메뉴 건너뛰기




Volumn 153, Issue 6, 2013, Pages 1312-

XOTULIN antagonizes LUBAC signaling by specifically hydrolyzing met1-linked polyubiquitin

Author keywords

[No Author keywords available]

Indexed keywords

I KAPPA B KINASE BETA; MET 1 PROTEIN; OTULIN PROTEIN; POLYUBIQUITIN; PROTEIN; PROTEINASE; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 84878862687     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2013.05.014     Document Type: Article
Times cited : (389)

References (56)
  • 1
    • 0030746105 scopus 로고    scopus 로고
    • In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome
    • Amerik AYu, S. Swaminathan, B.A. Krantz, K.D. Wilkinson, and M. Hochstrasser In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome EMBO J. 16 1997 4826 4838
    • (1997) EMBO J. , vol.16 , pp. 4826-4838
    • Ayu, A.1    Swaminathan, S.2    Krantz, B.A.3    Wilkinson, K.D.4    Hochstrasser, M.5
  • 2
    • 79955620198 scopus 로고    scopus 로고
    • Constructing and decoding unconventional ubiquitin chains
    • C. Behrends, and J.W. Harper Constructing and decoding unconventional ubiquitin chains Nat. Struct. Mol. Biol. 18 2011 520 528
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 520-528
    • Behrends, C.1    Harper, J.W.2
  • 5
    • 0030093114 scopus 로고    scopus 로고
    • A flexible motif search technique based on generalized profiles
    • P. Bucher, K. Karplus, N. Moeri, and K. Hofmann A flexible motif search technique based on generalized profiles Comput. Chem. 20 1996 3 23
    • (1996) Comput. Chem. , vol.20 , pp. 3-23
    • Bucher, P.1    Karplus, K.2    Moeri, N.3    Hofmann, K.4
  • 11
    • 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
    • T.L. Haas, C.H. Emmerich, B. Gerlach, A.C. Schmukle, S.M. Cordier, E. Rieser, R. Feltham, J. Vince, U. Warnken, and T. Wenger Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction Mol. Cell 36 2009 831 844
    • (2009) Mol. Cell , vol.36 , pp. 831-844
    • Haas, T.L.1    Emmerich, C.H.2    Gerlach, B.3    Schmukle, A.C.4    Cordier, S.M.5    Rieser, E.6    Feltham, R.7    Vince, J.8    Warnken, U.9    Wenger, T.10
  • 12
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-kappaB signaling
    • M.S. Hayden, and S. Ghosh Shared principles in NF-kappaB signaling Cell 132 2008 344 362
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 14
    • 77951622671 scopus 로고    scopus 로고
    • A20: From ubiquitin editing to tumour suppression
    • S.G. Hymowitz, and I.E. Wertz A20: from ubiquitin editing to tumour suppression Nat. Rev. Cancer 10 2010 332 341
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 332-341
    • Hymowitz, S.G.1    Wertz, I.E.2
  • 17
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-[kappa]B activity
    • M. Karin, and Y. Ben-Neriah Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity Annu. Rev. Immunol. 18 2000 621 663
    • (2000) Annu. Rev. Immunol. , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 22
    • 84864222562 scopus 로고    scopus 로고
    • Atypical ubiquitylation - The unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages
    • Y. Kulathu, and D. Komander Atypical ubiquitylation - the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages Nat. Rev. Mol. Cell Biol. 13 2012 508 523
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 508-523
    • Kulathu, Y.1    Komander, D.2
  • 25
    • 84878832998 scopus 로고    scopus 로고
    • OTU Deubiquitinases Reveal Mechanisms of Linkage Specificity and Enable Ubiquitin Chain Restriction Analysis
    • 10.1016/j.cell.2013.05.046 Published online July 3, 2013
    • T.E. Mevissen, M.K. Hospenthal, P.P. Geurink, P.R. Elliott, M. Akutsu, N. Arnaudo, R. Ekkebus, Y. Kulathu, T. Wauer, and F. El Oualid OTU Deubiquitinases Reveal Mechanisms of Linkage Specificity and Enable Ubiquitin Chain Restriction Analysis Cell 154 2013 10.1016/j.cell.2013.05.046 Published online July 3, 2013
    • (2013) Cell , vol.154
    • Mevissen, T.E.1    Hospenthal, M.K.2    Geurink, P.P.3    Elliott, P.R.4    Akutsu, M.5    Arnaudo, N.6    Ekkebus, R.7    Kulathu, Y.8    Wauer, T.9    El Oualid, F.10
  • 28
    • 0021679940 scopus 로고
    • The yeast ubiquitin gene: Head-to-tail repeats encoding a polyubiquitin precursor protein
    • E. Ozkaynak, D. Finley, and A. Varshavsky The yeast ubiquitin gene: head-to-tail repeats encoding a polyubiquitin precursor protein Nature 312 1984 663 666
    • (1984) Nature , vol.312 , pp. 663-666
    • Ozkaynak, E.1    Finley, D.2    Varshavsky, A.3
  • 30
    • 84867096523 scopus 로고    scopus 로고
    • The E3 ligase HOIP specifies linear ubiquitin chain assembly through its RING-IBR-RING domain and the unique LDD extension
    • J.J. Smit, D. Monteferrario, S.M. Noordermeer, W.J. van Dijk, B.A. van der Reijden, and T.K. Sixma The E3 ligase HOIP specifies linear ubiquitin chain assembly through its RING-IBR-RING domain and the unique LDD extension EMBO J. 31 2012 3833 3844
    • (2012) EMBO J. , vol.31 , pp. 3833-3844
    • Smit, J.J.1    Monteferrario, D.2    Noordermeer, S.M.3    Van Dijk, W.J.4    Van Der Reijden, B.A.5    Sixma, T.K.6
  • 32
    • 77449150629 scopus 로고    scopus 로고
    • CYLD: A tumor suppressor deubiquitinase regulating NF-kappaB activation and diverse biological processes
    • S.-C. Sun CYLD: a tumor suppressor deubiquitinase regulating NF-kappaB activation and diverse biological processes Cell Death Differ. 17 2010 25 34
    • (2010) Cell Death Differ. , vol.17 , pp. 25-34
    • Sun, S.-C.1
  • 33
    • 84862248877 scopus 로고    scopus 로고
    • LUBAC, a novel ubiquitin ligase for linear ubiquitination, is crucial for inflammation and immune responses
    • F. Tokunaga, and K. Iwai LUBAC, a novel ubiquitin ligase for linear ubiquitination, is crucial for inflammation and immune responses Microbes Infect. 14 2012 563 572
    • (2012) Microbes Infect. , vol.14 , pp. 563-572
    • Tokunaga, F.1    Iwai, K.2
  • 37
    • 77956903406 scopus 로고    scopus 로고
    • Engineered diubiquitin synthesis reveals Lys29-isopeptide specificity of an OTU deubiquitinase
    • S. Virdee, Y. Ye, D.P. Nguyen, D. Komander, and J.W. Chin Engineered diubiquitin synthesis reveals Lys29-isopeptide specificity of an OTU deubiquitinase Nat. Chem. Biol. 6 2010 750 757
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 750-757
    • Virdee, S.1    Ye, Y.2    Nguyen, D.P.3    Komander, D.4    Chin, J.W.5
  • 38
    • 84858124845 scopus 로고    scopus 로고
    • Generation and physiological roles of linear ubiquitin chains
    • H. Walczak, K. Iwai, and I. Dikic Generation and physiological roles of linear ubiquitin chains BMC Biol. 10 2012 23
    • (2012) BMC Biol. , vol.10 , pp. 23
    • Walczak, H.1    Iwai, K.2    Dikic, I.3
  • 39
    • 79952290609 scopus 로고    scopus 로고
    • The mechanism of linkage-specific ubiquitin chain elongation by a single-subunit E2
    • K.E. Wickliffe, S. Lorenz, D.E. Wemmer, J. Kuriyan, and M. Rape The mechanism of linkage-specific ubiquitin chain elongation by a single-subunit E2 Cell 144 2011 769 781
    • (2011) Cell , vol.144 , pp. 769-781
    • Wickliffe, K.E.1    Lorenz, S.2    Wemmer, D.E.3    Kuriyan, J.4    Rape, M.5
  • 40
    • 84862806447 scopus 로고    scopus 로고
    • The mechanism of OTUB1-mediated inhibition of ubiquitination
    • R. Wiener, X. Zhang, T. Wang, and C. Wolberger The mechanism of OTUB1-mediated inhibition of ubiquitination Nature 483 2012 618 622
    • (2012) Nature , vol.483 , pp. 618-622
    • Wiener, R.1    Zhang, X.2    Wang, T.3    Wolberger, C.4
  • 41
    • 70350015537 scopus 로고    scopus 로고
    • A ubiquitin replacement strategy in human cells reveals distinct mechanisms of IKK activation by TNFalpha and IL-1beta
    • M. Xu, B. Skaug, W. Zeng, and Z.J. Chen A ubiquitin replacement strategy in human cells reveals distinct mechanisms of IKK activation by TNFalpha and IL-1beta Mol. Cell 36 2009 302 314
    • (2009) Mol. Cell , vol.36 , pp. 302-314
    • Xu, M.1    Skaug, B.2    Zeng, W.3    Chen, Z.J.4
  • 42
    • 79953314427 scopus 로고    scopus 로고
    • Polyubiquitin binding and cross-reactivity in the USP domain deubiquitinase USP21
    • Y. Ye, M. Akutsu, F. Reyes-Turcu, R.I. Enchev, K.D. Wilkinson, and D. Komander Polyubiquitin binding and cross-reactivity in the USP domain deubiquitinase USP21 EMBO Rep. 12 2011 350 357
    • (2011) EMBO Rep. , vol.12 , pp. 350-357
    • Ye, Y.1    Akutsu, M.2    Reyes-Turcu, F.3    Enchev, R.I.4    Wilkinson, K.D.5    Komander, D.6
  • 44
    • 79952301200 scopus 로고    scopus 로고
    • Molecular basis for ubiquitin and ISG15 cross-reactivity in viral ovarian tumor domains
    • M. Akutsu, Y. Ye, S. Virdee, J.W. Chin, and D. Komander Molecular basis for ubiquitin and ISG15 cross-reactivity in viral ovarian tumor domains Proc. Natl. Acad. Sci. USA 108 2011 2228 2233
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 2228-2233
    • Akutsu, M.1    Ye, Y.2    Virdee, S.3    Chin, J.W.4    Komander, D.5
  • 47
    • 77955417276 scopus 로고    scopus 로고
    • Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne
    • A. Bremm, S.M.V. Freund, and D. Komander Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne Nat. Struct. Mol. Biol. 17 2010 939 947
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 939-947
    • Bremm, A.1    Freund, S.M.V.2    Komander, D.3
  • 50
  • 51
    • 0037100671 scopus 로고    scopus 로고
    • MAFFT: A novel method for rapid multiple sequence alignment based on fast Fourier transform
    • K. Katoh, K. Misawa, K.-I. Kuma, and T. Miyata MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform Nucleic Acids Res. 30 2002 3059 3066
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3059-3066
    • Katoh, K.1    Misawa, K.2    Kuma, K.-I.3    Miyata, T.4
  • 52
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • G. Langer, S.X. Cohen, V.S. Lamzin, and A. Perrakis Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7 Nat. Protoc. 3 2008 1171 1179
    • (2008) Nat. Protoc. , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 54
    • 28844462033 scopus 로고    scopus 로고
    • Controlled synthesis of polyubiquitin chains
    • C.M. Pickart, and S. Raasi Controlled synthesis of polyubiquitin chains Methods Enzymol. 399 2005 21 36
    • (2005) Methods Enzymol. , vol.399 , pp. 21-36
    • Pickart, C.M.1    Raasi, S.2
  • 55
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • G.M. Sheldrick A short history of SHELX Acta Crystallogr. A 64 2008 112 122
    • (2008) Acta Crystallogr. A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 56
    • 16344373015 scopus 로고    scopus 로고
    • Protein homology detection by HMM-HMM comparison
    • J. Söding Protein homology detection by HMM-HMM comparison Bioinformatics 21 2005 951 960
    • (2005) Bioinformatics , vol.21 , pp. 951-960
    • Söding, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.