메뉴 건너뛰기




Volumn 10, Issue 7, 2009, Pages 706-713

Linear polyubiquitination: A new regulator of NF-κB activation

Author keywords

[No Author keywords available]

Indexed keywords

A20 BINDING INHIBITOR OF IMMUNOGLOBULIN ENHANCER BINDING PROTEIN 1; HOIL IL INTERACTING PROTEIN; I KAPPA B; I KAPPA B KINASE ALPHA; I KAPPA B KINASE BETA; I KAPPA B KINASE GAMMA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LINEAR UBIQUITIN BINDING CHAIN ASSEMBLY COMPLEX; LONGER ISOFORM OF HAEM OXIDIZED IRON REGULATORY PROTEIN UBIQUITIN LIGASE 1; POLYUBIQUITIN; PROTEIN K63; STRESS ACTIVATED PROTEIN KINASE; TRANSFORMING GROWTH FACTOR BETA ACTIVATED KINASE 1; TRANSFORMING GROWTH FACTOR BETA ACTIVATED KINASE 1 BINDING PROTEIN; TRANSFORMING GROWTH FACTOR BETA ACTIVATED KINASE 1 BINDING PROTEIN 2; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR ALPHA RECEPTOR; TUMOR NECROSIS FACTOR ALPHA RECEPTOR 1; UBIQUITIN ASSOCIATED; UBIQUITIN CONJUGATING ENZYME E2; UBIQUITIN LIKE; UNCLASSIFIED DRUG;

EID: 67650064603     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.1038/embor.2009.144     Document Type: Review
Times cited : (190)

References (53)
  • 2
    • 0026607096 scopus 로고
    • Early hydrogen-bonding events in the folding reaction of ubiquitin
    • Briggs MS, Roder H (1992) Early hydrogen-bonding events in the folding reaction of ubiquitin. Proc Natl Acad Sci USA 89:2017-2021
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2017-2021
    • Briggs, M.S.1    Roder, H.2
  • 3
    • 0042467554 scopus 로고    scopus 로고
    • Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-κB
    • Brummelkamp TR, Nijman SM, Dirac AM, Bernards R (2003) Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-κB. Nature 424: 797-801
    • (2003) Nature , vol.424 , pp. 797-801
    • Brummelkamp, T.R.1    Nijman, S.M.2    Dirac, A.M.3    Bernards, R.4
  • 5
  • 7
    • 0025644201 scopus 로고
    • A 25-kilodalton ubiquitin carrier protein (E2) catalyzes multi-ubiquitin chain synthesis via lysine 48 of ubiquitin
    • Chen Z, Pickart CM (1990) A 25-kilodalton ubiquitin carrier protein (E2) catalyzes multi-ubiquitin chain synthesis via lysine 48 of ubiquitin. J Biol Chem 265:21835-21842
    • (1990) J Biol Chem , vol.265 , pp. 21835-21842
    • Chen, Z.1    Pickart, C.M.2
  • 8
    • 59649086030 scopus 로고    scopus 로고
    • Nonproteolytic functions of ubiquitin in cell signaling
    • Chen ZJ, Sun LJ (2009) Nonproteolytic functions of ubiquitin in cell signaling. Mol Cell 33:275-286
    • (2009) Mol Cell , vol.33 , pp. 275-286
    • Chen, Z.J.1    Sun, L.J.2
  • 9
    • 65249083913 scopus 로고    scopus 로고
    • Ubiquitin in NF-κB signaling
    • Chiu YH, Zhao M, Chen ZJ (2009) Ubiquitin in NF-κB signaling. Chem Rev 109:1549-1560
    • (2009) Chem Rev , vol.109 , pp. 1549-1560
    • Chiu, Y.H.1    Zhao, M.2    Chen, Z.J.3
  • 10
    • 0018187738 scopus 로고
    • A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes
    • Ciechanover A, Hod Y, Hershko A (1978) A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes. Biochem Biophys Res Commun 81: 1100-1105
    • (1978) Biochem Biophys Res Commun , vol.81 , pp. 1100-1105
    • Ciechanover, A.1    Hod, Y.2    Hershko, A.3
  • 11
    • 8744275653 scopus 로고    scopus 로고
    • Characteristics of mycobacterial infection in patients with immunodeficiency and nuclear factor-κB essential modulator mutation, with or without ectodermal dysplasia
    • Dai YS, Liang MG, Gellis SE, Bonilla FA, Schneider LC, Geha RS, Orange JS (2004) Characteristics of mycobacterial infection in patients with immunodeficiency and nuclear factor-κB essential modulator mutation, with or without ectodermal dysplasia. J Am Acad Dermatol 51: 718-722
    • (2004) J Am Acad Dermatol , vol.51 , pp. 718-722
    • Dai, Y.S.1    Liang, M.G.2    Gellis, S.E.3    Bonilla, F.A.4    Schneider, L.C.5    Geha, R.S.6    Orange, J.S.7
  • 12
    • 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, Wang C, Spencer E, Yang L, Braun A, You J, Slaughter C, Pickart C, Chen ZJ (2000) Activation of the IκB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell 103: 351-361
    • (2000) Cell , vol.103 , pp. 351-361
    • Deng, L.1    Wang, C.2    Spencer, E.3    Yang, L.4    Braun, A.5    You, J.6    Slaughter, C.7    Pickart, C.8    Chen, Z.J.9
  • 13
    • 34347265174 scopus 로고    scopus 로고
    • Structural mechanisms underlying posttranslational modification by ubiquitin-like proteins
    • Dye BT, Schulman BA (2007) Structural mechanisms underlying posttranslational modification by ubiquitin-like proteins. Annu Rev Biophy's Biomol Struct 36: 131-150
    • (2007) Annu Rev Biophy's Biomol Struct , vol.36 , pp. 131-150
    • Dye, B.T.1    Schulman, B.A.2
  • 14
    • 33646034316 scopus 로고    scopus 로고
    • Attivation of IKK byTNFα requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO
    • Ea CK, Deng L, Xia ZP, Pineda G, Chen ZJ (2006) Attivation of IKK byTNFα requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO. Mol Cell 22:245-257
    • (2006) Mol Cell , vol.22 , pp. 245-257
    • Ea, C.K.1    Deng, L.2    Xia, Z.P.3    Pineda, G.4    Chen, Z.J.5
  • 15
    • 0023666139 scopus 로고
    • The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses
    • Finley D, Ozkaynak E, Varshavsky A (1987) The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses. Cell 48:1035-1046
    • (1987) Cell , vol.48 , pp. 1035-1046
    • Finley, D.1    Ozkaynak, E.2    Varshavsky, A.3
  • 16
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A (2002) The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction. Physiol Rev 82: 373-428
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 17
    • 39049183044 scopus 로고    scopus 로고
    • Regulation and function of IKK and IKK-related kinases
    • Hacker H, Karin M (2006) Regulation and function of IKK and IKK-related kinases. Sci STKE 2006: Re13
    • (2006) Sci STKE , vol.2006
    • Hacker, H.1    Karin, M.2
  • 18
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-κB signaling
    • Hayden MS, Ghosh S (2008) Shared principles in NF-κB signaling. Cell 132: 344-362
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 19
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins
    • Hicke L, Dunn R (2003) Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu Rev Cell Dev Biol 19: 141-172
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 20
    • 30344482590 scopus 로고    scopus 로고
    • Lingering mysteries of ubiquitin-chain assembly
    • Hochstrasser M (2006) Lingering mysteries of ubiquitin-chain assembly. Cell 124: 27-34
    • (2006) Cell , vol.124 , pp. 27-34
    • Hochstrasser, M.1
  • 21
    • 0033525582 scopus 로고    scopus 로고
    • Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair
    • Hofmann PM, Pickart CM (1999) Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair. Cell 96: 645-653
    • (1999) Cell , vol.96 , pp. 645-653
    • Hofmann, P.M.1    Pickart, C.M.2
  • 22
    • 44649101850 scopus 로고    scopus 로고
    • Atypical ubiquitin chains: New molecular signals. 'Protein Modifications: Beyond the Usual Suspects' review series
    • Ikeda F, Dikic I (2008) Atypical ubiquitin chains: New molecular signals. 'Protein Modifications: Beyond the Usual Suspects' review series. EMBO Rep 9: 536-542
    • (2008) EMBO Rep , vol.9 , pp. 536-542
    • Ikeda, F.1    Dikic, I.2
  • 23
    • 43049162227 scopus 로고    scopus 로고
    • Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex
    • Jin L, Williamson A, Banerjee S, Philipp I, Rape M (2008) Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex. Cell 133: 653-665
    • (2008) Cell , vol.133 , pp. 653-665
    • Jin, L.1    Williamson, A.2    Banerjee, S.3    Philipp, I.4    Rape, M.5
  • 24
    • 33749346301 scopus 로고    scopus 로고
    • Modification of proteins by ubiquitin and ubiquitin-like proteins
    • Kerscher O, Felberbaum R, Hochstrasser M (2006) Modification of proteins by ubiquitin and ubiquitin-like proteins. Annu Rev Cell Dev Biol 22: 159-180
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 159-180
    • Kerscher, O.1    Felberbaum, R.2    Hochstrasser, M.3
  • 26
    • 0035370106 scopus 로고    scopus 로고
    • Functional redundancy of the zinc fingers of A20 for inhibition of NF-κB activation and protein-protein interactions
    • Klinkenberg M, Van Huffel S, Heyninck K, Beyaert R (2001) Functional redundancy of the zinc fingers of A20 for inhibition of NF-κB activation and protein-protein interactions. FEBS Lett 498 93-97
    • (2001) FEBS Lett , vol.498 , pp. 93-97
    • Klinkenberg, M.1    Van Huffel, S.2    Heyninck, K.3    Beyaert, R.4
  • 31
    • 33750497452 scopus 로고    scopus 로고
    • Mutual regulation of conventional protein kinase C and a ubiquitin ligase complex
    • Nakamura M, Tokunaga F, Sakata S, Iwai K (2006) Mutual regulation of conventional protein kinase C and a ubiquitin ligase complex. Biochem Biophys Res Commun 351: 340-347
    • (2006) Biochem Biophys Res Commun , vol.351 , pp. 340-347
    • Nakamura, M.1    Tokunaga, F.2    Sakata, S.3    Iwai, K.4
  • 32
    • 60149104060 scopus 로고    scopus 로고
    • ABIN-T is a ubiquitin sensor that restricts cell death and sustains embryonic development
    • Oshima S et al (2009) ABIN-T is a ubiquitin sensor that restricts cell death and sustains embryonic development. Nature 457: 906-909
    • (2009) Nature , vol.457 , pp. 906-909
    • Oshima, S.1
  • 34
    • 8844237615 scopus 로고    scopus 로고
    • Polyubiquitin chains: Polymeric protein signals
    • Pickart CM, Fushman D (2004) Polyubiquitin chains: Polymeric protein signals. Curr Opin Chem Biol 8: 610-616
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 610-616
    • Pickart, C.M.1    Fushman, D.2
  • 35
    • 62549155321 scopus 로고    scopus 로고
    • Specific recognition of linear ubiquitin chains by NEMO is important for NF-κB activation
    • Rahighi S et al (2009) Specific recognition of linear ubiquitin chains by NEMO is important for NF-κB activation. Cell 136: 1098-1109
    • (2009) Cell , vol.136 , pp. 1098-1109
    • Rahighi, S.1
  • 36
    • 65249186662 scopus 로고    scopus 로고
    • Polyubiquitin binding and disassembly by deubiquitinating enzymes
    • Reyes-Turcu FE, Wilkinson KD (2009) Polyubiquitin binding and disassembly by deubiquitinating enzymes. Chem Rev 109: 1495-1508
    • (2009) Chem Rev , vol.109 , pp. 1495-1508
    • Reyes-Turcu, F.E.1    Wilkinson, K.D.2
  • 37
    • 33646066025 scopus 로고    scopus 로고
    • The ubiquitin bindring domain ZnF UBP recognizes the C-terminal diglycine motif of unanchored ubiquitin
    • Reyes-Turcu FE, Horton JR, Mullally JE, Heroux A, Cheng X, Wilkinson KD (2006) The ubiquitin bindring domain ZnF UBP recognizes the C-terminal diglycine motif of unanchored ubiquitin. Cell 124:1197-1208
    • (2006) Cell , vol.124 , pp. 1197-1208
    • Reyes-Turcu, F.E.1    Horton, J.R.2    Mullally, J.E.3    Heroux, A.4    Cheng, X.5    Wilkinson, K.D.6
  • 38
    • 42949159409 scopus 로고    scopus 로고
    • Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site
    • Rushe M et al (2008) Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure 16: 798-808
    • (2008) Structure , vol.16 , pp. 798-808
    • Rushe, M.1
  • 39
    • 34250007128 scopus 로고    scopus 로고
    • The mouse polyubiquitin gene UbC is essential for fetal liver development, cell-cycle progression and stress tolerance
    • Ryu KY, Maehr R, Gilchrist CA, Long MA, Bouley DM, Mueller B, Ploegh HL, Kopito RR (2007) The mouse polyubiquitin gene UbC is essential for fetal liver development, cell-cycle progression and stress tolerance. EMBO J 26: 2693-2706
    • (2007) EMBO J , vol.26 , pp. 2693-2706
    • Ryu, K.Y.1    Maehr, R.2    Gilchrist, C.A.3    Long, M.A.4    Bouley, D.M.5    Mueller, B.6    Ploegh, H.L.7    Kopito, R.R.8
  • 41
    • 27744577296 scopus 로고    scopus 로고
    • TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivo
    • Shim JH et al (2005) TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivo. Genes Dev 19: 2668-2681
    • (2005) Genes Dev , vol.19 , pp. 2668-2681
    • Shim, J.H.1
  • 42
    • 0028847989 scopus 로고
    • A ubiquitin mutant with specific defects in DNA repair and multiubiquitination
    • Spence J, Sadis S, Haas AL, Finley D (1995) A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol Cell Biol 15: 1265-1273
    • (1995) Mol Cell Biol , vol.15 , pp. 1265-1273
    • Spence, J.1    Sadis, S.2    Haas, A.L.3    Finley, D.4
  • 43
    • 34447118188 scopus 로고    scopus 로고
    • RBCK1 negatively regulates tumor necrosis factor- and interleukin-1-triggered NF-κB activation by targeting TAB2/3 for degradation
    • Tian Y, Zhang Y, Zhong B, Wang YY, Diao FC, Wang RP, Zhang M, Chen DY, Zhai ZH, Shu HB (2007) RBCK1 negatively regulates tumor necrosis factor- and interleukin-1-triggered NF-κB activation by targeting TAB2/3 for degradation. J Biol Chem 282: 16776-16782
    • (2007) J Biol Chem , vol.282 , pp. 16776-16782
    • Tian, Y.1    Zhang, Y.2    Zhong, B.3    Wang, Y.Y.4    Diao, F.C.5    Wang, R.P.6    Zhang, M.7    Chen, D.Y.8    Zhai, Z.H.9    Shu, H.B.10
  • 44
    • 59649103156 scopus 로고    scopus 로고
    • Involvement of linear polyubiquitylation of NEMO in NF-κB activation
    • Tokunaga F et al (2009) Involvement of linear polyubiquitylation of NEMO in NF-κB activation. Nat Cell Biol 11: 123-132
    • (2009) Nat Cell Biol , vol.11 , pp. 123-132
    • Tokunaga, F.1
  • 45
    • 0042467558 scopus 로고    scopus 로고
    • CYLD is a deubiquitinating enzyme that negatively regulates NF-κB activation by TNFR family members
    • Trompouki E, Hatzivassiliou E, Tsichritzis T, Farmer H, Ashworth A, Mosialos G (2003) CYLD is a deubiquitinating enzyme that negatively regulates NF-κB activation by TNFR family members. Nature 424 793-796
    • (2003) Nature , vol.424 , pp. 793-796
    • Trompouki, E.1    Hatzivassiliou, E.2    Tsichritzis, T.3    Farmer, H.4    Ashworth, A.5    Mosialos, G.6
  • 46
    • 0034703437 scopus 로고    scopus 로고
    • Detecting and measuring cotranslational protein degradation in vivo
    • Turner GC, Varshavsky A (2000) Detecting and measuring cotranslational protein degradation in vivo. Science 289: 2117-2120
    • (2000) Science , vol.289 , pp. 2117-2120
    • Turner, G.C.1    Varshavsky, A.2
  • 47
    • 44649166613 scopus 로고    scopus 로고
    • Ubiquitin binding mediates the NF-κB inhibitory potential of ABIN proteins
    • Wagner S et al (2008) Ubiquitin binding mediates the NF-κB inhibitory potential of ABIN proteins. Oncogene 27: 3739-3745
    • (2008) Oncogene , vol.27 , pp. 3739-3745
    • Wagner, S.1
  • 49
    • 33645703930 scopus 로고    scopus 로고
    • Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-κB activation
    • Wu CJ, Conze DB, Li T, Srinivasula SM, Ashwell JD (2006) Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-κB activation. Nat Cell Biol 8: 398-406
    • (2006) Nat Cell Biol , vol.8 , pp. 398-406
    • Wu, C.J.1    Conze, D.B.2    Li, T.3    Srinivasula, S.M.4    Ashwell, J.D.5
  • 51
    • 33747615237 scopus 로고    scopus 로고
    • Key function for the Ubc13 E2 ubiquitin-conjugating enzyme in immune receptor signaling
    • Yamamoto M et al (2006a) Key function for the Ubc13 E2 ubiquitin-conjugating enzyme in immune receptor signaling. Nat Immunol 7: 962-970
    • (2006) Nat Immunol , vol.7 , pp. 962-970
    • Yamamoto, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.