Sougrat, R. & Lippincott-Schwartz, J. Molecular basis for Golgi maintenance and biogenesis. Curr. Opin. Cell Biol.16, 364–372 (2004). CASPubMed Google Scholar
Barlowe, C. et al. COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum. Cell77, 895–907 (1994). CASPubMed Google Scholar
Roberg, K. J., Crotwell, M., Espenshade, P., Gimeno, R. & Kaiser, C. A. LST1 is a SEC24 homologue used for selective export of the plasma membrane ATPase from the endoplasmic reticulum. J. Cell Biol.145, 659–672 (1999). CASPubMedPubMed Central Google Scholar
Shimoni, Y. et al. Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae. J. Cell Biol.151, 973–984 (2000). CASPubMedPubMed Central Google Scholar
Mironov, A. A. et al. ER-to-Golgi carriers arise through direct en bloc protrusion and multistage maturation of specialized ER exit domains. Dev. Cell5, 583–594 (2003). CASPubMed Google Scholar
Garcia-Mata, R., Szul, T., Alvarez, C. & Sztul, E. ADP-ribosylation factor/COPI-dependent events at the endoplasmic reticulum–Golgi interface are regulated by the guanine nucleotide exchange factor GBF1. Mol. Biol. Cell14, 2250–2261 (2003). CASPubMedPubMed Central Google Scholar
Gagnon, E. et al. Endoplasmic reticulum-mediated phagocytosis is a mechanism of entry into macrophages. Cell110, 119–131 (2002). This article indicates that the ER membrane seems to become involved with phagocytic events at a very early stage and fuses with the phagocytic cup, leaving ER proteins orientated to the inner face of the phagosome. CASPubMed Google Scholar
Muller-Taubenberger, A. et al. Calreticulin and calnexin in the endoplasmic reticulum are important for phagocytosis. EMBO J.20, 6772–6782 (2001). CASPubMedPubMed Central Google Scholar
Becker, T., Volchuk, A. & Rothman, J. E. Differential use of endoplasmic reticulum membrane for phagocytosis in J774 macrophages. Proc. Natl Acad. Sci. USA102, 4022–4026 (2005). CASPubMedPubMed Central Google Scholar
Touret, N. et al. Quantitative and dynamic assessment of the contribution of the endoplasmic reticulum to phagosome formation. Cell123, 157–170 (2005). This article highlights that the plasma membrane is the main constituent of nascent phagosomes, which then fuse with endosomes and, eventually, with lysosomes to become degradative organelles. CASPubMed Google Scholar
Houde, M. et al. Phagosomes are competent organelles for antigen cross-presentation. Nature425, 402–406 (2003). CASPubMed Google Scholar
Guermonprez, P. et al. ER–phagosome fusion defines an MHC class I cross-presentation compartment in dendritic cells. Nature425, 397–402 (2003). The phagosomes of DCs are organelles in which MHC class I molecules can be loaded with peptides that have been added exogenously. This article confirms the capacity of these phagosomes to carry out cross-presentation. CASPubMed Google Scholar
Desjardins, M. ER-mediated phagocytosis: a new membrane for new functions. Nature Rev. Immunol.3, 280–291 (2003). CAS Google Scholar
Watts, C. & Amigorena, S. Phagocytosis and antigen presentation. Semin. Immunol.13, 373–379 (2001). CASPubMed Google Scholar
Sandvig, K. & van Deurs, B. Membrane traffic exploited by protein toxins. Annu. Rev. Cell Dev. Biol.18, 1–24 (2002). CASPubMed Google Scholar
Vieira, O. V., Botelho, R. J. & Grinstein, S. Phagosome maturation: aging gracefully. Biochem. J.366, 689–704 (2002). CASPubMedPubMed Central Google Scholar
Gremion, C. & Cerny, A. Hepatitis C virus and the immune system: a concise review. Rev. Med. Virol.15, 235–268 (2005). PubMed Google Scholar
El-Hage, N. & Luo, G. Replication of hepatitis C virus RNA occurs in a membrane-bound replication complex containing nonstructural viral proteins and RNA. J. Gen. Virol.84, 2761–2769 (2003). CASPubMed Google Scholar
Moradpour, D. et al. Membrane association of hepatitis C virus nonstructural proteins and identification of the membrane alteration that harbors the viral replication complex. Antiviral Res.60, 103–109 (2003). CASPubMed Google Scholar
Aizaki, H., Lee, K. J., Sung, V. M., Ishiko, H. & Lai, M. M. Characterization of the hepatitis C virus RNA replication complex associated with lipid rafts. Virology324, 450–461 (2004). CASPubMed Google Scholar
Egger, D. et al. Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex. J. Virol.76, 5974–5984 (2002). CASPubMedPubMed Central Google Scholar
Pavio, N., Romano, P. R., Graczyk, T. M., Feinstone, S. M. & Taylor, D. R. Protein synthesis and endoplasmic reticulum stress can be modulated by the hepatitis C virus envelope protein E2 through the eukaryotic initiation factor 2α kinase PERK. J. Virol.77, 3578–3585 (2003). CASPubMedPubMed Central Google Scholar
Tardif, K. D., Waris, G. & Siddiqui, A. Hepatitis C virus, ER stress, and oxidative stress. Trends Microbiol.13, 159–163 (2005). CASPubMed Google Scholar
Waris, G., Tardif, K. D. & Siddiqui, A. Endoplasmic reticulum (ER) stress: hepatitis C virus induces an ER–nucleus signal transduction pathway and activates NF-κB and STAT-3. Biochem. Pharmacol.64, 1425–1430 (2002). CASPubMed Google Scholar
Gale, M. J. Jr. et al. Evidence that hepatitis C virus resistance to interferon is mediated through repression of the PKR protein kinase by the nonstructural 5A protein. Virology230, 217–227 (1997). CASPubMed Google Scholar
Taylor, D. R., Shi, S. T., Romano, P. R., Barber, G. N. & Lai, M. M. Inhibition of the interferon-inducible protein kinase PKR by HCV E2 protein. Science285, 107–110 (1999). CASPubMed Google Scholar
Konan, K. V. et al. Nonstructural protein precursor NS4A/B from hepatitis C virus alters function and ultrastructure of host secretory apparatus. J. Virol.77, 7843–7855 (2003). CASPubMedPubMed Central Google Scholar
Rust, R. C. et al. Cellular COPII proteins are involved in production of the vesicles that form the poliovirus replication complex. J. Virol.75, 9808–9818 (2001). CASPubMedPubMed Central Google Scholar
Doedens, J. R. & Kirkegaard, K. Inhibition of cellular protein secretion by poliovirus proteins 2B and 3A. EMBO J.14, 894–907 (1995). CASPubMedPubMed Central Google Scholar
Doedens, J. R., Giddings, T. H. Jr. & Kirkegaard, K. Inhibition of endoplasmic reticulum-to-Golgi traffic by poliovirus protein 3A: genetic and ultrastructural analysis. J. Virol.71, 9054–9064 (1997). CASPubMedPubMed Central Google Scholar
Deitz, S. B., Dodd, D. A., Cooper, S., Parham, P. & Kirkegaard, K. MHC I-dependent antigen presentation is inhibited by poliovirus protein 3A. Proc. Natl Acad. Sci. USA97, 13790–13795 (2000). CASPubMedPubMed Central Google Scholar
Neznanov, N. et al. Poliovirus protein 3A inhibits tumor necrosis factor (TNF)-induced apoptosis by eliminating the TNF receptor from the cell surface. J. Virol.75, 10409–10420 (2001). CASPubMedPubMed Central Google Scholar
Dodd, D. A., Giddings, T. H. Jr. & Kirkegaard, K. Poliovirus 3A protein limits interleukin-6 (IL-6), IL-8, and β interferon secretion during viral infection. J. Virol.75, 8158–8165 (2001). CASPubMedPubMed Central Google Scholar
Choe, S. S., Dodd, D. A. & Kirkegaard, K. Inhibition of cellular protein secretion by picornaviral 3A proteins. Virology337, 18–29 (2005). CASPubMed Google Scholar
Wessels, E., Duijsings, D., Notebaart, R. A., Melchers, W. J. & van Kuppeveld, F. J. A proline-rich region in the coxsackievirus 3A protein is required for the protein to inhibit endoplasmic reticulum-to-Golgi transport. J. Virol.79, 5163–5173 (2005). CASPubMedPubMed Central Google Scholar
Hewitt, E. W. The MHC class I antigen presentation pathway: strategies for viral immune evasion. Immunology110, 163–169 (2003). CASPubMedPubMed Central Google Scholar
Lybarger, L., Wang, X., Harris, M. & Hansen, T. H. Viral immune evasion molecules attack the ER peptide-loading complex and exploit ER-associated degradation pathways. Curr. Opin. Immunol.17, 71–78 (2005). CASPubMed Google Scholar
Ahn, K. et al. Human cytomegalovirus inhibits antigen presentation by a sequential multistep process. Proc. Natl Acad. Sci. USA93, 10990–10995 (1996). CASPubMedPubMed Central Google Scholar
Park, B. et al. Human cytomegalovirus inhibits tapasin-dependent peptide loading and optimization of the MHC class I peptide cargo for immune evasion. Immunity20, 71–85 (2004). This paper shows that the human CMV protein US3 interferes with the tapasin-mediated optimization of peptide binding to MHC class I molecules in the ER. CASPubMed Google Scholar
Hegde, N. R. et al. Inhibition of HLA-DR assembly, transport, and loading by human cytomegalovirus glycoprotein US3: a novel mechanism for evading major histocompatibility complex class II antigen presentation. J. Virol.76, 10929–10941 (2002). CASPubMedPubMed Central Google Scholar
Binder, E. M. & Kim, K. Location, location, location: trafficking and function of secreted proteases of Toxoplasma and Plasmodium. Traffic5, 914–924 (2004). CASPubMed Google Scholar
Mordue, D. G. & Sibley, L. D. Intracellular fate of vacuoles containing Toxoplasma gondii is determined at the time of formation and depends on the mechanism of entry. J. Immunol.159, 4452–4459 (1997). CASPubMed Google Scholar
Mordue, D. G., Hakansson, S., Niesman, I. & Sibley, L. D. Toxoplasma gondii resides in a vacuole that avoids fusion with host cell endocytic and exocytic vesicular trafficking pathways. Exp. Parasitol.92, 87–99 (1999). CASPubMed Google Scholar
Jones, T. C., Yeh, S. & Hirsch, J. G. The interaction between Toxoplasma gondii and mammalian cells. I. Mechanism of entry and intracellular fate of the parasite. J. Exp. Med.136, 1157–1172 (1972). CASPubMedPubMed Central Google Scholar
Sinai, A. P., Webster, P. & Joiner, K. A. Association of host cell endoplasmic reticulum and mitochondria with the Toxoplasma gondii parasitophorous vacuole membrane: a high affinity interaction. J. Cell Sci.110, 2117–2128 (1997). CASPubMed Google Scholar
Hakansson, S., Charron, A. J. & Sibley, L. D. Toxoplasma evacuoles: a two-step process of secretion and fusion forms the parasitophorous vacuole. EMBO J.20, 3132–3144 (2001). CASPubMedPubMed Central Google Scholar
Sinai, A. P. & Joiner, K. A. The Toxoplasma gondii protein ROP2 mediates host organelle association with the parasitophorous vacuole membrane. J. Cell Biol.154, 95–108 (2001). CASPubMedPubMed Central Google Scholar
Carey, K. L., Jongco, A. M., Kim, K. & Ward, G. E. The Toxoplasma gondii rhoptry protein ROP4 is secreted into the parasitophorous vacuole and becomes phosphorylated in infected cells. Eukaryot. Cell3, 1320–1330 (2004). CASPubMedPubMed Central Google Scholar
Nakaar, V. et al. Pleiotropic effect due to targeted depletion of secretory rhoptry protein ROP2 in Toxoplasma gondii. J. Cell Sci.116, 2311–2320 (2003). This study shows that targeted depletion ofROP2gene expression by RNAi results in the loss of association of the mitochondrion with the membrane of the parasitophorous vacuole and in attenuated virulence ofT. gondiiin mice. CASPubMed Google Scholar
Henriquez, F. L. et al. Toxoplasma gondii dense granule protein 3 (GRA3) is a type I transmembrane protein that possesses a cytoplasmic dilysine (KKXX) endoplasmic reticulum (ER) retrieval motif. Parasitology131, 169–179 (2005). CASPubMed Google Scholar
Roop, R. M., Bellaire, B. H., Valderas, M. W. & Cardelli, J. A. Adaptation of the brucellae to their intracellular niche. Mol. Microbiol.52, 621–630 (2004). CASPubMed Google Scholar
Lapaque, N., Moriyon, I., Moreno, E. & Gorvel, J. P. Brucella lipopolysaccharide acts as a virulence factor. Curr. Opin. Microbiol.8, 60–66 (2005). CASPubMed Google Scholar
Fretin, D. et al. The sheathed flagellum of Brucella melitensis is involved in persistence in a murine model of infection. Cell. Microbiol.7, 687–698 (2005). CASPubMed Google Scholar
Pizarro-Cerda, J., Moreno, E., Sanguedolce, V., Mege, J. L. & Gorvel, J. P. Virulent Brucella abortus prevents lysosome fusion and is distributed within autophagosome-like compartments. Infect. Immun.66, 2387–2392 (1998). CASPubMedPubMed Central Google Scholar
Arenas, G. N., Staskevich, A. S., Aballay, A. & Mayorga, L. S. Intracellular trafficking of Brucella abortus in J774 macrophages. Infect. Immun.68, 4255–4263 (2000). CASPubMedPubMed Central Google Scholar
Naroeni, A., Jouy, N., Ouahrani-Bettache, S., Liautard, J. P. & Porte, F. _Brucella suis_-impaired specific recognition of phagosomes by lysosomes due to phagosomal membrane modifications. Infect. Immun.69, 486–493 (2001). CASPubMedPubMed Central Google Scholar
Celli, J. et al. Brucella evades macrophage killing via VirB-dependent sustained interactions with the endoplasmic reticulum. J. Exp. Med.198, 545–556 (2003). CASPubMedPubMed Central Google Scholar
Chaves-Olarte, E. et al. Activation of Rho and Rab GTPases dissociates Brucella abortus internalization from intracellular trafficking. Cell. Microbiol.4, 663–676 (2002). CASPubMed Google Scholar
Arellano-Reynoso, B. et al. Cyclic _β_-1,2-glucan is a Brucella virulence factor required for intracellular survival. Nature Immunol.6, 618–625 (2005). This article shows that theB. abortusmoleculeβ-1,2-glucan acts on the lipid rafts of vacuoles to prevent lysosomal fusion. This allows these pathogenic bacteria to reach the ER and survive. CAS Google Scholar
Anderson, T. D. & Cheville, N. F. Ultrastructural morphometric analysis of _Brucella abortus_-infected trophoblasts in experimental placentitis. Bacterial replication occurs in rough endoplasmic reticulum. Am. J. Pathol.124, 226–237 (1986). CASPubMedPubMed Central Google Scholar
Detilleux, P. G., Deyoe, B. L. & Cheville, N. F. Penetration and intracellular growth of Brucella abortus in nonphagocytic cells in vitro. Infect. Immun.58, 2320–2328 (1990). CASPubMedPubMed Central Google Scholar
Pizarro-Cerda, J. et al. Brucella abortus transits through the autophagic pathway and replicates in the endoplasmic reticulum of nonprofessional phagocytes. Infect. Immun.66, 5711–5724 (1998). CASPubMedPubMed Central Google Scholar
Celli, J., Salcedo, S. P. & Gorvel, J. P. Brucella coopts the small GTPase Sar1 for intracellular replication. Proc. Natl Acad. Sci. USA102, 1673–1678 (2005). This study shows that SAR1 has an important role in allowingB. abortusto create a specialized vacuole that allows intracellular replication. CASPubMedPubMed Central Google Scholar
Comerci, D. J., Martinez-Lorenzo, M. J., Sieira, R., Gorvel, J. P. & Ugalde, R. A. Essential role of the VirB machinery in the maturation of the _Brucella abortus_-containing vacuole. Cell. Microbiol.3, 159–168 (2001). CASPubMed Google Scholar
Giambartolomei, G. H. et al. Diminished production of T helper 1 cytokines correlates with T cell unresponsiveness to Brucella cytoplasmic proteins in chronic human brucellosis. J. Infect. Dis.186, 252–259 (2002). CASPubMed Google Scholar
Zhan, Y., Yang, J. & Cheers, C. Cytokine response of T-cell subsets from _Brucella abortus_-infected mice to soluble Brucella proteins. Infect. Immun.61, 2841–2847 (1993). CASPubMedPubMed Central Google Scholar
Fields, B. S. The molecular ecology of legionellae. Trends Microbiol.4, 286–290 (1996). CASPubMed Google Scholar
McDade, J. E. et al. Legionnaires' disease: isolation of a bacterium and demonstration of its role in other respiratory diseases. N. Engl. J. Med.297, 1197–1203 (1977). CASPubMed Google Scholar
Horwitz, M. A. & Silverstein, S. C. Legionnaires' disease bacterium (Legionella pneumophila) multiplies intracellularly in human monocytes. J. Clin. Invest.66, 441–450 (1980). CASPubMedPubMed Central Google Scholar
Nash, T. W., Libby, D. M. & Horwitz, M. A. Interaction between the legionnaires' disease bacterium (Legionella pneumophila) and human alveolar macrophages. Influence of antibody, lymphokines, and hydrocortisone. J. Clin. Invest.74, 771–782 (1984). CASPubMedPubMed Central Google Scholar
Horwitz, M. A. Formation of a novel phagosome by the legionnaires' disease bacterium (L egionella pneumophila) in human monocytes. J. Exp. Med.158, 1319–1331 (1983). CASPubMed Google Scholar
Horwitz, M. A. The legionnaires' disease bacterium (Legionella pneumophila) inhibits phagosome lysosome fusion in human monocytes. J. Exp. Med.158, 2108–2126 (1983). CASPubMed Google Scholar
Vogel, J. P., Andrews, H. L., Wong, S. K. & Isberg, R. R. Conjugative transfer by the virulence system of Legionella pneumophila. Science279, 873–876 (1998). CASPubMed Google Scholar
Segal, G., Purcell, M. & Shuman, H. A. Host cell killing and bacterial conjugation require overlapping sets of genes within a 22-kb region of the Legionella pneumophila genome. Proc. Natl Acad. Sci. USA95, 1669–1674 (1998). CASPubMedPubMed Central Google Scholar
Marra, A., Blander, S. J., Horwitz, M. A. & Shuman, H. A. Identification of a Legionella pneumophila locus required for intracellular multiplication in human macrophages. Proc. Natl Acad. Sci. USA89, 9607–9611 (1992). CASPubMedPubMed Central Google Scholar
Berger, K. H. & Isberg, R. R. Two distinct defects in intracellular growth complemented by a single genetic locus in Legionella pneumophila. Mol. Microbiol.7, 7–19 (1993). CASPubMed Google Scholar
Tilney, L. G., Harb, O. S., Connelly, P. S., Robinson, C. G. & Roy, C. R. How the parasitic bacterium Legionella pneumophila modifies its phagosome and transforms it into rough ER: implications for conversion of plasma membrane to the ER membrane. J. Cell Sci.114, 4637–4650 (2001). CASPubMed Google Scholar
Zuckman, D. M., Hung, J. B. & Roy, C. R. Pore-forming activity is not sufficient for Legionella pneumophila phagosome trafficking and intracellular growth. Mol. Microbiol.32, 990–1001 (1999). CASPubMed Google Scholar
Coers, J. et al. Identification of Icm protein complexes that play distinct roles in the biogenesis of an organelle permissive for Legionella pneumophila intracellular growth. Mol. Microbiol.38, 719–736 (2000). CASPubMed Google Scholar
Swanson, M. S. & Isberg, R. R. Association of Legionella pneumophila with the macrophage endoplasmic reticulum. Infect. Immun.63, 3609–3620 (1995). CASPubMedPubMed Central Google Scholar
Abu Kwaik, Y. The phagosome containing Legionella pneumophila within the protozoan Hartmannella vermiformis is surrounded by the rough endoplasmic reticulum. Appl. Environ. Microbiol.62, 2022–2028 (1996). CASPubMedPubMed Central Google Scholar
Kagan, J. C., Stein, M. P., Pypaert, M. & Roy, C. R. Legionella subvert the functions of Rab1 and Sec22b to create a replicative organelle. J. Exp. Med.199, 1201–1211 (2004). This study describes thatL. pneumophilarecruits the host GTPase RAB1 and the ER-derived vesicles that contain ERS24 (also known as SEC22B) to drive fusion of the bacterium-containing vacuole with the ER. CASPubMedPubMed Central Google Scholar
Kagan, J. C. & Roy, C. R. Legionella phagosomes intercept vesicular traffic from endoplasmic reticulum exit sites. Nature Cell Biol.4, 945–954 (2002). CASPubMed Google Scholar
Derre, I. & Isberg, R. R. Legionella pneumophila replication vacuole formation involves rapid recruitment of proteins of the early secretory system. Infect. Immun.72, 3048–3053 (2004). CASPubMedPubMed Central Google Scholar
Nagai, H., Kagan, J. C., Zhu, X., Kahn, R. A. & Roy, C. R. A bacterial guanine nucleotide exchange factor activates ARF on Legionella phagosomes. Science295, 679–682 (2002). CASPubMed Google Scholar
Neild, A. L. & Roy, C. R. Immunity to vacuolar pathogens: what can we learn from Legionella? Cell. Microbiol.6, 1011–1018 (2004). CASPubMed Google Scholar
Neild, A., Murata, T. & Roy, C. R. Processing and major histocompatibility complex class II presentation of Legionella pneumophila antigens by infected macrophages. Infect. Immun.73, 2336–2343 (2005). CASPubMedPubMed Central Google Scholar
Reggiori, F. et al. Early stages of the secretory pathway, but not endosomes, are required for Cvt vesicle and autophagosome assembly in Saccharomyces cerevisiae. Mol. Biol. Cell15, 2189–2204 (2004). CASPubMedPubMed Central Google Scholar
Ishihara, N. et al. Autophagosome requires specific early Sec proteins for its formation and NSF/SNARE for vacuolar fusion. Mol. Biol. Cell12, 3690–3702 (2001). CASPubMedPubMed Central Google Scholar
Meiling-Wesse, K. et al. Trs85 (Gsg1), a component of the TRAPP complexes is required for the organization of the preautophagosomal structure during selective autophagy via the Cvt pathway. J. Biol. Chem.280, 33669–33678 (2005). CASPubMed Google Scholar
Walker, D. H., Popov, V. L., Crocquet-Valdes, P. A., Welsh, C. J. & Feng, H. M. Cytokine-induced, nitric oxide-dependent, intracellular antirickettsial activity of mouse endothelial cells. Lab. Invest.76, 129–138 (1997). CASPubMed Google Scholar
Sturgill-Koszycki, S. & Swanson, M. S. Legionella pneumophila replication vacuoles mature into acidic, endocytic organelles. J. Exp. Med.192, 1261–1272 (2000). CASPubMedPubMed Central Google Scholar
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). CASPubMedPubMed Central Google Scholar
Rich, K. A., Burkett, C. & Webster, P. Cytoplasmic bacteria can be targets for autophagy. Cell. Microbiol.5, 455–468 (2003). CASPubMed Google Scholar
Nakagawa, I. et al. Autophagy defends cells against invading group A Streptococcus. Science306, 1037–1040 (2004). CASPubMed Google Scholar
Ogawa, M. et al. Escape of intracellular Shigella from autophagy. Science307, 727–731 (2005). In this study, the type-III-secretion-system effector IcsB is shown to protect intracellularS. flexnerifrom autophagy by associating with the autophagosome protein ATG5 and inhibiting its binding to VirG. CASPubMed Google Scholar
Dunn, W. A. Jr. Autophagy and related mechanisms of lysosome-mediated protein degradation. Trends Cell Biol.4, 139–143 (1994). CASPubMed Google Scholar
Jackson, W. T. et al. Subversion of cellular autophagosomal machinery by RNA viruses. PLoS Biol.3, e156 (2005). PubMedPubMed Central Google Scholar
Prentice, E., Jerome, W. G., Yoshimori, T., Mizushima, N. & Denison, M. R. Coronavirus replication complex formation utilizes components of cellular autophagy. J. Biol. Chem.279, 10136–10141 (2004). CASPubMed Google Scholar
Gutierrez, M. G. et al. Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages. Cell119, 753–766 (2004). CASPubMed Google Scholar
Rutkowski, D. T. & Kaufman, R. J. A trip to the ER: coping with stress. Trends Cell Biol.14, 20–28 (2004). CASPubMed Google Scholar
Li, X. D., Lankinen, H., Putkuri, N., Vapalahti, O. & Vaheri, A. Tula hantavirus triggers pro-apoptotic signals of ER stress in Vero E6 cells. Virology333, 180–199 (2005). CASPubMed Google Scholar
Dimcheff, D. E., Faasse, M. A., McAtee, F. J. & Portis, J. L. Endoplasmic reticulum (ER) stress induced by a neurovirulent mouse retrovirus is associated with prolonged BiP binding and retention of a viral protein in the ER. J. Biol. Chem.279, 33782–33790 (2004). CASPubMed Google Scholar
Cheng, G., Feng, Z. & He, B. Herpes simplex virus 1 infection activates the endoplasmic reticulum resident kinase PERK and mediates eIF-2α dephosphorylation by the γ134.5 protein. J. Virol.79, 1379–1388 (2005). CASPubMedPubMed Central Google Scholar
Boyce, M. et al. A selective inhibitor of eIF2α dephosphorylation protects cells from ER stress. Science307, 935–939 (2005). This study shows that treatment with salubrinal (an inhibitor of protein-phosphatase-1-mediated dephosphorylation of the translation-initiation factor EIF2α) protects cells from ER stress that is caused by the accumulation of unfolded proteins. CASPubMed Google Scholar
Szegezdi, E., Fitzgerald, U. & Samali, A. Caspase-12 and ER-stress-mediated apoptosis: the story so far. Ann. NY Acad. Sci.1010, 186–194 (2003). CASPubMed Google Scholar
Nakagawa, T. et al. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β. Nature403, 98–103 (2000). CASPubMed Google Scholar
Hitomi, J. et al. Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Aβ-induced cell death. J. Cell Biol.165, 347–356 (2004). CASPubMedPubMed Central Google Scholar
Boyle, K. A., Pietropaolo, R. L. & Compton, T. Engagement of the cellular receptor for glycoprotein B of human cytomegalovirus activates the interferon-responsive pathway. Mol. Cell. Biol.19, 3607–3613 (1999). CASPubMedPubMed Central Google Scholar
Zhu, H., Cong, J. P. & Shenk, T. Use of differential display analysis to assess the effect of human cytomegalovirus infection on the accumulation of cellular RNAs: induction of interferon-responsive RNAs. Proc. Natl Acad. Sci. USA94, 13985–13990 (1997). CASPubMedPubMed Central Google Scholar
Chin, K. C. & Cresswell, P. Viperin (cig5), an IFN-inducible antiviral protein directly induced by human cytomegalovirus. Proc. Natl Acad. Sci. USA98, 15125–15130 (2001). CASPubMedPubMed Central Google Scholar
Taylor, G. A., Feng, C. G. & Sher, A. p47 GTPases: regulators of immunity to intracellular pathogens. Nature Rev. Immunol.4, 100–109 (2004). CAS Google Scholar
MacMicking, J. D. IFN-inducible GTPases and immunity to intracellular pathogens. Trends Immunol.25, 601–609 (2004). CASPubMed Google Scholar
Gilly, M. & Wall, R. The IRG-47 gene is IFN-γ induced in B cells and encodes a protein with GTP-binding motifs. J. Immunol.148, 3275–3281 (1992). CASPubMed Google Scholar
Carlow, D. A., Marth, J., Clark-Lewis, I. & Teh, H. S. Isolation of a gene encoding a developmentally regulated T cell-specific protein with a guanine nucleotide triphosphate-binding motif. J. Immunol.154, 1724–1734 (1995). CASPubMed Google Scholar
Lafuse, W. P., Brown, D., Castle, L. & Zwilling, B. S. Cloning and characterization of a novel cDNA that is IFN-γ-induced in mouse peritoneal macrophages and encodes a putative GTP-binding protein. J. Leukoc. Biol.57, 477–483 (1995). CASPubMed Google Scholar
Sorace, J. M., Johnson, R. J., Howard, D. L. & Drysdale, B. E. Identification of an endotoxin and IFN-inducible cDNA: possible identification of a novel protein family. J. Leukoc. Biol.58, 477–484 (1995). CASPubMed Google Scholar
Taylor, G. A. et al. Identification of a novel GTPase, the inducibly expressed GTPase, that accumulates in response to interferon γ. J. Biol. Chem.271, 20399–20405 (1996). CASPubMed Google Scholar
Carlow, D. A., Teh, S. J. & Teh, H. S. Specific antiviral activity demonstrated by TGTP, a member of a new family of interferon-induced GTPases. J. Immunol.161, 2348–2355 (1998). CASPubMed Google Scholar
Martens, S. et al. Mechanisms regulating the positioning of mouse p47 resistance GTPases LRG-47 and IIGP1 on cellular membranes: retargeting to plasma membrane induced by phagocytosis. J. Immunol.173, 2594–2606 (2004). CASPubMed Google Scholar
Zerrahn, J., Schaible, U. E., Brinkmann, V., Guhlich, U. & Kaufmann, S. H. The IFN-inducible Golgi- and endoplasmic reticulum-associated 47-kDa GTPase IIGP is transiently expressed during listeriosis. J. Immunol.168, 3428–3436 (2002). CASPubMed Google Scholar
Taylor, G. A. et al. The inducibly expressed GTPase localizes to the endoplasmic reticulum, independently of GTP binding. J. Biol. Chem.272, 10639–10645 (1997). CASPubMed Google Scholar
Taylor, G. A. et al. Pathogen-specific loss of host resistance in mice lacking the IFN-γ-inducible gene IGTP. Proc. Natl Acad. Sci. USA97, 751–755 (2000). CASPubMedPubMed Central Google Scholar
Collazo, C. M. et al. The function of γ interferon-inducible GTP-binding protein IGTP in host resistance to Toxoplasma gondii is Stat1 dependent and requires expression in both hematopoietic and nonhematopoietic cellular compartments. Infect. Immun.70, 6933–6939 (2002). CASPubMedPubMed Central Google Scholar
Collazo, C. M. et al. Inactivation of LRG-47 and IRG-47 reveals a family of interferon γ-inducible genes with essential, pathogen-specific roles in resistance to infection. J. Exp. Med.194, 181–188 (2001). CASPubMedPubMed Central Google Scholar
MacMicking, J. D., Taylor, G. A. & McKinney, J. D. Immune control of tuberculosis by IFN-γ-inducible LRG-47. Science302, 654–659 (2003). This study shows that the activity of the GTPase LRG47 is responsible for the acidification ofM. tuberculosis-containing vacuoles following activation by IFNγ. CASPubMed Google Scholar
Fromme, J. C. & Schekman, R. COPII-coated vesicles: flexible enough for large cargo? Curr. Opin. Cell Biol.17, 345–352 (2005). CASPubMed Google Scholar
Altan-Bonnet, N., Phair, R. D., Polishchuk, R. S., Weigert, R. & Lippincott-Schwartz, J. A role for Arf1 in mitotic Golgi disassembly, chromosome segregation, and cytokinesis. Proc. Natl Acad. Sci. USA100, 13314–13319 (2003). CASPubMedPubMed Central Google Scholar