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Volumn 22, Issue 7, 2012, Pages 355-364

Diverse ubiquitin signaling in NF-κB activation

Author keywords

Linear ubiquitination; LUBAC; NF B; Ubiquitin

Indexed keywords

DNA; I KAPPA B KINASE GAMMA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INHIBITOR OF APOPTOSIS PROTEIN; INTERLEUKIN 1BETA; LINEAR UBIQUITIN CHAIN ASSEMBLY COMPLEX; POLYUBIQUITIN; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED PROTEIN WITH A DEATH DOMAIN; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 84862761186     PISSN: 09628924     EISSN: 18793088     Source Type: Journal    
DOI: 10.1016/j.tcb.2012.04.001     Document Type: Review
Times cited : (148)

References (87)
  • 1
    • 23944474593 scopus 로고    scopus 로고
    • Intracellular protein degradation: from a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting
    • Ciechanover A. Intracellular protein degradation: from a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting. Cell Death Differ. 2005, 12:1178-1190.
    • (2005) Cell Death Differ. , vol.12 , pp. 1178-1190
    • Ciechanover, A.1
  • 3
    • 50149086108 scopus 로고    scopus 로고
    • Diversity of degradation signals in the ubiquitin-proteasome system
    • Ravid T., Hochstrasser M. Diversity of degradation signals in the ubiquitin-proteasome system. Nat. Rev. Mol. Cell Biol. 2008, 9:679-690.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 679-690
    • Ravid, T.1    Hochstrasser, M.2
  • 4
    • 59649086030 scopus 로고    scopus 로고
    • Nonproteolytic functions of ubiquitin in cell signaling
    • Chen Z.J., Sun L.J. Nonproteolytic functions of ubiquitin in cell signaling. Mol. Cell 2009, 33:275-286.
    • (2009) Mol. Cell , vol.33 , pp. 275-286
    • Chen, Z.J.1    Sun, L.J.2
  • 5
    • 44649101850 scopus 로고    scopus 로고
    • Atypical ubiquitin chains: new molecular signals. 'Protein Modifications: Beyond the Usual Suspects' review series
    • Ikeda F., Dikic I. Atypical ubiquitin chains: new molecular signals. 'Protein Modifications: Beyond the Usual Suspects' review series. EMBO Rep. 2008, 9:536-542.
    • (2008) EMBO Rep. , vol.9 , pp. 536-542
    • Ikeda, F.1    Dikic, I.2
  • 6
    • 79955620198 scopus 로고    scopus 로고
    • Constructing and decoding unconventional ubiquitin chains
    • Behrends C., Harper J.W. Constructing and decoding unconventional ubiquitin chains. Nat. Struct. Mol. Biol. 2011, 18:520-528.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 520-528
    • Behrends, C.1    Harper, J.W.2
  • 7
    • 67650744586 scopus 로고    scopus 로고
    • The role of ubiquitin in NF-κB regulatory pathways
    • Skaug B., et al. The role of ubiquitin in NF-κB regulatory pathways. Annu. Rev. Biochem. 2009, 78:769-796.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 769-796
    • Skaug, B.1
  • 10
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-κB signaling
    • Hayden M.S., Ghosh S. Shared principles in NF-κB signaling. Cell 2008, 132:344-362.
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 12
    • 80052014052 scopus 로고    scopus 로고
    • Inflammation meets cancer, with NF-κB as the matchmaker
    • Ben-Neriah Y., Karin M. Inflammation meets cancer, with NF-κB as the matchmaker. Nat. Immunol. 2011, 12:715-723.
    • (2011) Nat. Immunol. , vol.12 , pp. 715-723
    • Ben-Neriah, Y.1    Karin, M.2
  • 13
    • 2342464085 scopus 로고    scopus 로고
    • The two NF-κB activation pathways and their role in innate and adaptive immunity
    • Bonizzi G., Karin M. The two NF-κB activation pathways and their role in innate and adaptive immunity. Trends Immunol. 2004, 25:280-288.
    • (2004) Trends Immunol. , vol.25 , pp. 280-288
    • Bonizzi, G.1    Karin, M.2
  • 14
    • 65249083913 scopus 로고    scopus 로고
    • Ubiquitin in NF-κB signaling
    • Chiu Y.H., et al. Ubiquitin in NF-κB signaling. Chem. Rev. 2009, 109:1549-1560.
    • (2009) Chem. Rev. , vol.109 , pp. 1549-1560
    • Chiu, Y.H.1
  • 15
    • 77957252647 scopus 로고    scopus 로고
    • The IKK complex, a central regulator of NF-κB activation
    • Israel A. The IKK complex, a central regulator of NF-κB activation. Cold Spring Harb. Perspect. Biol. 2010, 2:a000158.
    • (2010) Cold Spring Harb. Perspect. Biol. , vol.2
    • Israel, A.1
  • 16
    • 78650920066 scopus 로고    scopus 로고
    • Non-canonical NF-κB signaling pathway
    • Sun S.C. Non-canonical NF-κB signaling pathway. Cell Res. 2011, 21:71-85.
    • (2011) Cell Res. , vol.21 , pp. 71-85
    • Sun, S.C.1
  • 17
    • 80052906832 scopus 로고    scopus 로고
    • Linear polyubiquitin chains: a new modifier involved in NFκB activation and chronic inflammation, including dermatitis
    • Iwai K. Linear polyubiquitin chains: a new modifier involved in NFκB activation and chronic inflammation, including dermatitis. Cell Cycle 2011, 10:3095-3104.
    • (2011) Cell Cycle , vol.10 , pp. 3095-3104
    • Iwai, K.1
  • 18
    • 67650064603 scopus 로고    scopus 로고
    • Linear polyubiquitination: a new regulator of NF-κB activation
    • Iwai K., Tokunaga F. Linear polyubiquitination: a new regulator of NF-κB activation. EMBO Rep. 2009, 10:706-713.
    • (2009) EMBO Rep. , vol.10 , pp. 706-713
    • Iwai, K.1    Tokunaga, F.2
  • 19
    • 69949093459 scopus 로고    scopus 로고
    • Direct activation of protein kinases by unanchored polyubiquitin chains
    • Xia Z.P., et al. Direct activation of protein kinases by unanchored polyubiquitin chains. Nature 2009, 461:114-119.
    • (2009) Nature , vol.461 , pp. 114-119
    • Xia, Z.P.1
  • 20
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the IκB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
    • Deng L., et al. Activation of the IκB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell 2000, 103:351-361.
    • (2000) Cell , vol.103 , pp. 351-361
    • Deng, L.1
  • 21
    • 49549117842 scopus 로고    scopus 로고
    • Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies
    • Newton K., et al. Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies. Cell 2008, 134:668-678.
    • (2008) Cell , vol.134 , pp. 668-678
    • Newton, K.1
  • 22
    • 43249120917 scopus 로고    scopus 로고
    • Lys63-linked polyubiquitination of IRAK-1 is required for interleukin-1 receptor- and toll-like receptor-mediated NF-κB activation
    • Conze D.B., et al. Lys63-linked polyubiquitination of IRAK-1 is required for interleukin-1 receptor- and toll-like receptor-mediated NF-κB activation. Mol. Cell. Biol. 2008, 28:3538-3547.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 3538-3547
    • Conze, D.B.1
  • 23
    • 34248570795 scopus 로고    scopus 로고
    • Ubiquitin-mediated activation of TAK1 and IKK
    • Adhikari A., et al. Ubiquitin-mediated activation of TAK1 and IKK. Oncogene 2007, 26:3214-3226.
    • (2007) Oncogene , vol.26 , pp. 3214-3226
    • Adhikari, A.1
  • 24
    • 33747615237 scopus 로고    scopus 로고
    • Key function for the Ubc13 E2 ubiquitin-conjugating enzyme in immune receptor signaling
    • Yamamoto M., et al. Key function for the Ubc13 E2 ubiquitin-conjugating enzyme in immune receptor signaling. Nat. Immunol. 2006, 7:962-970.
    • (2006) Nat. Immunol. , vol.7 , pp. 962-970
    • Yamamoto, M.1
  • 25
    • 77950367657 scopus 로고    scopus 로고
    • Two mechanistically and temporally distinct NF-κB activation pathways in IL-1 signaling
    • Yamazaki K., et al. Two mechanistically and temporally distinct NF-κB activation pathways in IL-1 signaling. Sci. Signal. 2009, 2:ra66.
    • (2009) Sci. Signal. , vol.2
    • Yamazaki, K.1
  • 26
    • 70350015537 scopus 로고    scopus 로고
    • A Ubiquitin replacement strategy in human cells reveals distinct mechanisms of IKK activation by TNFα and IL-1β
    • Xu M., et al. A Ubiquitin replacement strategy in human cells reveals distinct mechanisms of IKK activation by TNFα and IL-1β. Mol. Cell 2009, 36:302-314.
    • (2009) Mol. Cell , vol.36 , pp. 302-314
    • Xu, M.1
  • 27
    • 33750219981 scopus 로고    scopus 로고
    • A ubiquitin ligase complex assembles linear polyubiquitin chains
    • Kirisako T., et al. A ubiquitin ligase complex assembles linear polyubiquitin chains. EMBO J. 2006, 25:4877-4887.
    • (2006) EMBO J. , vol.25 , pp. 4877-4887
    • Kirisako, T.1
  • 28
    • 80755153309 scopus 로고    scopus 로고
    • K11-linked ubiquitin chains as novel regulators of cell division
    • Wickliffe K.E., et al. K11-linked ubiquitin chains as novel regulators of cell division. Trends Cell Biol. 2011, 21:656-663.
    • (2011) Trends Cell Biol. , vol.21 , pp. 656-663
    • Wickliffe, K.E.1
  • 29
    • 59649103156 scopus 로고    scopus 로고
    • Involvement of linear polyubiquitylation of NEMO in NF-κB activation
    • Tokunaga F., et al. Involvement of linear polyubiquitylation of NEMO in NF-κB activation. Nat. Cell Biol. 2009, 11:123-132.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 123-132
    • Tokunaga, F.1
  • 30
    • 34547422758 scopus 로고    scopus 로고
    • Spontaneous mutations in the mouse Sharpin gene result in multiorgan inflammation, immune system dysregulation and dermatitis
    • Seymour R.E., et al. Spontaneous mutations in the mouse Sharpin gene result in multiorgan inflammation, immune system dysregulation and dermatitis. Genes Immun. 2007, 8:416-421.
    • (2007) Genes Immun. , vol.8 , pp. 416-421
    • Seymour, R.E.1
  • 31
    • 79953237668 scopus 로고    scopus 로고
    • SHARPIN is a component of the NF-κB-activating linear ubiquitin chain assembly complex
    • Tokunaga F., et al. SHARPIN is a component of the NF-κB-activating linear ubiquitin chain assembly complex. Nature 2011, 471:633-636.
    • (2011) Nature , vol.471 , pp. 633-636
    • Tokunaga, F.1
  • 32
    • 79953240109 scopus 로고    scopus 로고
    • Linear ubiquitination prevents inflammation and regulates immune signalling
    • Gerlach B., et al. Linear ubiquitination prevents inflammation and regulates immune signalling. Nature 2011, 471:591-596.
    • (2011) Nature , vol.471 , pp. 591-596
    • Gerlach, B.1
  • 33
    • 79960993122 scopus 로고    scopus 로고
    • Systems analysis identifies an essential role for SHANK-associated RH domain-interacting protein (SHARPIN) in macrophage Toll-like receptor 2 (TLR2) responses
    • Zak D.E., et al. Systems analysis identifies an essential role for SHANK-associated RH domain-interacting protein (SHARPIN) in macrophage Toll-like receptor 2 (TLR2) responses. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:11536-11541.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 11536-11541
    • Zak, D.E.1
  • 34
    • 79953239980 scopus 로고    scopus 로고
    • SHARPIN forms a linear ubiquitin ligase complex regulating NF-κB activity and apoptosis
    • Ikeda F., et al. SHARPIN forms a linear ubiquitin ligase complex regulating NF-κB activity and apoptosis. Nature 2011, 471:637-641.
    • (2011) Nature , vol.471 , pp. 637-641
    • Ikeda, F.1
  • 35
    • 43049162227 scopus 로고    scopus 로고
    • Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex
    • Jin L., et al. Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex. Cell 2008, 133:653-665.
    • (2008) Cell , vol.133 , pp. 653-665
    • Jin, L.1
  • 36
    • 78650300883 scopus 로고    scopus 로고
    • C-IAP1 and UbcH5 promote K11-linked polyubiquitination of RIP1 in TNF signalling
    • Dynek J.N., et al. c-IAP1 and UbcH5 promote K11-linked polyubiquitination of RIP1 in TNF signalling. EMBO J. 2010, 29:4198-4209.
    • (2010) EMBO J. , vol.29 , pp. 4198-4209
    • Dynek, J.N.1
  • 37
    • 79953846027 scopus 로고    scopus 로고
    • Modulation of K11-linkage formation by variable loop residues within UbcH5A
    • Bosanac I., et al. Modulation of K11-linkage formation by variable loop residues within UbcH5A. J. Mol. Biol. 2011, 408:420-431.
    • (2011) J. Mol. Biol. , vol.408 , pp. 420-431
    • Bosanac, I.1
  • 38
    • 0026968499 scopus 로고
    • Receptor protein tyrosine kinases and phosphatases
    • Hunter T., et al. Receptor protein tyrosine kinases and phosphatases. Cold Spring Harb. Symp. Quant. Biol. 1992, 57:25-41.
    • (1992) Cold Spring Harb. Symp. Quant. Biol. , vol.57 , pp. 25-41
    • Hunter, T.1
  • 39
    • 27544434183 scopus 로고    scopus 로고
    • Essential function for the kinase TAK1 in innate and adaptive immune responses
    • Sato S., et al. Essential function for the kinase TAK1 in innate and adaptive immune responses. Nat. Immunol. 2005, 6:1087-1095.
    • (2005) Nat. Immunol. , vol.6 , pp. 1087-1095
    • Sato, S.1
  • 40
    • 27744577296 scopus 로고    scopus 로고
    • TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivo
    • Shim J.H., et al. TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivo. Genes Dev. 2005, 19:2668-2681.
    • (2005) Genes Dev. , vol.19 , pp. 2668-2681
    • Shim, J.H.1
  • 42
    • 79955481873 scopus 로고    scopus 로고
    • Crystal structure of inhibitor of κB kinase β
    • Xu G., et al. Crystal structure of inhibitor of κB kinase β. Nature 2011, 472:325-330.
    • (2011) Nature , vol.472 , pp. 325-330
    • Xu, G.1
  • 43
    • 33645703930 scopus 로고    scopus 로고
    • Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-κB activation
    • Wu C.J., et al. Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-κB activation. Nat. Cell Biol. 2006, 8:398-406.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 398-406
    • Wu, C.J.1
  • 44
    • 77953108542 scopus 로고    scopus 로고
    • The diversity of ubiquitin recognition: hot spots and varied specificity
    • Winget J.M., Mayor T. The diversity of ubiquitin recognition: hot spots and varied specificity. Mol. Cell 2010, 38:627-635.
    • (2010) Mol. Cell , vol.38 , pp. 627-635
    • Winget, J.M.1    Mayor, T.2
  • 45
    • 44649166613 scopus 로고    scopus 로고
    • Ubiquitin binding mediates the NF-κB inhibitory potential of ABIN proteins
    • Wagner S., et al. Ubiquitin binding mediates the NF-κB inhibitory potential of ABIN proteins. Oncogene 2008, 27:3739-3745.
    • (2008) Oncogene , vol.27 , pp. 3739-3745
    • Wagner, S.1
  • 46
    • 70350020147 scopus 로고    scopus 로고
    • NEMO specifically recognizes K63-linked poly-ubiquitin chains through a new bipartite ubiquitin-binding domain
    • Laplantine E., et al. NEMO specifically recognizes K63-linked poly-ubiquitin chains through a new bipartite ubiquitin-binding domain. EMBO J. 2009, 28:2885-2895.
    • (2009) EMBO J. , vol.28 , pp. 2885-2895
    • Laplantine, E.1
  • 47
    • 62549155321 scopus 로고    scopus 로고
    • Specific recognition of linear ubiquitin chains by NEMO is important for NF-κB activation
    • Rahighi S., et al. Specific recognition of linear ubiquitin chains by NEMO is important for NF-κB activation. Cell 2009, 136:1098-1109.
    • (2009) Cell , vol.136 , pp. 1098-1109
    • Rahighi, S.1
  • 48
    • 0036771830 scopus 로고    scopus 로고
    • The NF-κB signalling pathway in human diseases: from incontinentia pigmenti to ectodermal dysplasias and immune-deficiency syndromes
    • Smahi A., et al. The NF-κB signalling pathway in human diseases: from incontinentia pigmenti to ectodermal dysplasias and immune-deficiency syndromes. Hum. Mol. Genet. 2002, 11:2371-2375.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2371-2375
    • Smahi, A.1
  • 49
    • 79961003254 scopus 로고    scopus 로고
    • A new mechanism of X-linked anhidrotic ectodermal dysplasia with immunodeficiency: impairment of ubiquitin binding despite normal folding of NEMO protein
    • Hubeau M., et al. A new mechanism of X-linked anhidrotic ectodermal dysplasia with immunodeficiency: impairment of ubiquitin binding despite normal folding of NEMO protein. Blood 2011, 118:926-935.
    • (2011) Blood , vol.118 , pp. 926-935
    • Hubeau, M.1
  • 50
    • 61649103747 scopus 로고    scopus 로고
    • Structural basis for recognition of diubiquitins by NEMO
    • Lo Y.C., et al. Structural basis for recognition of diubiquitins by NEMO. Mol. Cell 2009, 33:602-615.
    • (2009) Mol. Cell , vol.33 , pp. 602-615
    • Lo, Y.C.1
  • 51
    • 34548225910 scopus 로고    scopus 로고
    • Coordinated regulation of Toll-like receptor and NOD2 signaling by K63-linked polyubiquitin chains
    • Abbott D.W., et al. Coordinated regulation of Toll-like receptor and NOD2 signaling by K63-linked polyubiquitin chains. Mol. Cell. Biol. 2007, 27:6012-6025.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 6012-6025
    • Abbott, D.W.1
  • 52
    • 0345826149 scopus 로고    scopus 로고
    • Bcl10 activates the NF-κB pathway through ubiquitination of NEMO
    • Zhou H., et al. Bcl10 activates the NF-κB pathway through ubiquitination of NEMO. Nature 2004, 427:167-171.
    • (2004) Nature , vol.427 , pp. 167-171
    • Zhou, H.1
  • 53
    • 77956627845 scopus 로고    scopus 로고
    • "Without Ub I am nothing": NEMO as a multifunctional player in ubiquitin-mediated control of NF-κB activation
    • Gautheron J., Courtois G. "Without Ub I am nothing": NEMO as a multifunctional player in ubiquitin-mediated control of NF-κB activation. Cell. Mol. Life Sci. 2010, 67:3101-3113.
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 3101-3113
    • Gautheron, J.1    Courtois, G.2
  • 54
    • 36048999753 scopus 로고    scopus 로고
    • IAP antagonists induce autoubiquitination of c-IAPs, NF-κB activation, and TNFα-dependent apoptosis
    • Varfolomeev E., et al. IAP antagonists induce autoubiquitination of c-IAPs, NF-κB activation, and TNFα-dependent apoptosis. Cell 2007, 131:669-681.
    • (2007) Cell , vol.131 , pp. 669-681
    • Varfolomeev, E.1
  • 55
    • 36148954336 scopus 로고    scopus 로고
    • IAP antagonists target cIAP1 to induce TNFα-dependent apoptosis
    • Vince J.E., et al. IAP antagonists target cIAP1 to induce TNFα-dependent apoptosis. Cell 2007, 131:682-693.
    • (2007) Cell , vol.131 , pp. 682-693
    • Vince, J.E.1
  • 56
    • 71149105333 scopus 로고    scopus 로고
    • Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction
    • Haas T.L., et al. Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction. Mol. Cell 2009, 36:831-844.
    • (2009) Mol. Cell , vol.36 , pp. 831-844
    • Haas, T.L.1
  • 57
    • 84855517985 scopus 로고    scopus 로고
    • Specific recognition of linear ubiquitin chains by the Npl4 zinc finger (NZF) domain of the HOIL-1L subunit of the linear ubiquitin chain assembly complex
    • Sato Y., et al. Specific recognition of linear ubiquitin chains by the Npl4 zinc finger (NZF) domain of the HOIL-1L subunit of the linear ubiquitin chain assembly complex. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:20520-20525.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 20520-20525
    • Sato, Y.1
  • 58
    • 78650915537 scopus 로고    scopus 로고
    • Deubiquitinases in the regulation of NF-κB signaling
    • Harhaj E.W., Dixit V.M. Deubiquitinases in the regulation of NF-κB signaling. Cell Res. 2011, 21:22-39.
    • (2011) Cell Res. , vol.21 , pp. 22-39
    • Harhaj, E.W.1    Dixit, V.M.2
  • 59
    • 77449150629 scopus 로고    scopus 로고
    • CYLD: a tumor suppressor deubiquitinase regulating NF-κB activation and diverse biological processes
    • Sun S.C. CYLD: a tumor suppressor deubiquitinase regulating NF-κB activation and diverse biological processes. Cell Death Differ. 2010, 17:25-34.
    • (2010) Cell Death Differ. , vol.17 , pp. 25-34
    • Sun, S.C.1
  • 60
    • 77951622671 scopus 로고    scopus 로고
    • A20: from ubiquitin editing to tumour suppression
    • Hymowitz S.G., Wertz I.E. A20: from ubiquitin editing to tumour suppression. Nat. Rev. Cancer 2010, 10:332-341.
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 332-341
    • Hymowitz, S.G.1    Wertz, I.E.2
  • 61
    • 66049161737 scopus 로고    scopus 로고
    • A20 takes on tumors: tumor suppression by an ubiquitin-editing enzyme
    • Malynn B.A., Ma A. A20 takes on tumors: tumor suppression by an ubiquitin-editing enzyme. J. Exp. Med. 2009, 206:977-980.
    • (2009) J. Exp. Med. , vol.206 , pp. 977-980
    • Malynn, B.A.1    Ma, A.2
  • 62
    • 3943054838 scopus 로고    scopus 로고
    • De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-κB signalling
    • Wertz I.E., et al. De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-κB signalling. Nature 2004, 430:694-699.
    • (2004) Nature , vol.430 , pp. 694-699
    • Wertz, I.E.1
  • 63
    • 77649225756 scopus 로고    scopus 로고
    • Inhibition of NF-κB signaling by A20 through disruption of ubiquitin enzyme complexes
    • Shembade N., et al. Inhibition of NF-κB signaling by A20 through disruption of ubiquitin enzyme complexes. Science 2010, 327:1135-1139.
    • (2010) Science , vol.327 , pp. 1135-1139
    • Shembade, N.1
  • 64
    • 61949257849 scopus 로고    scopus 로고
    • RNF11, a new piece in the A20 puzzle
    • Jacque E., Ley S.C. RNF11, a new piece in the A20 puzzle. EMBO J. 2009, 28:455-456.
    • (2009) EMBO J. , vol.28 , pp. 455-456
    • Jacque, E.1    Ley, S.C.2
  • 65
    • 80051986818 scopus 로고    scopus 로고
    • The kinase IKKα inhibits activation of the transcription factor NF-κB by phosphorylating the regulatory molecule TAX1BP1
    • Shembade N., et al. The kinase IKKα inhibits activation of the transcription factor NF-κB by phosphorylating the regulatory molecule TAX1BP1. Nat. Immunol. 2011, 12:834-843.
    • (2011) Nat. Immunol. , vol.12 , pp. 834-843
    • Shembade, N.1
  • 66
    • 81355150892 scopus 로고    scopus 로고
    • Direct, noncatalytic mechanism of IKK inhibition by A20
    • Skaug B., et al. Direct, noncatalytic mechanism of IKK inhibition by A20. Mol. Cell 2011, 44:559-571.
    • (2011) Mol. Cell , vol.44 , pp. 559-571
    • Skaug, B.1
  • 67
    • 0042467554 scopus 로고    scopus 로고
    • Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-κB
    • Brummelkamp T.R., et al. Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-κB. Nature 2003, 424:797-801.
    • (2003) Nature , vol.424 , pp. 797-801
    • Brummelkamp, T.R.1
  • 68
    • 0041967054 scopus 로고    scopus 로고
    • The tumour suppressor CYLD negatively regulates NF-κB signalling by deubiquitination
    • Kovalenko A., et al. The tumour suppressor CYLD negatively regulates NF-κB signalling by deubiquitination. Nature 2003, 424:801-805.
    • (2003) Nature , vol.424 , pp. 801-805
    • Kovalenko, A.1
  • 69
    • 0042467558 scopus 로고    scopus 로고
    • CYLD is a deubiquitinating enzyme that negatively regulates NF-κB activation by TNFR family members
    • Trompouki E., et al. CYLD is a deubiquitinating enzyme that negatively regulates NF-κB activation by TNFR family members. Nature 2003, 424:793-796.
    • (2003) Nature , vol.424 , pp. 793-796
    • Trompouki, E.1
  • 70
    • 67349231313 scopus 로고    scopus 로고
    • Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains
    • Komander D., et al. Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains. EMBO Rep. 2009, 10:466-473.
    • (2009) EMBO Rep. , vol.10 , pp. 466-473
    • Komander, D.1
  • 71
    • 43749122598 scopus 로고    scopus 로고
    • NF-kappaB suppression by the deubiquitinating enzyme Cezanne: a novel negative feedback loop in pro-inflammatory signaling
    • Enesa K., et al. NF-kappaB suppression by the deubiquitinating enzyme Cezanne: a novel negative feedback loop in pro-inflammatory signaling. J. Biol. Chem. 2008, 283:7036-7045.
    • (2008) J. Biol. Chem. , vol.283 , pp. 7036-7045
    • Enesa, K.1
  • 72
    • 74049114641 scopus 로고    scopus 로고
    • Ubiquitin-specific peptidase 21 inhibits tumor necrosis factor alpha-induced nuclear factor kB activation via binding to and deubiquitinating receptor-interacting protein 1
    • Xu G., et al. Ubiquitin-specific peptidase 21 inhibits tumor necrosis factor alpha-induced nuclear factor kB activation via binding to and deubiquitinating receptor-interacting protein 1. J. Biol. Chem. 2010, 285:969-978.
    • (2010) J. Biol. Chem. , vol.285 , pp. 969-978
    • Xu, G.1
  • 73
    • 33751576420 scopus 로고    scopus 로고
    • Cutting edge: pivotal function of Ubc13 in thymocyte TCR signaling
    • Yamamoto M., et al. Cutting edge: pivotal function of Ubc13 in thymocyte TCR signaling. J. Immunol. 2006, 177:7520-7524.
    • (2006) J. Immunol. , vol.177 , pp. 7520-7524
    • Yamamoto, M.1
  • 74
    • 70349441058 scopus 로고    scopus 로고
    • Ubiquitin-binding domains - from structures to functions
    • Dikic I., et al. Ubiquitin-binding domains - from structures to functions. Nat. Rev. Mol. Cell Biol. 2009, 10:659-671.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 659-671
    • Dikic, I.1
  • 75
    • 77952336245 scopus 로고    scopus 로고
    • Distinct consequences of posttranslational modification by linear versus K63-linked polyubiquitin chains
    • Zhao S., Ulrich H.D. Distinct consequences of posttranslational modification by linear versus K63-linked polyubiquitin chains. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:7704-7709.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 7704-7709
    • Zhao, S.1    Ulrich, H.D.2
  • 76
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley D. Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu. Rev. Biochem. 2009, 78:477-513.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 477-513
    • Finley, D.1
  • 78
    • 67349132223 scopus 로고    scopus 로고
    • Physiological functions of the HECT family of ubiquitin ligases
    • Rotin D., Kumar S. Physiological functions of the HECT family of ubiquitin ligases. Nat. Rev. Mol. Cell Biol. 2009, 10:398-409.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 398-409
    • Rotin, D.1    Kumar, S.2
  • 79
    • 79957949190 scopus 로고    scopus 로고
    • UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids
    • Wenzel D.M., et al. UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature 2011, 474:105-108.
    • (2011) Nature , vol.474 , pp. 105-108
    • Wenzel, D.M.1
  • 80
    • 71449123070 scopus 로고    scopus 로고
    • Detection of sequential polyubiquitylation on a millisecond timescale
    • Pierce N.W., et al. Detection of sequential polyubiquitylation on a millisecond timescale. Nature 2009, 462:615-619.
    • (2009) Nature , vol.462 , pp. 615-619
    • Pierce, N.W.1
  • 81
    • 0028847989 scopus 로고
    • A ubiquitin mutant with specific defects in DNA repair and multiubiquitination
    • Spence J., et al. A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol. Cell. Biol. 1995, 15:1265-1273.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1265-1273
    • Spence, J.1
  • 82
    • 0041706156 scopus 로고    scopus 로고
    • A proteomics approach to understanding protein ubiquitination
    • Peng J., et al. A proteomics approach to understanding protein ubiquitination. Nat. Biotechnol. 2003, 21:921-926.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 921-926
    • Peng, J.1
  • 83
    • 67650620318 scopus 로고    scopus 로고
    • Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes
    • Reyes-Turcu F.E., et al. Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes. Annu. Rev. Biochem. 2009, 78:363-397.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 363-397
    • Reyes-Turcu, F.E.1
  • 84
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: structure and function of the deubiquitinases
    • Komander D., et al. Breaking the chains: structure and function of the deubiquitinases. Nat. Rev. Mol. Cell Biol. 2009, 10:550-563.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 550-563
    • Komander, D.1
  • 85
    • 70350461507 scopus 로고    scopus 로고
    • Building ubiquitin chains: E2 enzymes at work
    • Ye Y., Rape M. Building ubiquitin chains: E2 enzymes at work. Nat. Rev. Mol. Cell Biol. 2009, 10:755-764.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 755-764
    • Ye, Y.1    Rape, M.2
  • 86
    • 0033525582 scopus 로고    scopus 로고
    • Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair
    • Hofmann R.M., Pickart C.M. Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair. Cell 1999, 96:645-653.
    • (1999) Cell , vol.96 , pp. 645-653
    • Hofmann, R.M.1    Pickart, C.M.2
  • 87
    • 70350004240 scopus 로고    scopus 로고
    • Key role of Ubc5 and lysine-63 polyubiquitination in viral activation of IRF3
    • Zeng W., et al. Key role of Ubc5 and lysine-63 polyubiquitination in viral activation of IRF3. Mol. Cell 2009, 36:315-325.
    • (2009) Mol. Cell , vol.36 , pp. 315-325
    • Zeng, W.1


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