Deubiquitylation and regulation of the immune response
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Adhikari, A., Xu, M. & Chen, Z. J. Ubiquitin-mediated activation of TAK1 and IKK. Oncogene 26, 3214–3226 (2007).
Liu, Y. C., Penninger, J. & Karin, M. Immunity by ubiquitylation: a reversible process of modification. Nature Rev. Immunol. 5, 941–952 (2005).
Nijman, S. M. et al. A genomic and functional inventory of deubiquitinating enzymes. Cell 123, 773–786 (2005).
Gong, B. & Leznik, E. The role of ubiquitin C-terminal hydrolase L1 in neurodegenerative disorders. Drug News Perspect. 20, 365–370 (2007).
Makarova, K. S., Aravind, L. & Koonin, E. V. A novel superfamily of predicted cysteine proteases from eukaryotes, viruses and Chlamydia pneumoniae. Trends Biochem. Sci. 25, 50–52 (2000).
Kayagaki, N. et al. DUBA: a deubiquitinase that regulates type I interferon production. Science 318, 1628–1632 (2007). This paper identifies DUBA as a key regulator of antiviral innate immunity.
Wertz, I. E. et al. De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kB signalling. Nature 430, 694–699 (2004). This paper shows that A20 has both DUB and E3-ligase functions.
Lin, A. E. & Mak, T. W. The role of E3 ligases in autoimmunity and the regulation of autoreactive T cells. Curr. Opin. Immunol. 19, 665–673 (2007).
Bignell, G. R. et al. Identification of the familial cylindromatosis tumour-suppressor gene. Nature Genet. 25, 160–165 (2000). This paper reports the identification of CYLD as a tumour suppressor.
Borodovsky, A. et al. Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family. Chem. Biol. 9, 1149–1159 (2002).
Brummelkamp, T. R., Nijman, S. M., Dirac, A. M. & Bernards, R. Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-κB. Nature 424, 797–801 (2003).
Kovalenko, A. et al. The tumour suppressor CYLD negatively regulates NF-κB signalling by deubiquitination. Nature 424, 801–805 (2003).
Trompouki, E. et al. CYLD is a deubiquitinating enzyme that negatively regulates NF-kB activation by TNFR family members. Nature 424, 793–796 (2003). References 12–14 are key reports of the signalling function of CYLD.
Massoumi, R., Chmielarska, K., Hennecke, K., Pfeifer,A. & Fassler, R. Cyld inhibits tumor cell proliferation by blocking bcl-3-dependent NF-κB signaling. Cell 125, 665–677 (2006).
Yoshida, H., Jono, H., Kai, H. & Li, J. D. The tumor suppressor CYLD acts as a negative regulator for Toll-like receptor 2 signaling via negative cross-talk with TRAF6 and TRAF7. J. Biol. Chem. 280, 41111–41121 (2005).
Jin, W. et al. Deubiquitinating enzyme CYLD regulates RANK signaling and osteoclastogenesis. J. Clinic. Invest. (in the press).
Reiley, W. W. et al. Regulation of T cell development by the deubiquitinating enzyme CYLD. Nature Immunol. 7, 411–417 (2006). This paper was the first to show the in vivo role of CYLD in regulating immune functions.
Reiley, W. W. et al. Deubiquitinating enzyme CYLD negatively regulates the ubiquitin-dependent kinase Tak1 and prevents abnormal T cell responses. J. Exp. Med. 204, 1475–1485 (2007).
Wright, A. et al. Regulation of early wave of germ cell apoptosis and spermatogenesis by deubiquitinating enzyme CYLD. Dev. Cell 13, 705–716 (2007).
Stokes, A. et al. TRPA1 is a substrate for de-ubiquitination by the tumor suppressor CYLD. Cell Signal. 18, 1584–1594 (2006).
Lim, J. H. et al. Tumor suppressor CYLD acts as a negative regulator for non-typeable Haemophilus influenza-induced inflammation in the middle ear and lung of mice. PLoS ONE 2, e1032 (2007).
Lim, J. H. et al. Tumor suppressor CYLD regulates acute lung injury in lethal Streptococcus pneumoniae infections. Immunity 27, 349–360 (2007).
Zhang, J. et al. Impaired regulation of NF-κB and increased susceptibility to colitis-associated tumorigenesis in CYLD-deficient mice. J. Clin. Invest. 116, 3042–3049 (2006).
Hövelmeyer, N. et al. Regulation of B cell homeostasis and activation by the tumor suppressor gene CYLD. J. Exp. Med. 204, 2615–2627 (2007).
Gao, J. et al. The tumor suppressor CYLD regulates microtubule dynamics and plays a role in cell migration. J. Biol. Chem. 283, 8802–8809 (2008).
Stegmeier, F. et al. The tumor suppressor CYLD regulates entry into mitosis. Proc. Natl Acad. Sci. USA 104, 8869–8874 (2007).
Saito, K. et al. The CAP-Gly domain of CYLD associates with the proline-rich sequence in NEMO/IKKγ. Structure 12, 1719–1728 (2004).
Ea, C. K., Deng, L., Xia, Z. P., Pineda, G. & Chen, Z. J. Activation of IKK by TNFα requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO. Mol. Cell 22, 245–257 (2006).
Li, H., Kobayashi, M., Blonska, M., You, Y. & Lin, X. Ubiquitination of RIP is required for tumor necrosis factor a-induced NF-κB activation. J. Biol. Chem. 281, 13636–13643 (2006).
Wu, C. J., Conze, D. B., Li, T., Srinivasula, S. M. & Ashwell, J. D. Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-κB activation. Nature Cell Biol. 8, 398–406 (2006).
Komander, D. et al. The structure of the CYLD USP domain explains its specificity for Lys63-linked polyubiquitin and reveals a B Box module. Mol. Cell 29, 451–464 (2008).
Xue, L. et al. Tumor suppressor CYLD regulates JNK-induced cell death in Drosophila. Dev. Cell 13, 446–454 (2007).
Wooten, M. W. et al. Essential role of sequestosome 1/p62 in regulating accumulation of Lys63-ubiquitinated proteins. J. Biol. Chem. 283, 6783–6789 (2008).
Beyaert, R., Heyninck, K. & Van Huffel, S. A20 and A20-binding proteins as cellular inhibitors of nuclear factor-κB-dependent gene expression and apoptosis. Biochem. Pharmacol. 60, 1143–1151 (2000).
Lee, E. G. et al. Failure to regulate TNF-induced NF-κB and cell death responses in A20-deficient mice. Science 289, 2350–4 (2000). This study was the first to report the in vivo role of A20 in regulating inflammation.
Boone, D. L. et al. The ubiquitin-modifying enzyme A20 is required for termination of Toll-like receptor responses. Nature Immunol. 5, 1052–1060 (2004).
Hitotsumatsu, O. et al. The ubiquitin-editing enzyme A20 restricts nucleotide-binding oligomerization domain containing 2-triggered signals. Immunity 28, 381–390 (2008).
Evans, P. C. et al. Zinc-finger protein A20, a regulator of inflammation and cell survival, has de-ubiquitinating activity. Biochem. J. 378, 727–734 (2004).
Mauro, C. et al. ABIN-1 binds to NEMO/IKKg and co-operates with A20 in inhibiting NF-κB. J. Biol. Chem. 281, 18482–18488 (2006).
Shembade, N. et al. The E3 ligase Itch negatively regulates inflammatory signaling pathways by controlling the function of the ubiquitin-editing enzyme A20. Nature Immunol. 9, 254–262 (2008).
Komander, D. & Barford, D. Structure of the A20 OTU domain and mechanistic insights into deubiquitination. Biochem. J. 409, 77–85 (2008).
Lin, S. C. et al. Molecular basis for the unique deubiquitinating activity of the NF-κB inhibitor A20. J. Mol. Biol. 376, 526–540 (2008).
Shembade, N., Harhaj, N. S., Liebl, D. J. & Harhaj, E. W. Essential role for TAX1BP1 in the termination of TNF-α-, IL-1- and LPS-mediated NF-κB and JNK signaling. EMBO J. 26, 3910–3922 (2007).
Iha, H. et al. Inflammatory cardiac valvulitis in TAX1BP1-deficient mice through selective NF-κB activation. EMBO J. 27, 629–641 (2008).
Jin, D. Y. et al. A human suppressor of c-Jun N-terminal kinase 1 activation by tumor necrosis factor α. J. Biol. Chem. 272, 25816–25823 (1997).
De Valck, D. et al. The zinc finger protein A20 interacts with a novel anti-apoptotic protein which is cleaved by specific caspases. Oncogene 18, 4182–4190 (1999).
Wagner, S. et al. Ubiquitin binding mediates the NF-κB inhibitory potential of ABINs. Oncogene 21 January 2008 (doi:10.1038/sj.onc.1211042).
Evans, P. C. et al. Isolation and characterization of two novel A20-like proteins. Biochem. J. 357, 617–623 (2001).
Evans, P. C. et al. A novel type of deubiquitinating enzyme. J. Biol. Chem. 278, 23180–23186 (2003).
Enesa, K. et al. NF-κB suppression by the deubiquitinating enzyme Cezanne: a novel negative feedback loop in pro-inflammatory signaling. J. Biol. Chem. 283, 7036–7045 (2008).
Balakirev, M. Y., Tcherniuk, S. O., Jaquinod, M. & Chroboczek, J. Otubains: a new family of cysteine proteases in the ubiquitin pathway. EMBO Rep. 4, 517–522 (2003).
Soares, L. et al. Two isoforms of otubain 1 regulate T cell anergy via GRAIL. Nature Immunol. 5, 45–54 (2004).
Schweitzer, K., Bozko, P. M., Dubiel, W. & Naumann, M. CSN controls NF-κB by deubiquitinylation of IκBα. EMBO J. 26, 1532–1541 (2007).
Scherer, D. C., Brockman, J. A., Chen, A., Maniatis, T. & Ballard, D. W. Signal-induced degradation of IκBα requires site-specific ubiquitination. Proc. Natl Acad. Sci. USA 92, 11259–11263 (1995).
Schwechheimer, C. & Deng, X. W. COP9 signalosome revisited: a novel mediator of protein degradation. Trends Cell Biol. 11, 420–426 (2001).
Baek, K. H. Cytokine-regulated protein degradation by the ubiquitination system. Curr. Protein Pept. Sci. 7, 171–177 (2006).
Gesbert, F., Malardé, V. & Dautry-Varsat, A. Ubiquitination of the common cytokine receptor gammac and regulation of expression by an ubiquitination/deubiquitination machinery. Biochem. Biophys. Res. Commun. 334, 474–480 (2005).
Migone, T. S. et al. The deubiquitinating enzyme DUB-2 prolongs cytokine-induced signal transducers and activators of transcription activation and suppresses apoptosis following cytokine withdrawal. Blood 98, 1935–1941 (2001).
Hiscott, J. Triggering the innate antiviral response through IRF-3 activation. J. Biol. Chem. 282, 15325–15329 (2007).
Liew, F. Y., Xu, D., Brint, E. K. & O'Neill, L. A. Negative regulation of Toll-like receptor-mediated immune responses. Nature Rev. Immunol. 5, 446–458 (2005).
Baccala, R., Hoebe, K., Kono, D. H., Beutler, B. & Theofilopoulos, A. N. TLR-dependent and TLR-independent pathways of type I interferon induction in systemic autoimmunity. Nature Med. 13, 543–551 (2007).
Turer, E. E. et al. Homeostatic MyD88-dependent signals cause lethal inflamMation in the absence of A20. J. Exp. Med. 205, 451–464 (2008).
Reiley, W., Zhang, M., Wu, X., Graner, E. & Sun, S. -C. Regulation of the deubiquitinating enzyme CYLD by IκB kinase γ-dependent phosphorylation. Mol. Cell. Biol. 25, 3886–3895 (2005).
Hiscott, J. Convergence of the NF-κB and IRF pathways in the regulation of the innate antiviral response. Cytokine Growth Factor Rev. 18, 483–490 (2007).
Häcker, H. et al. Specificity in Toll-like receptor signalling through distinct effector functions of TRAF3 and TRAF6. Nature 439, 204–207 (2006).
Oganesyan, G. et al. Critical role of TRAF3 in the Toll-like receptor-dependent and -independent antiviral response. Nature 439, 208–211 (2006).
Guo, B. & Cheng, G. Modulation of the interferon antiviral response by the TBK1/IKKi adaptor protein TANK. J. Biol. Chem. 282, 11817–11826 (2007).
Gatot, J. S. et al. Lipopolysaccharide-mediated interferon regulatory factor activation involves TBK1-IKKε-dependent Lys(63)-linked polyubiquitination and phosphorylation of TANK/I-TRAF. J. Biol. Chem. 282, 31131–31146 (2007).
Zhao, T. et al. The NEMO adaptor bridges the nuclear factor-κB and interferon regulatory factor signaling pathways. Nature Immunol. 8, 592–600 (2007).
Gack, M. U. et al. TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity. Nature 446, 916–920 (2007). This paper reports the regulation of RIG-I signalling function by K63-linked ubiquitylation.
Zhang, M. et al. Regulation of IKK-related kinases and antiviral responses by tumor suppressor CYLD. J. Biol. Chem. 8 May 2008 (doi:10.1074/jbc.M801451200).
Wang, Y. Y., Li, L., Han, K. J., Zhai, Z. & Shu, H. B. A20 is a potent inhibitor of TLR3- and Sendai virus-induced activation of NF-κB and ISRE and IFN-β promoter. FEBS J. 576, 86–90 (2004).
Saitoh, T. et al. A20 is a negative regulator of IFN regulatory factor 3 signaling. J. Immunol. 174, 1507–1512 (2005).
Lin, R. et al. Negative regulation of the retinoic acid-inducible gene I-induced antiviral state by the ubiquitin-editing protein A20. J. Biol. Chem. 281, 2095–2103 (2006).
Starr, T. K., Jameson, S. C. & Hogquist, K. A. Positive and negative selection of T cells. Annu. Rev. Immunol. 21, 139–176 (2003).
Molina, T. J. et al. Profound block in thymocyte development in mice lacking p56lck. Nature 357, 161–164 (1992).
Palacios, E. H. & Weiss, A. Function of the Src-family kinases, Lck and Fyn, in T-cell development and activation. Oncogene 23, 7990–8000 (2004).
Rao, N. et al. Negative regulation of Lck by Cbl ubiquitin ligase. Proc. Natl Acad. Sci. USA 99, 3794–3799 (2002).
Thien, C. B., Bowtell, D. D. & Langdon, W. Y. Perturbed regulation of ZAP-70 and sustained tyrosine phosphorylation of LAT and SLP-76 in c-Cbl-deficient thymocytes. J. Immunol. 162, 7133–7139 (1999).
Naramura, M., Kole, H. K., Hu, R. J. & Gu, H. Altered thymic positive selection and intracellular signals in Cbl-deficient mice. Proc. Natl Acad. Sci. USA 95, 15547–15552 (1998).
Murphy, M. A. et al. Tissue hyperplasia and enhanced T-cell signalling via ZAP-70 in c-Cbl-deficient mice. Mol. Cell. Biol. 18, 4872–4882 (1998).
Hawash, I. Y., Kesavan, K. P., Magee, A. I., Geahlen, R. L. & Harrison, M. L. The Lck SH3 domain negatively regulates localization to lipid rafts through an interaction with c-Cbl. J. Biol. Chem. 277, 5683–5691 (2002).
Kronenberg, M. & Rudensky, A. Regulation of immunity by self-reactive T cells. Nature 435, 598–604 (2005).
Kyewski, B. & Klein, L. A central role for central tolerance. Annu. Rev. Immunol. 24, 571–606 (2006).
Choi, S. & Schwartz, R. H. Molecular mechanisms for adaptive tolerance and other T cell anergy models. Semin. Immunol. 19, 140–152 (2007).
MacKenzie, D. A. et al. GRAIL is up-regulated in CD4+ CD25+ T regulatory cells and is sufficient for conversion of T cells to a regulatory phenotype. J. Biol. Chem. 282, 9696–9702 (2007).
Mouchantaf, R. et al. The ubiquitin ligase itch is auto-ubiquitylated in vivo and in vitro but is protected from degradation by interacting with the deubiquitylating enzyme FAM/USP9X. J. Biol. Chem. 281, 38738–38747 (2006).
Liu, Y. C. The E3 ubiquitin ligase Itch in T cell activation, differentiation, and tolerance. Semin. Immunol. 19, 197–205 (2007).
Perry, W. L. et al. The itchy locus encodes a novel ubiquitin protein ligase that is disrupted in a18H mice. Nature Genet. 18, 143–146 (1998).
Rawlings, D. J., Sommer, K. & Moreno-García, M. E. The CARMA1 signalosome links the signalling machinery of adaptive and innate immunity in lymphocytes. Nature Rev. Immunol. 6, 799–812 (2006).
Sun, L., Deng, L., Ea, C. -K., Xia, Z. -P. & Chen, Z. J. The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes. Mol. Cell 14, 289–301 (2004).
Zhou, H. et al. Bcl10 activates the NF-κB pathway through ubiquitination of NEMO. Nature 427, 167–171 (2004).
Oeckinghaus, A. et al. Malt1 ubiquitination triggers NF-κB signaling upon T-cell activation. EMBO J. 26, 4634–4645 (2007).
Liu, H. H., Xie, M., Schneider, M. D. & Chen, Z. J. Essential role of TAK1 in thymocyte development and activation. Proc. Natl Acad. Sci. USA 103, 11677–11682 (2006).
Sato, S. et al. TAK1 is indispensable for development of T cells and prevention of colitis by the generation of regulatory T cells. Int. Immunol. 18, 1405–1411 (2006).
Wan, Y. Y., Chi, H., Xie, M., Schneider, M. D. & Flavell, R. A. The kinase TAK1 integrates antigen and cytokine receptor signaling for T cell development, survival and function. Nature Immunol. 7, 851–858 (2006).
Thiefes, A. et al. The Yersinia enterocolitica effector YopP inhibits host cell signalling by inactivating the protein kinase TAK1 in the IL-1 signalling pathway. EMBO Rep. 7, 838–844 (2006).
Yamamoto, M. et al. Cutting Edge: pivotal function of Ubc13 in thymocyte TCR signaling. J. Immunol. 177, 7520–7524 (2006).
King, C. G. et al. TRAF6 is a T cell-intrinsic negative regulator required for the maintenance of immune homeostasis. Nature Med. 12, 1088–1092 (2006).
Coornaert, B. et al. T cell antigen receptor stimulation induces MALT1 paracaspase-mediated cleavage of the NF-κB inhibitor A20. Nature Immunol. 9, 263–271 (2008).
Baumgart, D. C. & Carding, S. R. Inflammatory bowel disease: cause and immunobiology. Lancet 369, 1627–1640 (2007).
Sen, R. Control of B lymphocyte apoptosis by the transcription factor NF-κB. Immunity 25, 871–883 (2006).
Claudio, E., Brown, K., Park, S., Wang, H. & Siebenlist, U. BAFF-induced NEMO-independent processing of NF-κB2 in maturing B cells. Nature Immunol. 3, 958–965 (2002).
Kayagaki, N. et al. BAFF/BLyS receptor 3 binds the B-cell survival factor BAFF ligand through a discrete surface loop and promotes processing of NF-κB2. Immunity 17, 515–524 (2002).
Jin, W. et al. Deubiquitinating enzyme CYLD regulates the peripheral development and naive phenotype maintenance of B cells. J. Biol. Chem. 282, 15884–15893 (2007).
Annunziata, C. M. et al. Frequent engagement of the classical and alternative NF-κB pathways by diverse genetic abnormalities in multiple myeloma. Cancer Cell 12, 115–130 (2007).
Keats, J. J. et al. Promiscuous mutations activate the noncanonical NF-κB pathway in multiple myeloma. Cancer Cell 12, 131–144 (2007).
Sigismund, S., Polo, S. & Di Fiore, P. P. Signaling through monoubiquitination. Curr. Top. Microbiol. Immunol. 286, 149–185 (2004).
Beinke, S. & Ley, S. C. Functions of NF-κB1 and NF-κB2 in immune cell biology. Biochem. J. 382, 393–409 (2004).
Xiao, G., Harhaj, E. W. & Sun, S. C. NF-κB-inducing kinase regulates the processing of NF-κB2 p100. Mol. Cell. 7, 401–409 (2001).
Bonizzi, G. & Karin, M. The two NF-κB activation pathways and their role in innate and adaptive immunity. Trends Immunol. 25, 280–288 (2004).
Hacker, H. & Karin, M. Regulation and function of IKK and IKK-related kinases. Sci. STKE 357, re13 (2006).