메뉴 건너뛰기




Volumn 586, Issue 16, 2012, Pages 2225-2231

Mutational analysis reveals a dual role of Mdm2 acidic domain in the regulation of p53 stability

Author keywords

Acidic domain; Binding partner; Mdm2; Mutagenesis; p53 degradation; Ubiquitin ligase activity

Indexed keywords

AMINO ACID; PROTEASOME; PROTEIN C8ALPHA; PROTEIN MDM2; PROTEIN P53; PROTEIN S6B; TRANSCRIPTION FACTOR YY1; UNCLASSIFIED DRUG;

EID: 84864279057     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.05.034     Document Type: Article
Times cited : (7)

References (51)
  • 2
    • 0028834902 scopus 로고
    • Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53
    • S.N. Jones, A.E. Roe, L.A. Donehower, and A. Bradley Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53 Nature 378 1995 206 208
    • (1995) Nature , vol.378 , pp. 206-208
    • Jones, S.N.1    Roe, A.E.2    Donehower, L.A.3    Bradley, A.4
  • 4
    • 0028823020 scopus 로고
    • Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
    • Montes. de Oca, R. Luna, D.S. Wagner, and G. Lozano Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53 Nature 378 1995 203 206
    • (1995) Nature , vol.378 , pp. 203-206
    • De Oca, M.1    Luna, R.2    Wagner, D.S.3    Lozano, G.4
  • 5
    • 0034863683 scopus 로고    scopus 로고
    • Rescue of embryonic lethality in Mdm4-null mice by loss of Trp53 suggests a nonoverlapping pathway with MDM2 to regulate p53
    • DOI 10.1038/ng714
    • J. Parant, A. Chavez-Reyes, N.A. Little, W. Yan, V. Reinke, A.G. Jochemsen, and G. Lozano Rescue of embryonic lethality in Mdm4-null mice by loss of Trp53 suggests a nonoverlapping pathway with MDM2 to regulate p53 Nat. Genet. 29 2001 92 95 (Pubitemid 32801817)
    • (2001) Nature Genetics , vol.29 , Issue.1 , pp. 92-95
    • Parant, J.1    Chavez-Reyes, A.2    Little, N.A.3    Yan, W.4    Reinke, V.5    Jochemsen, A.G.6    Lozano, G.7
  • 6
    • 33845185824 scopus 로고    scopus 로고
    • Mdm2 is critically and continuously required to suppress lethal p53 activity in vivo
    • DOI 10.1016/j.ccr.2006.10.010, PII S1535610806003163
    • I. Ringshausen, C.C. O'Shea, A.J. Finch, L.B. Swigart, and G.I. Evan Mdm2 is critically and continuously required to suppress lethal p53 activity in vivo Cancer Cell 10 2006 501 514 (Pubitemid 44854749)
    • (2006) Cancer Cell , vol.10 , Issue.6 , pp. 501-514
    • Ringshausen, I.1    O'Shea, C.C.2    Finch, A.J.3    Swigart, L.B.4    Evan, G.I.5
  • 7
    • 33845270990 scopus 로고    scopus 로고
    • Regulating the p53 pathway: In vitro hypotheses, in vivo veritas
    • DOI 10.1038/nrc2012, PII NRC2012
    • F. Toledo, and G.M. Wahl Regulating the p53 pathway: in vitro hypotheses, in vivo veritas Nat. Rev. Cancer 6 2006 909 923 (Pubitemid 44862676)
    • (2006) Nature Reviews Cancer , vol.6 , Issue.12 , pp. 909-923
    • Toledo, F.1    Wahl, G.M.2
  • 9
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • DOI 10.1038/387296a0
    • Y. Haupt, R. Maya, A. Kazaz, and M. Oren Mdm2 promotes the rapid degradation of p53 Nature 387 1997 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
    • M.H. Kubbutat, S.N. Jones, and K.H. Vousden Regulation of p53 stability by Mdm2 Nature 387 1997 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
    • 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
    • M.V. Poyurovsky, C. Priest, A. Kentsis, K.L.B. Borden, Z. Pan, N. Pavletich, and C. Prives The Mdm2 RING domain C-terminus is required for supramolecular assembly and ubiquitin ligase activity EMBO J. 26 2007 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
  • 12
    • 34249711818 scopus 로고    scopus 로고
    • Hetero-oligomerization with MdmX rescues the ubiquitin/Nedd8 ligase activity of RING finger mutants of Mdm2
    • DOI 10.1074/jbc.M610879200
    • R.K. Singh, S. Iyappan, and M. Scheffner Hetero-oligomerization with MdmX rescues the ubiquitin/Nedd8 ligase activity of RING finger mutants of Mdm2 J. Biol. Chem. 282 2007 10901 10907 (Pubitemid 47100746)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.15 , pp. 10901-10907
    • Singh, R.K.1    Iyappan, S.2    Scheffner, M.3
  • 13
    • 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
    • S. Uldrijan, W. Pannekoek, and K.H. Vousden An essential function of the extreme C-terminus of MDM2 can be provided by MDMX EMBO J. 26 2007 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
  • 14
    • 0035868386 scopus 로고    scopus 로고
    • The contribution of the acidic domain of MDM2 to p53 and MDM2 stability
    • DOI 10.1038/sj.onc.1204241
    • M. Argentini, N. Barboule, and B. Wasylyk The contribution of the acidic domain of MDM2 to p53 and MDM2 stability Oncogene 20 2001 1267 1275 (Pubitemid 32269932)
    • (2001) Oncogene , vol.20 , Issue.11 , pp. 1267-1275
    • Argentini, M.1    Barboule, N.2    Wasylyk, B.3
  • 15
    • 0038788827 scopus 로고    scopus 로고
    • Critical contribution of the MDM2 acidic domain to p53 ubiquitination
    • DOI 10.1128/MCB.23.14.4939-4947.2003
    • H. Kawai, D. Wiederschain, and Z. Yuan Critical contribution of the MDM2 acidic domain to p53 ubiquitination Mol. Cell. Biol. 23 2003 4939 4947 (Pubitemid 36793339)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.14 , pp. 4939-4947
    • Kawai, H.1    Wiederschain, D.2    Yuan, Z.-M.3
  • 20
    • 0033521621 scopus 로고    scopus 로고
    • Association of p19(ARF) with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53
    • DOI 10.1093/emboj/18.1.22
    • R. Honda, and H. Yasuda Association of p19(ARF) with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53 EMBO J. 18 1999 22 27 (Pubitemid 29005019)
    • (1999) EMBO Journal , vol.18 , Issue.1 , pp. 22-27
    • Honda, R.1    Yasuda, H.2
  • 23
    • 0032549711 scopus 로고    scopus 로고
    • ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways
    • DOI 10.1016/S0092-8674(00)81401-4
    • Y. Zhang, Y. Xiong, and W.G. Yarbrough ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways Cell 92 1998 725 734 (Pubitemid 28155312)
    • (1998) Cell , vol.92 , Issue.6 , pp. 725-734
    • Zhang, Y.1    Xiong, Y.2    Yarbrough, W.G.3
  • 25
    • 7244238177 scopus 로고    scopus 로고
    • Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5
    • DOI 10.1074/jbc.M403722200
    • M. Dai, and H. Lu Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5 J. Biol. Chem. 279 2004 44475 44482 (Pubitemid 39430853)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.43 , pp. 44475-44482
    • Dai, M.-S.1    Lu, H.2
  • 26
    • 4344660471 scopus 로고    scopus 로고
    • Inhibition of HDM2 and activation of p53 by ribosomal protein L23
    • DOI 10.1128/MCB.24.17.7669-7680.2004
    • A. Jin, K. Itahana, K. O'Keefe, and Y. Zhang Inhibition of HDM2 and activation of p53 by ribosomal protein L23 Mol. Cell. Biol. 24 2004 7669 7680 (Pubitemid 39121492)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.17 , pp. 7669-7680
    • Jin, A.1    Itahana, K.2    O'Keefe, K.3    Zhang, Y.4
  • 27
    • 0038724615 scopus 로고    scopus 로고
    • Regulation of HDM2 activity by the ribosomal protein L11
    • DOI 10.1016/S1535-6108(03)00134-X
    • M.A.E. Lohrum, R.L. Ludwig, M.H.G. Kubbutat, M. Hanlon, and K.H. Vousden Regulation of HDM2 activity by the ribosomal protein L11 Cancer Cell 3 2003 577 587 (Pubitemid 36808652)
    • (2003) Cancer Cell , vol.3 , Issue.6 , pp. 577-587
    • Lohrum, M.A.E.1    Ludwig, R.L.2    Kubbutat, M.H.G.3    Hanlon, M.4    Vousden, K.H.5
  • 28
    • 79959570611 scopus 로고    scopus 로고
    • Interplay between ribosomal protein S27a and MDM2 protein in p53 activation in response to ribosomal stress
    • X. Sun, T. DeVine, K.B. Challagundla, and M. Dai Interplay between ribosomal protein S27a and MDM2 protein in p53 activation in response to ribosomal stress J. Biol. Chem. 286 2011 22730 22741
    • (2011) J. Biol. Chem. , vol.286 , pp. 22730-22741
    • Sun, X.1    Devine, T.2    Challagundla, K.B.3    Dai, M.4
  • 29
    • 0242721592 scopus 로고    scopus 로고
    • Ribosomal Protein L11 Negatively Regulates Oncoprotein MDM2 and Mediates a p53-Dependent Ribosomal-Stress Checkpoint Pathway
    • DOI 10.1128/MCB.23.23.8902-8912.2003
    • Y. Zhang, G.W. Wolf, K. Bhat, A. Jin, T. Allio, W.A. Burkhart, and Y. Xiong Ribosomal protein L11 negatively regulates oncoprotein MDM2 and mediates a p53-dependent ribosomal-stress checkpoint pathway Mol. Cell. Biol. 23 2003 8902 8912 (Pubitemid 37433388)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.23 , pp. 8902-8912
    • Zhang, Y.1    Wolf, G.W.2    Bhat, K.3    Jin, A.4    Allio, T.5    Burkhart, W.A.6    Xiong, Y.7
  • 31
    • 0029171789 scopus 로고
    • Regulation of transcription functions of the p53 tumor suppressor by the mdm-2 oncogene
    • J. Chen, J. Lin, and A.J. Levine Regulation of transcription functions of the p53 tumor suppressor by the mdm-2 oncogene Mol. Med. 1 1995 142 152
    • (1995) Mol. Med. , vol.1 , pp. 142-152
    • Chen, J.1    Lin, J.2    Levine, A.J.3
  • 32
    • 0034708458 scopus 로고    scopus 로고
    • Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53
    • DOI 10.1074/jbc.275.12.8945
    • S. Fang, J.P. Jensen, R.L. Ludwig, K.H. Vousden, and A.M. Weissman Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53 J. Biol. Chem. 275 2000 8945 8951 (Pubitemid 30180252)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.12 , pp. 8945-8951
    • Fang, S.1    Jensen, J.P.2    Ludwig, R.L.3    Vousden, K.H.4    Weissman, A.M.5
  • 33
    • 79955534071 scopus 로고    scopus 로고
    • Inhibition of p53 DNA binding function by the MDM2 protein acidic domain
    • B. Cross, L. Chen, Q. Cheng, B. Li, Z. Yuan, and J. Chen Inhibition of p53 DNA binding function by the MDM2 protein acidic domain J. Biol. Chem. 286 2011 16018 16029
    • (2011) J. Biol. Chem. , vol.286 , pp. 16018-16029
    • Cross, B.1    Chen, L.2    Cheng, Q.3    Li, B.4    Yuan, Z.5    Chen, J.6
  • 34
    • 48849114168 scopus 로고    scopus 로고
    • Acidic domain is indispensable for MDM2 to negatively regulate the acetylation of p53
    • Q. Wang, Y. Yang, L. Wang, P. Zhang, and L. Yu Acidic domain is indispensable for MDM2 to negatively regulate the acetylation of p53 Biochem. Biophys. Res. Commun. 374 2008 437 441
    • (2008) Biochem. Biophys. Res. Commun. , vol.374 , pp. 437-441
    • Wang, Q.1    Yang, Y.2    Wang, L.3    Zhang, P.4    Yu, L.5
  • 35
    • 0345824731 scopus 로고    scopus 로고
    • P53-Independent Functions of MDM2
    • G. Ganguli, and B. Wasylyk p53-independent functions of MDM2 Mol. Cancer Res. 1 2003 1027 1035 (Pubitemid 38044978)
    • (2003) Molecular Cancer Research , vol.1 , Issue.14 , pp. 1027-1035
    • Ganguli, G.1    Wasylyk, B.2
  • 36
    • 77955871461 scopus 로고    scopus 로고
    • The Mdm2-p53 relationship evolves: Mdm2 swings both ways as an oncogene and a tumor suppressor
    • J.J. Manfredi The Mdm2-p53 relationship evolves: Mdm2 swings both ways as an oncogene and a tumor suppressor Genes Dev. 24 2010 1580 1589
    • (2010) Genes Dev. , vol.24 , pp. 1580-1589
    • Manfredi, J.J.1
  • 37
    • 0034632666 scopus 로고    scopus 로고
    • The contribution of the RING finger domain of MDM2 to cell cycle progression
    • M. Argentini, N. Barboule, and B. Wasylyk The contribution of the RING finger domain of MDM2 to cell cycle progression Oncogene 19 2000 3849 3857 (Pubitemid 30658975)
    • (2000) Oncogene , vol.19 , Issue.34 , pp. 3849-3857
    • Argentini, M.1    Barboule, N.2    Wasylyk, B.3
  • 38
    • 0035839451 scopus 로고    scopus 로고
    • Mdm2 mutant defective in binding p300 promotes ubiquitination but not degradation of p53: Evidence for the role of p300 in integrating ubiquitination and proteolysis
    • Q. Zhu, J. Yao, G. Wani, M.A. Wani, and A.A. Wani Mdm2 mutant defective in binding p300 promotes ubiquitination but not degradation of p53: evidence for the role of p300 in integrating ubiquitination and proteolysis J. Biol. Chem. 276 2001 29695 29701
    • (2001) J. Biol. Chem. , vol.276 , pp. 29695-29701
    • Zhu, Q.1    Yao, J.2    Wani, G.3    Wani, M.A.4    Wani, A.A.5
  • 40
    • 0036340096 scopus 로고    scopus 로고
    • Hypophosphorylation of Mdm2 augments p53 stability
    • DOI 10.1128/MCB.22.17.6170-6182.2002
    • C. Blattner, T. Hay, D.W. Meek, and D.P. Lane Hypophosphorylation of Mdm2 augments p53 stability Mol. Cell. Biol. 22 2002 6170 6182 (Pubitemid 34857837)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.17 , pp. 6170-6182
    • Blattner, C.1    Hay, T.2    Meek, D.W.3    Lane, D.P.4
  • 41
    • 22344451422 scopus 로고    scopus 로고
    • Phosphorylation of the acidic domain of Mdm2 by protein kinase CK2
    • DOI 10.1007/s11010-005-3074-4
    • N. Allende-Vega, S. Dias, D. Milne, and D. Meek Phosphorylation of the acidic domain of Mdm2 by protein kinase CK2 Mol. Cell. Biochem. 274 2005 85 90 (Pubitemid 41001504)
    • (2005) Molecular and Cellular Biochemistry , vol.274 , Issue.1-2 , pp. 85-90
    • Allende-Vega, N.1    Dias, S.2    Milne, D.3    Meek, D.4
  • 42
    • 71749107527 scopus 로고    scopus 로고
    • Polo-like kinase-1 phosphorylates MDM2 at Ser260 and stimulates MDM2-mediated p53 turnover
    • S.S. Dias, C. Hogan, A. Ochocka, and D.W. Meek Polo-like kinase-1 phosphorylates MDM2 at Ser260 and stimulates MDM2-mediated p53 turnover FEBS Lett. 583 2009 3543 3548
    • (2009) FEBS Lett. , vol.583 , pp. 3543-3548
    • Dias, S.S.1    Hogan, C.2    Ochocka, A.3    Meek, D.W.4
  • 43
    • 23344447873 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3-dependent phosphorylation of Mdm2 regulates p53 abundance
    • DOI 10.1128/MCB.25.16.7170-7180.2005
    • R. Kulikov, K.A. Boehme, and C. Blattner Glycogen synthase kinase 3-dependent phosphorylation of Mdm2 regulates p53 abundance Mol. Cell. Biol. 25 2005 7170 7180 (Pubitemid 41105913)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.16 , pp. 7170-7180
    • Kulikov, R.1    Boehme, K.A.2    Blattner, C.3
  • 44
    • 33750478380 scopus 로고    scopus 로고
    • C-Abl phosphorylates Hdm2 at tyrosine 276 in response to DNA damage and regulates interaction with ARF
    • DOI 10.1038/sj.onc.1209671, PII 1209671
    • S.S. Dias, D.M. Milne, and D.W. Meek C-Abl phosphorylates Hdm2 at tyrosine 276 in response to DNA damage and regulates interaction with ARF Oncogene 25 2006 6666 6671 (Pubitemid 44646194)
    • (2006) Oncogene , vol.25 , Issue.50 , pp. 6666-6671
    • Dias, S.S.1    Milne, D.M.2    Meek, D.W.3
  • 45
    • 33749013398 scopus 로고    scopus 로고
    • Binding of p53 to the central domain of Mdm2 is regulated by phosphorylation
    • DOI 10.1074/jbc.M513311200
    • R. Kulikov, M. Winter, and C. Blattner Binding of p53 to the central domain of Mdm2 is regulated by phosphorylation J. Biol. Chem. 281 2006 28575 28583 (Pubitemid 44507000)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.39 , pp. 28575-28583
    • Kulikov, R.1    Winter, M.2    Blattner, C.3
  • 46
    • 33745949757 scopus 로고    scopus 로고
    • Dual-Site Regulation of MDM2 E3-Ubiquitin Ligase Activity
    • DOI 10.1016/j.molcel.2006.05.029, PII S1097276506003443
    • M. Wallace, E. Worrall, S. Pettersson, T.R. Hupp, and K.L. Ball Dual-site regulation of MDM2 E3-ubiquitin ligase activity Mol. Cell 23 2006 251 263 (Pubitemid 44062366)
    • (2006) Molecular Cell , vol.23 , Issue.2 , pp. 251-263
    • Wallace, M.1    Worrall, E.2    Pettersson, S.3    Hupp, T.R.4    Ball, K.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.