메뉴 건너뛰기




Volumn 288, Issue 26, 2013, Pages 18939-18946

Auto-ubiquitination of Mdm2 enhances its substrate ubiquitin ligase activity

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; IONS;

EID: 84879582826     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.454470     Document Type: Article
Times cited : (51)

References (31)
  • 1
    • 0842303313 scopus 로고    scopus 로고
    • Back to the future with ubiquitin
    • Pickart, C. M. (2004) Back to the future with ubiquitin. Cell 116, 181-190
    • (2004) Cell , vol.116 , pp. 181-190
    • Pickart, C.M.1
  • 3
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • DOI 10.1038/nrm1547
    • Petroski, M. D., and Deshaies, R. J. (2005) Function and regulation of cullin-RING ubiquitin ligases. Nat. Rev. Mol. Cell Biol. 6, 9-20 (Pubitemid 40064895)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.1 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 4
    • 70350461507 scopus 로고    scopus 로고
    • Building ubiquitin chains: E2 enzymes at work
    • Ye, Y., and Rape, M. (2009) Building ubiquitin chains: E2 enzymes at work. Nat. Rev. Mol. Cell Biol. 10, 755-764
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 755-764
    • Ye, Y.1    Rape, M.2
  • 5
    • 27144495057 scopus 로고    scopus 로고
    • E2 conjugating enzymes must disengage from their E1 enzymes before E3-dependent ubiquitin and ubiquitin-like transfer
    • DOI 10.1038/nsmb984, PII N984
    • Eletr, Z. M., Huang, D. T., Duda, D. M., Schulman, B. A., and Kuhlman, B. (2005) E2 conjugating enzymes must disengage from their E1 enzymes before E3-dependent ubiquitin and ubiquitin-like transfer. Nat. Struct. Mol. Biol. 12, 933-934 (Pubitemid 41486719)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.10 , pp. 933-934
    • Eletr, Z.M.1    Huang, D.T.2    Duda, D.M.3    Schulman, B.A.4    Kuhlman, B.5
  • 6
    • 70450218366 scopus 로고    scopus 로고
    • Rapid E2-E3 assembly and disassembly enable processive ubiquitylation of cullin-RING ubiquitin ligase substrates
    • Kleiger, G., Saha, A., Lewis, S., Kuhlman, B., and Deshaies, R. J. (2009) Rapid E2-E3 assembly and disassembly enable processive ubiquitylation of cullin-RING ubiquitin ligase substrates. Cell 139, 957-968
    • (2009) Cell , vol.139 , pp. 957-968
    • Kleiger, G.1    Saha, A.2    Lewis, S.3    Kuhlman, B.4    Deshaies, R.J.5
  • 8
    • 65349103899 scopus 로고    scopus 로고
    • Blinded by the light: The growing complexity of p53
    • Vousden, K. H., and Prives, C. (2009) Blinded by the light: the growing complexity of p53. Cell 137, 413-431
    • (2009) Cell , vol.137 , pp. 413-431
    • Vousden, K.H.1    Prives, C.2
  • 9
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • DOI 10.1038/387296a0
    • Haupt, Y., Maya, R., Kazaz, A., and Oren, M. (1997) Mdm2 promotes the rapid degradation of p53. Nature 387, 296-299 (Pubitemid 27220766)
    • (1997) Nature , vol.387 , Issue.6630 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 10
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • DOI 10.1038/387299a0
    • Kubbutat, M. H., Jones, S. N., and Vousden, K. H. (1997) Regulation of p53 stability by Mdm2. Nature 387, 299-303 (Pubitemid 27220767)
    • (1997) Nature , vol.387 , Issue.6630 , pp. 299-303
    • Kubbutat, M.H.G.1    Jones, S.N.2    Vousden, K.H.3
  • 11
    • 0032512057 scopus 로고    scopus 로고
    • Mdm2 association with p53 targets its ubiquitination
    • Fuchs, S. Y., Adler, V., Buschmann, T., Wu, X., and Ronai, Z. (1998)Mdm2 association with p53 targets its ubiquitination. Oncogene 17, 2543-2547 (Pubitemid 28544725)
    • (1998) Oncogene , vol.17 , Issue.19 , pp. 2543-2547
    • Fuchs, S.Y.1    Adler, V.2    Buschmann, T.3    Wu, X.4    Ronai, Z.5
  • 12
    • 35148847384 scopus 로고    scopus 로고
    • Targeted Inactivation of Mdm2 RING Finger E3 Ubiquitin Ligase Activity in the Mouse Reveals Mechanistic Insights into p53 Regulation
    • DOI 10.1016/j.ccr.2007.09.007, PII S1535610807002668
    • Itahana, K., Mao, H., Jin, A., Itahana, Y., Clegg, H. V., Lindström, M. S., Bhat, K. P., Godfrey, V. L., Evan, G. I., and Zhang, Y. (2007) Targeted inactivation of Mdm2 RING finger E3 ubiquitin ligase activity in the mouse reveals mechanistic insights into p53 regulation. Cancer Cell 12, 355-366 (Pubitemid 47539309)
    • (2007) Cancer Cell , vol.12 , Issue.4 , pp. 355-366
    • Itahana, K.1    Mao, H.2    Jin, A.3    Itahana, Y.4    Clegg, H.V.5    Lindstrom, M.S.6    Bhat, K.P.7    Godfrey, V.L.8    Evan, G.I.9    Zhang, Y.10
  • 14
    • 79952280229 scopus 로고    scopus 로고
    • p53 regulates biosynthesis through direct inactivation of glucose-6-phosphate dehydrogenase
    • Jiang, P., Du, W., Wang, X., Mancuso, A., Gao, X., Wu, M., and Yang, X. (2011) p53 regulates biosynthesis through direct inactivation of glucose-6-phosphate dehydrogenase. Nat. Cell Biol. 13, 310-316
    • (2011) Nat. Cell Biol. , vol.13 , pp. 310-316
    • Jiang, P.1    Du, W.2    Wang, X.3    Mancuso, A.4    Gao, X.5    Wu, M.6    Yang, X.7
  • 15
    • 33644850903 scopus 로고    scopus 로고
    • A UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination
    • DOI 10.1016/j.molcel.2006.02.008, PII S1097276506000906
    • Brzovic, P. S., Lissounov, A., Christensen, D. E., Hoyt, D. W., and Klevit, R. E. (2006) A UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination. Mol. Cell 21, 873-880 (Pubitemid 43376136)
    • (2006) Molecular Cell , vol.21 , Issue.6 , pp. 873-880
    • Brzovic, P.S.1    Lissounov, A.2    Christensen, D.E.3    Hoyt, D.W.4    Klevit, R.E.5
  • 16
    • 34447123808 scopus 로고    scopus 로고
    • RING domain-mediated interaction is a requirement for MDM2's E3 ligase activity
    • DOI 10.1158/0008-5472.CAN-07-1313
    • Kawai, H., Lopez-Pajares, V., Kim, M. M., Wiederschain, D., and Yuan, Z. M. (2007) RING domain-mediated interaction is a requirement for MDM2's E3 ligase activity. Cancer Res. 67, 6026-6030 (Pubitemid 47037481)
    • (2007) Cancer Research , vol.67 , Issue.13 , pp. 6026-6030
    • Kawai, H.1    Lopez-Pajares, V.2    Kim, M.M.3    Wiederschain, D.4    Yuan, Z.-M.5
  • 20
    • 33947243954 scopus 로고    scopus 로고
    • A ubiquitin ligase transfers preformed polyubiquitin chains from a conjugating enzyme to a substrate
    • DOI 10.1038/nature05542, PII NATURE05542
    • Li, W., Tu, D., Brunger, A. T., and Ye, Y. (2007)Aubiquitin ligase transfers preformed polyubiquitin chains from a conjugating enzyme to a substrate. Nature 446, 333-337 (Pubitemid 46426147)
    • (2007) Nature , vol.446 , Issue.7133 , pp. 333-337
    • Li, W.1    Tu, D.2    Brunger, A.T.3    Ye, Y.4
  • 23
    • 0032478179 scopus 로고    scopus 로고
    • The hydrophobic effect contributes to polyubiquitin chain recognition
    • DOI 10.1021/bi972514p
    • Beal, R. E., Toscano-Cantaffa, D., Young, P., Rechsteiner, M., and Pickart, C. M. (1998) The hydrophobic effect contributes to polyubiquitin chain recognition. Biochemistry 37, 2925-2934 (Pubitemid 28145745)
    • (1998) Biochemistry , vol.37 , Issue.9 , pp. 2925-2934
    • Beal, R.E.1    Toscano-Cantaffa, D.2    Young, P.3    Rechsteiner, M.4    Pickart, C.M.5
  • 24
    • 0042466637 scopus 로고    scopus 로고
    • Interdimer processing mechanism of procaspase-8 activation
    • DOI 10.1093/emboj/cdg414
    • Chang, D. W., Xing, Z., Capacio, V. L., Peter, M. E., and Yang, X. (2003) Interdimer processing mechanism of procaspase-8 activation. EMBO J. 22, 4132-4142 (Pubitemid 37021742)
    • (2003) EMBO Journal , vol.22 , Issue.16 , pp. 4132-4142
    • Chang, D.W.1    Xing, Z.2    Capacio, V.L.3    Peter, M.E.4    Yang, X.5
  • 25
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Lemmon, M. A., and Schlessinger, J. (2010) Cell signaling by receptor tyrosine kinases. Cell 141, 1117-1134
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 26
    • 0034440818 scopus 로고    scopus 로고
    • Proteases for cell suicide: Functions and regulation of caspases
    • DOI 10.1128/MMBR.64.4.821-846.2000
    • Chang, H. Y., and Yang, X. (2000) Proteases for cell suicide: functions and regulation of caspases. Microbiol. Mol. Biol. Rev. 64, 821-846 (Pubitemid 32475932)
    • (2000) Microbiology and Molecular Biology Reviews , vol.64 , Issue.4 , pp. 821-846
    • Chang, H.Y.1    Yang, X.2
  • 27
    • 0031615875 scopus 로고    scopus 로고
    • Autoproteolytic activation of pro-caspases by oligomerization
    • Yang, X., Chang, H. Y., and Baltimore, D. (1998) Autoproteolytic activation of pro-caspases by oligomerization. Mol. Cell 1, 319-325 (Pubitemid 128378672)
    • (1998) Molecular Cell , vol.1 , Issue.2 , pp. 319-325
    • Yang, X.1    Chang, H.Y.2    Baltimore, D.3
  • 28
    • 0033051322 scopus 로고    scopus 로고
    • MDM2 interacts with MDMX through their RING finger domains
    • DOI 10.1016/S0014-5793(99)00254-9, PII S0014579399002549
    • Tanimura, S., Ohtsuka, S., Mitsui, K., Shirouzu, K., Yoshimura, A., and Ohtsubo, M. (1999) MDM2 interacts with MDMX through their RING finger domains. FEBS Lett. 447, 5-9 (Pubitemid 29134936)
    • (1999) FEBS Letters , vol.447 , Issue.1 , pp. 5-9
    • Tanimura, S.1    Ohtsuka, S.2    Mitsui, K.3    Shirouzu, K.4    Yoshimura, A.5    Ohtsubo, M.6
  • 29
    • 33846239416 scopus 로고    scopus 로고
    • The Mdm2 RING domain C-terminus is required for supramolecular assembly and ubiquitin ligase activity
    • DOI 10.1038/sj.emboj.7601465, PII 7601465
    • Poyurovsky, M. V., Priest, C., Kentsis, A., Borden, K. L., Pan, Z. Q., Pavletich, N., and Prives, C. (2007) The Mdm2 RING domain C-terminus is required for supramolecular assembly and ubiquitin ligase activity.EMBO J. 26, 90-101 (Pubitemid 46094702)
    • (2007) EMBO Journal , vol.26 , Issue.1 , pp. 90-101
    • Poyurovsky, M.V.1    Priest, C.2    Kentsis, A.3    Borden, K.L.B.4    Pan, Z.-Q.5    Pavletich, N.6    Prives, C.7
  • 30
    • 33846193699 scopus 로고    scopus 로고
    • An essential function of the extreme C-terminus of MDM2 can be provided by MDMX
    • DOI 10.1038/sj.emboj.7601469, PII 7601469
    • Uldrijan, S., Pannekoek, W. J., and Vousden, K. H. (2007) An essential function of the extreme C-terminus of MDM2 can be provided by MDMX. EMBO J. 26, 102-112 (Pubitemid 46094703)
    • (2007) EMBO Journal , vol.26 , Issue.1 , pp. 102-112
    • Uldrijan, S.1    Pannekoek, W.-J.2    Vousden, K.H.3
  • 31
    • 42149105590 scopus 로고    scopus 로고
    • Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans
    • Linke, K., Mace, P. D., Smith, C. A., Vaux, D. L., Silke, J., and Day, C. L. (2008) Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans. Cell Death Differ. 15, 841-848
    • (2008) Cell Death Differ. , vol.15 , pp. 841-848
    • Linke, K.1    Mace, P.D.2    Smith, C.A.3    Vaux, D.L.4    Silke, J.5    Day, C.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.