Indoleamine 2,3-dioxygenase is a signaling protein in long-term tolerance by dendritic cells
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Fazekas de St Groth, B. The evolution of self-tolerance: a new cell arises to meet the challenge of self-reactivity. Immunol. Today 19, 448–454 (1998).
Flajnik, M.F. & Kasahara, M. Origin and evolution of the adaptive immune system: genetic events and selective pressures. Nat. Rev. Genet. 11, 47–59 (2010).
Grohmann, U. & Bronte, V. Control of immune response by amino acid metabolism. Immunol. Rev. 236, 243–264 (2010).
Forouhar, F. et al. Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenase. Proc. Natl. Acad. Sci. USA 104, 473–478 (2007).
Ball, H.J., Yuasa, H.J., Austin, C.J., Weiser, S. & Hunt, N.H. Indoleamine 2,3-dioxygenase-2; a new enzyme in the kynurenine pathway. Int. J. Biochem. Cell Biol. 41, 467–471 (2009).
Metz, R. et al. Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan. Cancer Res. 67, 7082–7087 (2007).
Mellor, A.L. & Munn, D.H. IDO expression by dendritic cells: tolerance and tryptophan catabolism. Nat. Rev. Immunol. 4, 762–774 (2004).
Puccetti, P. & Grohmann, U. IDO and regulatory T cells: a role for reverse signalling and non-canonical NF-κB activation. Nat. Rev. Immunol. 7, 817–823 (2007).
Grohmann, U., Fallarino, F. & Puccetti, P. Tolerance, DCs and tryptophan: much ado about IDO. Trends Immunol. 24, 242–248 (2003).
Romani, L. et al. Defective tryptophan catabolism underlies inflammation in mouse chronic granulomatous disease. Nature 451, 211–215 (2008).
Belladonna, M.L. et al. Cutting edge: Autocrine TGF-β sustains default tolerogenesis by IDO-competent dendritic cells. J. Immunol. 181, 5194–5198 (2008).
Belladonna, M.L., Orabona, C., Grohmann, U. & Puccetti, P. TGF-β and kynurenines as the key to infectious tolerance. Trends Mol. Med. 15, 41–49 (2009).
Irla, M. et al. MHC class II-restricted antigen presentation by plasmacytoid dendritic cells inhibits T cell-mediated autoimmunity. J. Exp. Med. 207, 1891–1905 (2010).
Matta, B.M., Castellaneta, A. & Thomson, A.W. Tolerogenic plasmacytoid DC. Eur. J. Immunol. 40, 2667–2676 (2010).
Lande, R. & Gilliet, M. Plasmacytoid dendritic cells: key players in the initiation and regulation of immune responses. Ann. NY Acad. Sci. 1183, 89–103 (2010).
Swiecki, M. & Colonna, M. Unraveling the functions of plasmacytoid dendritic cells during viral infections, autoimmunity, and tolerance. Immunol. Rev. 234, 142–162 (2010).
Huang, L., Baban, B., Johnson, B.A. III & Mellor, A.L. Dendritic cells, indoleamine 2,3 dioxygenase and acquired immune privilege. Int. Rev. Immunol. 29, 133–155 (2010).
Orabona, C. et al. CD28 induces immunostimulatory signals in dendritic cells via CD80 and CD86. Nat. Immunol. 5, 1134–1142 (2004).
Grohmann, U. et al. Reverse signaling through GITR ligand enables dexamethasone to activate IDO in allergy. Nat. Med. 13, 579–586 (2007).
Neel, B.G., Gu, H. & Pao, L. The 'Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling. Trends Biochem. Sci. 28, 284–293 (2003).
Billadeau, D.D. & Leibson, P.J. ITAMs versus ITIMs: striking a balance during cell regulation. J. Clin. Invest. 109, 161–168 (2002).
Sweeney, M.C. et al. Decoding protein-protein interactions through combinatorial chemistry: sequence specificity of SHP-1, SHP-2, and SHIP SH2 domains. Biochemistry 44, 14932–14947 (2005).
Orr, S.J. et al. CD33 responses are blocked by SOCS3 through accelerated proteasomal-mediated turnover. Blood 109, 1061–1068 (2007).
Orr, S.J. et al. SOCS3 targets Siglec 7 for proteasomal degradation and blocks Siglec 7-mediated responses. J. Biol. Chem. 282, 3418–3422 (2007).
Orabona, C. et al. SOCS3 drives proteasomal degradation of indoleamine 2,3-dioxygenase (IDO) and antagonizes IDO-dependent tolerogenesis. Proc. Natl. Acad. Sci. USA 105, 20828–20833 (2008).
Williams, J.C., Wierenga, R.K. & Saraste, M. Insights into Src kinase functions: structural comparisons. Trends Biochem. Sci. 23, 179–184 (1998).
Daëron, M., Jaeger, S., Du Pasquier, L. & Vivier, E. Immunoreceptor tyrosine-based inhibition motifs: a quest in the past and future. Immunol. Rev. 224, 11–43 (2008).
An, H. et al. Phosphatase SHP-1 promotes TLR- and RIG-I-activated production of type I interferon by inhibiting the kinase IRAK1. Nat. Immunol. 9, 542–550 (2008).
Hoshino, K. et al. IκB kinase-α is critical for interferon-α production induced by Toll-like receptors 7 and 9. Nature 440, 949–953 (2006).
Tas, S.W. et al. Noncanonical NF-κB signaling in dendritic cells is required for indoleamine 2,3-dioxygenase (IDO) induction and immune regulation. Blood 110, 1540–1549 (2007).
Orabona, C. et al. Toward the identification of a tolerogenic signature in IDO-competent dendritic cells. Blood 107, 2846–2854 (2006).
Taylor, M.W. & Feng, G.S. Relationship between interferon-γ, indoleamine 2,3-dioxygenase, and tryptophan catabolism. FASEB J. 5, 2516–2522 (1991).
Munn, D.H. et al. Prevention of allogeneic fetal rejection by tryptophan catabolism. Science 281, 1191–1193 (1998).
Grohmann, U. et al. CTLA-4–Ig regulates tryptophan catabolism in vivo. Nat. Immunol. 3, 1097–1101 (2002).
Fallarino, F. et al. Modulation of tryptophan catabolism by regulatory T cells. Nat. Immunol. 4, 1206–1212 (2003).
Fallarino, F. et al. The combined effects of tryptophan starvation and tryptophan catabolites down-regulate T cell receptor ζ-chain and induce a regulatory phenotype in naive T cells. J. Immunol. 176, 6752–6761 (2006).
Mezrich, J.D. et al. An interaction between kynurenine and the aryl hydrocarbon receptor can generate regulatory T cells. J. Immunol. 185, 3190–3198 (2010).
Abu-Dayyeh, I. et al. Identification of key cytosolic kinases containing evolutionarily conserved kinase tyrosine-based inhibitory motifs (KTIMs). Dev. Comp. Immunol. 34, 481–484 (2010).
Grohmann, U. et al. A defect in tryptophan catabolism impairs tolerance in nonobese diabetic mice. J. Exp. Med. 198, 153–160 (2003).
Fallarino, F. et al. IDO mediates TLR9-driven protection from experimental autoimmune diabetes. J. Immunol. 183, 6303–6312 (2009).
Fallarino, F. et al. Metabotropic glutamate receptor-4 modulates adaptive immunity and restrains neuroinflammation. Nat. Med. 16, 897–902 (2010).
Orabona, C. et al. Cutting edge: silencing suppressor of cytokine signaling 3 expression in dendritic cells turns CD28-Ig from immune adjuvant to suppressant. J. Immunol. 174, 6582–6586 (2005).
Belladonna, M.L. et al. IL-23 neutralization protects mice from Gram-negative endotoxic shock. Cytokine 34, 161–169 (2006).
Belladonna, M.L. et al. IL-23 and IL-12 have overlapping, but distinct, effects on murine dendritic cells. J. Immunol. 168, 5448–5454 (2002).
Bisognin, A. et al. A-MADMAN: annotation-based microarray data meta-analysis tool. BMC Bioinformatics 10, 201–211 (2009).
Muller, A.J., DuHadaway, J.B., Donover, P.S., Sutanto-Ward, E. & Prendergast, G.C. Inhibition of indoleamine 2,3-dioxygenase, an immunoregulatory target of the cancer suppression gene Bin1, potentiates cancer chemotherapy. Nat. Med. 11, 312–319 (2005).
