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Volumn 137, Issue 4, 2009, Pages 609-622

Modes of p53 Regulation

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN MDM2; PROTEIN MDMX; PROTEIN P53;

EID: 65549120715     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2009.04.050     Document Type: Review
Times cited : (1381)

References (150)
  • 1
    • 33847328747 scopus 로고    scopus 로고
    • FBXO11 promotes the Neddylation of p53 and inhibits its transcriptional activity
    • Abida W.M., Nikolaev A., Zhao W., Zhang W., and Gu W. FBXO11 promotes the Neddylation of p53 and inhibits its transcriptional activity. J. Biol. Chem. 282 (2007) 1797-1804
    • (2007) J. Biol. Chem. , vol.282 , pp. 1797-1804
    • Abida, W.M.1    Nikolaev, A.2    Zhao, W.3    Zhang, W.4    Gu, W.5
  • 2
    • 65549154109 scopus 로고    scopus 로고
    • Oncogenic viral protein HPV E7 upregulates the SIRT1 longivity protein in human cervical cancer cells
    • Allison S.J., Jiang M., and Milner J. Oncogenic viral protein HPV E7 upregulates the SIRT1 longivity protein in human cervical cancer cells. Aging 1 (2009) 316-327
    • (2009) Aging , vol.1 , pp. 316-327
    • Allison, S.J.1    Jiang, M.2    Milner, J.3
  • 3
    • 2942612843 scopus 로고    scopus 로고
    • Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53
    • An W., Kim J., and Roeder R.G. Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53. Cell 117 (2004) 735-748
    • (2004) Cell , vol.117 , pp. 735-748
    • An, W.1    Kim, J.2    Roeder, R.G.3
  • 4
    • 0034818446 scopus 로고    scopus 로고
    • Post-translational modifications and activation of p53 by genotoxic stresses
    • Appella E., and Anderson C.W. Post-translational modifications and activation of p53 by genotoxic stresses. Eur. J. Biochem. 268 (2001) 2764-2772
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2764-2772
    • Appella, E.1    Anderson, C.W.2
  • 5
    • 0033020147 scopus 로고    scopus 로고
    • Regulation of p53 function and stability by phosphorylation
    • Ashcroft M., Kubbutat M.H., and Vousden K.H. Regulation of p53 function and stability by phosphorylation. Mol. Cell. Biol. 19 (1999) 1751-1758
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1751-1758
    • Ashcroft, M.1    Kubbutat, M.H.2    Vousden, K.H.3
  • 6
    • 0034003005 scopus 로고    scopus 로고
    • Stress signals utilize multiple pathways to stabilize p53
    • Ashcroft M., Taya Y., and Vousden K.H. Stress signals utilize multiple pathways to stabilize p53. Mol. Cell. Biol. 20 (2000) 3224-3233
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3224-3233
    • Ashcroft, M.1    Taya, Y.2    Vousden, K.H.3
  • 10
    • 0025858631 scopus 로고
    • Wild-type but not mutant p53 immunopurified proteins bind to sequences adjacent to the SV40 origin of replication
    • Bargonetti J., Friedman P.N., Kern S.E., Vogelstein B., and Prives C. Wild-type but not mutant p53 immunopurified proteins bind to sequences adjacent to the SV40 origin of replication. Cell 65 (1991) 1083-1091
    • (1991) Cell , vol.65 , pp. 1083-1091
    • Bargonetti, J.1    Friedman, P.N.2    Kern, S.E.3    Vogelstein, B.4    Prives, C.5
  • 13
    • 0033522143 scopus 로고    scopus 로고
    • DNA damage induced p53 stabilization: no indication for an involvement of p53 phosphorylation
    • Blattner C., Tobiasch E., Litfen M., Rahmsdorf H.J., and Herrlich P. DNA damage induced p53 stabilization: no indication for an involvement of p53 phosphorylation. Oncogene 18 (1999) 1723-1732
    • (1999) Oncogene , vol.18 , pp. 1723-1732
    • Blattner, C.1    Tobiasch, E.2    Litfen, M.3    Rahmsdorf, H.J.4    Herrlich, P.5
  • 14
    • 0037377060 scopus 로고    scopus 로고
    • Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation
    • Brooks C.L., and Gu W. Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation. Curr. Opin. Cell Biol. 15 (2003) 164-171
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 164-171
    • Brooks, C.L.1    Gu, W.2
  • 15
    • 31544457877 scopus 로고    scopus 로고
    • p53 ubiquitination: Mdm2 and beyond
    • Brooks C.L., and Gu W. p53 ubiquitination: Mdm2 and beyond. Mol. Cell 21 (2006) 307-315
    • (2006) Mol. Cell , vol.21 , pp. 307-315
    • Brooks, C.L.1    Gu, W.2
  • 17
    • 0034704175 scopus 로고    scopus 로고
    • The N terminus of p53 regulates its dissociation from DNA
    • Cain C., Miller S., Ahn J., and Prives C. The N terminus of p53 regulates its dissociation from DNA. J. Biol. Chem. 275 (2000) 39944-39953
    • (2000) J. Biol. Chem. , vol.275 , pp. 39944-39953
    • Cain, C.1    Miller, S.2    Ahn, J.3    Prives, C.4
  • 18
    • 34047103990 scopus 로고    scopus 로고
    • C-terminal modifications regulate MDM2 dissociation and nuclear export of p53
    • Carter S., Bischof O., Dejean A., and Vousden K.H. C-terminal modifications regulate MDM2 dissociation and nuclear export of p53. Nat. Cell Biol. 9 (2007) 428-435
    • (2007) Nat. Cell Biol. , vol.9 , pp. 428-435
    • Carter, S.1    Bischof, O.2    Dejean, A.3    Vousden, K.H.4
  • 19
  • 22
    • 33745752959 scopus 로고    scopus 로고
    • Ser18 and 23 phosphorylation is required for p53-dependent apoptosis and tumor suppression
    • Chao C., Herr D., Chun J., and Xu Y. Ser18 and 23 phosphorylation is required for p53-dependent apoptosis and tumor suppression. EMBO J. 25 (2006) 2615-2622
    • (2006) EMBO J. , vol.25 , pp. 2615-2622
    • Chao, C.1    Herr, D.2    Chun, J.3    Xu, Y.4
  • 24
    • 21244451434 scopus 로고    scopus 로고
    • ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor
    • Chen D., Kon N., Li M., Zhang W., Qin J., and Gu W. ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor. Cell 121 (2005) 1071-1083
    • (2005) Cell , vol.121 , pp. 1071-1083
    • Chen, D.1    Kon, N.2    Li, M.3    Zhang, W.4    Qin, J.5    Gu, W.6
  • 26
    • 0027983669 scopus 로고
    • Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations
    • Cho Y., Gorina S., Jeffrey P.D., and Pavletich N.P. Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations. Science 265 (1994) 346-355
    • (1994) Science , vol.265 , pp. 346-355
    • Cho, Y.1    Gorina, S.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 30
    • 4344685939 scopus 로고    scopus 로고
    • Ribosomal protein L23 activates p53 by inhibiting MDM2 function in response to ribosomal perturbation but not to translation inhibition
    • Dai M.S., Zeng S.X., Jin Y., Sun X.X., David L., and Lu H. Ribosomal protein L23 activates p53 by inhibiting MDM2 function in response to ribosomal perturbation but not to translation inhibition. Mol. Cell. Biol. 24 (2004) 7654-7668
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7654-7668
    • Dai, M.S.1    Zeng, S.X.2    Jin, Y.3    Sun, X.X.4    David, L.5    Lu, H.6
  • 31
    • 34548049032 scopus 로고    scopus 로고
    • Hzf, a key modulator of p53 mediated transcription, functions as a critical determinant of cell survival and death upon genotoxic stress
    • Das S., Raj L., Zhao B., Bernstein A., Aaronson S.A., and Lee S.W. Hzf, a key modulator of p53 mediated transcription, functions as a critical determinant of cell survival and death upon genotoxic stress. Cell 130 (2007) 624-637
    • (2007) Cell , vol.130 , pp. 624-637
    • Das, S.1    Raj, L.2    Zhao, B.3    Bernstein, A.4    Aaronson, S.A.5    Lee, S.W.6
  • 32
    • 0018743916 scopus 로고
    • Detection of a transformation-related antigen in chemically induced sarcomas and other transformed cells of the mouse
    • DeLeo A.B., Jay G., Appella E., Dubois G.C., Law L.W., and Old L.J. Detection of a transformation-related antigen in chemically induced sarcomas and other transformed cells of the mouse. Proc. Natl. Acad. Sci. USA 76 (1979) 2420-2424
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 2420-2424
    • DeLeo, A.B.1    Jay, G.2    Appella, E.3    Dubois, G.C.4    Law, L.W.5    Old, L.J.6
  • 35
    • 0034881964 scopus 로고    scopus 로고
    • Transcriptional regulation by p53 through intrinsic DNA/chromatin binding and site-directed cofactor recruitment
    • Espinosa J.M., and Emerson B.M. Transcriptional regulation by p53 through intrinsic DNA/chromatin binding and site-directed cofactor recruitment. Mol. Cell 8 (2001) 57-69
    • (2001) Mol. Cell , vol.8 , pp. 57-69
    • Espinosa, J.M.1    Emerson, B.M.2
  • 36
    • 0034708458 scopus 로고    scopus 로고
    • Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53
    • Fang S., Jensen J.P., Ludwig R.L., Vousden K.H., and Weissman A.M. Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53. J. Biol. Chem. 275 (2000) 8945-8951
    • (2000) J. Biol. Chem. , vol.275 , pp. 8945-8951
    • Fang, S.1    Jensen, J.P.2    Ludwig, R.L.3    Vousden, K.H.4    Weissman, A.M.5
  • 37
    • 20744448187 scopus 로고    scopus 로고
    • Functional analysis of the roles of posttranslational modifications at the p53 C terminus in regulating p53 stability and activity
    • Feng L., Lin T., Uranishi H., Gu W., and Xu Y. Functional analysis of the roles of posttranslational modifications at the p53 C terminus in regulating p53 stability and activity. Mol. Cell. Biol. 25 (2005) 5389-5395
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5389-5395
    • Feng, L.1    Lin, T.2    Uranishi, H.3    Gu, W.4    Xu, Y.5
  • 38
    • 0024382760 scopus 로고
    • The p53 proto-oncogene can act as a suppressor of transformation
    • Finlay C.A., Hinds P.W., and Levine A.J. The p53 proto-oncogene can act as a suppressor of transformation. Cell 57 (1989) 1083-1093
    • (1989) Cell , vol.57 , pp. 1083-1093
    • Finlay, C.A.1    Hinds, P.W.2    Levine, A.J.3
  • 39
    • 0034234237 scopus 로고    scopus 로고
    • CBP/p300 in cell growth, transformation, and development
    • Goodman R.H., and Smolik S. CBP/p300 in cell growth, transformation, and development. Genes Dev. 14 (2000) 1553-1577
    • (2000) Genes Dev. , vol.14 , pp. 1553-1577
    • Goodman, R.H.1    Smolik, S.2
  • 40
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu W., and Roeder R.G. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 90 (1997) 595-606
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 42
    • 0033992478 scopus 로고    scopus 로고
    • p53 and human cancer: the first ten thousand mutations
    • Hainaut P., and Hollstein M. p53 and human cancer: the first ten thousand mutations. Adv. Cancer Res. 77 (2000) 81-137
    • (2000) Adv. Cancer Res. , vol.77 , pp. 81-137
    • Hainaut, P.1    Hollstein, M.2
  • 43
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y., Maya R., Kazaz A., and Oren M. Mdm2 promotes the rapid degradation of p53. Nature 387 (1997) 296-299
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 44
    • 0033521621 scopus 로고    scopus 로고
    • Association of p19(ARF) with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53
    • Honda R., and Yasuda H. Association of p19(ARF) with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53. EMBO J. 18 (1999) 22-27
    • (1999) EMBO J. , vol.18 , pp. 22-27
    • Honda, R.1    Yasuda, H.2
  • 45
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • Honda R., Tanaka H., and Yasuda H. Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett. 420 (1997) 25-27
    • (1997) FEBS Lett. , vol.420 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 48
    • 0026448672 scopus 로고
    • Regulation of the specific DNA binding function of p53
    • Hupp T.R., Meek D.W., Midgley C.A., and Lane D.P. Regulation of the specific DNA binding function of p53. Cell 71 (1992) 875-886
    • (1992) Cell , vol.71 , pp. 875-886
    • Hupp, T.R.1    Meek, D.W.2    Midgley, C.A.3    Lane, D.P.4
  • 49
    • 35148847384 scopus 로고    scopus 로고
    • Targeted inactivation of Mdm2 RING finger E3 ubiquitin ligase activity in the mouse reveals mechanistic insights into p53 regulation
    • Itahana K., Mao H., Jin A., Itahana Y., Clegg H.V., Lindstrom M.S., Bhat K.P., Godfrey V.L., Evan G.I., and Zhang Y. Targeted inactivation of Mdm2 RING finger E3 ubiquitin ligase activity in the mouse reveals mechanistic insights into p53 regulation. Cancer Cell 12 (2007) 355-366
    • (2007) Cancer Cell , vol.12 , 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
  • 50
    • 0035868964 scopus 로고    scopus 로고
    • p300/CBP-mediated p53 acetylation is commonly induced by p53-activating agents and inhibited by MDM2
    • Ito A., Lai C.H., Zhao X., Saito S., Hamilton M.H., Appella E., and Yao T.P. p300/CBP-mediated p53 acetylation is commonly induced by p53-activating agents and inhibited by MDM2. EMBO J. 20 (2001) 1331-1340
    • (2001) EMBO J. , vol.20 , pp. 1331-1340
    • Ito, A.1    Lai, C.H.2    Zhao, X.3    Saito, S.4    Hamilton, M.H.5    Appella, E.6    Yao, T.P.7
  • 52
    • 34047194383 scopus 로고    scopus 로고
    • Crippling p53 activities via knock-in mutations in mouse models
    • Iwakuma T., and Lozano G. Crippling p53 activities via knock-in mutations in mouse models. Oncogene 26 (2007) 2177-2184
    • (2007) Oncogene , vol.26 , pp. 2177-2184
    • Iwakuma, T.1    Lozano, G.2
  • 53
  • 55
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T., and Allis C.D. Translating the histone code. Science 293 (2001) 1074-1080
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 56
    • 13944278507 scopus 로고    scopus 로고
    • The p53QS transactivation-deficient mutant shows stress-specific apoptotic activity and induces embryonic lethality
    • Johnson T.M., Hammond E.M., Giaccia A., and Attardi L.D. The p53QS transactivation-deficient mutant shows stress-specific apoptotic activity and induces embryonic lethality. Nat. Genet. 37 (2005) 145-152
    • (2005) Nat. Genet. , vol.37 , pp. 145-152
    • Johnson, T.M.1    Hammond, E.M.2    Giaccia, A.3    Attardi, L.D.4
  • 57
    • 0028834902 scopus 로고
    • Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53
    • Jones S.N., Roe A.E., Donehower L.A., and Bradley A. 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
  • 58
    • 0037039319 scopus 로고    scopus 로고
    • Chromatin immunoprecipitation analysis fails to support the latency model for regulation of p53 DNA binding activity in vivo
    • Kaeser M.D., and Iggo R.D. Chromatin immunoprecipitation analysis fails to support the latency model for regulation of p53 DNA binding activity in vivo. Proc. Natl. Acad. Sci. USA 99 (2002) 95-100
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 95-100
    • Kaeser, M.D.1    Iggo, R.D.2
  • 60
    • 0033518119 scopus 로고    scopus 로고
    • Influence of promoter DNA topology on sequence-specific DNA binding and transactivation by tumor suppressor p53
    • Kim E., Rohaly G., Heinrichs S., Gimnopoulos D., Meissner H., and Deppert W. Influence of promoter DNA topology on sequence-specific DNA binding and transactivation by tumor suppressor p53. Oncogene 18 (1999) 7310-7318
    • (1999) Oncogene , vol.18 , pp. 7310-7318
    • Kim, E.1    Rohaly, G.2    Heinrichs, S.3    Gimnopoulos, D.4    Meissner, H.5    Deppert, W.6
  • 61
    • 38749088678 scopus 로고    scopus 로고
    • DBC1 is a negative regulator of SIRT1
    • Kim J.E., Chen J., and Lou Z. DBC1 is a negative regulator of SIRT1. Nature 451 (2008) 583-586
    • (2008) Nature , vol.451 , pp. 583-586
    • Kim, J.E.1    Chen, J.2    Lou, Z.3
  • 63
    • 22544484456 scopus 로고    scopus 로고
    • The C-terminal lysines fine-tune P53 stress responses in a mouse model but are not required for stability control or transactivation
    • Krummel K.A., Lee C.J., Toledo F., and Wahl G.M. The C-terminal lysines fine-tune P53 stress responses in a mouse model but are not required for stability control or transactivation. Proc. Natl. Acad. Sci. USA 102 (2005) 10188-10193
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 10188-10193
    • Krummel, K.A.1    Lee, C.J.2    Toledo, F.3    Wahl, G.M.4
  • 64
    • 59149085299 scopus 로고    scopus 로고
    • MSL2 promotes MDM2 independent cytoplasmic localization of p53
    • Kruse J.P., and Gu W. MSL2 promotes MDM2 independent cytoplasmic localization of p53. J. Biol. Chem. 284 (2008) 3250-3263
    • (2008) J. Biol. Chem. , vol.284 , pp. 3250-3263
    • Kruse, J.P.1    Gu, W.2
  • 65
    • 43949107925 scopus 로고    scopus 로고
    • SnapShot: p53 posttranslational modifications
    • Kruse J.P., and Gu W. SnapShot: p53 posttranslational modifications. Cell 133 (2008) 930
    • (2008) Cell , vol.133 , pp. 930
    • Kruse, J.P.1    Gu, W.2
  • 66
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • Kubbutat M.H., Jones S.N., and Vousden K.H. Regulation of p53 stability by Mdm2. Nature 387 (1997) 299-303
    • (1997) Nature , vol.387 , pp. 299-303
    • Kubbutat, M.H.1    Jones, S.N.2    Vousden, K.H.3
  • 67
    • 33749013398 scopus 로고    scopus 로고
    • Binding of p53 to the central domain of Mdm2 is regulated by phosphorylation
    • Kulikov R., Winter M., and Blattner C. Binding of p53 to the central domain of Mdm2 is regulated by phosphorylation. J. Biol. Chem. 281 (2006) 28575-28583
    • (2006) J. Biol. Chem. , vol.281 , pp. 28575-28583
    • Kulikov, R.1    Winter, M.2    Blattner, C.3
  • 69
    • 0027109075 scopus 로고
    • Cancer. p53, guardian of the genome
    • Lane D.P. Cancer. p53, guardian of the genome. Nature 358 (1992) 15-16
    • (1992) Nature , vol.358 , pp. 15-16
    • Lane, D.P.1
  • 70
    • 0018348655 scopus 로고
    • T antigen is bound to a host protein in SV40-transformed cells
    • Lane D.P., and Crawford L.V. T antigen is bound to a host protein in SV40-transformed cells. Nature 278 (1979) 261-263
    • (1979) Nature , vol.278 , pp. 261-263
    • Lane, D.P.1    Crawford, L.V.2
  • 71
    • 33646807491 scopus 로고    scopus 로고
    • Transcriptional regulation by p53: one protein, many possibilities
    • Laptenko O., and Prives C. Transcriptional regulation by p53: one protein, many possibilities. Cell Death Differ. 13 (2006) 951-961
    • (2006) Cell Death Differ. , vol.13 , pp. 951-961
    • Laptenko, O.1    Prives, C.2
  • 73
    • 2342553892 scopus 로고    scopus 로고
    • Mitochondrial p53 activates Bak and causes disruption of a Bak-Mcl1 complex
    • Leu J.I., Dumont P., Hafey M., Murphy M.E., and George D.L. Mitochondrial p53 activates Bak and causes disruption of a Bak-Mcl1 complex. Nat. Cell Biol. 6 (2004) 443-450
    • (2004) Nat. Cell Biol. , vol.6 , pp. 443-450
    • Leu, J.I.1    Dumont, P.2    Hafey, M.3    Murphy, M.E.4    George, D.L.5
  • 74
    • 0030941458 scopus 로고    scopus 로고
    • p53, the cellular gatekeeper for growth and division
    • Levine A.J. p53, the cellular gatekeeper for growth and division. Cell 88 (1997) 323-331
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 75
    • 0037061508 scopus 로고    scopus 로고
    • Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization
    • Li M., Chen D., Shiloh A., Luo J., Nikolaev A.Y., Qin J., and Gu W. Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization. Nature 416 (2002) 648-653
    • (2002) Nature , vol.416 , pp. 648-653
    • Li, M.1    Chen, D.2    Shiloh, A.3    Luo, J.4    Nikolaev, A.Y.5    Qin, J.6    Gu, W.7
  • 76
    • 0037184969 scopus 로고    scopus 로고
    • Acetylation of p53 inhibits its ubiquitination by Mdm2
    • Li M., Luo J., Brooks C.L., and Gu W. Acetylation of p53 inhibits its ubiquitination by Mdm2. J. Biol. Chem. 277 (2002) 50607-50611
    • (2002) J. Biol. Chem. , vol.277 , pp. 50607-50611
    • Li, M.1    Luo, J.2    Brooks, C.L.3    Gu, W.4
  • 77
    • 0348134742 scopus 로고    scopus 로고
    • Mono- versus polyubiquitination: differential control of p53 fate by Mdm2
    • Li M., Brooks C.L., Wu-Baer F., Chen D., Baer R., and Gu W. Mono- versus polyubiquitination: differential control of p53 fate by Mdm2. Science 302 (2003) 1972-1975
    • (2003) Science , vol.302 , pp. 1972-1975
    • Li, M.1    Brooks, C.L.2    Wu-Baer, F.3    Chen, D.4    Baer, R.5    Gu, W.6
  • 78
    • 1842421376 scopus 로고    scopus 로고
    • A dynamic role of HAUSP in the p53-Mdm2 pathway
    • Li M., Brooks C.L., Kon N., and Gu W. A dynamic role of HAUSP in the p53-Mdm2 pathway. Mol. Cell 13 (2004) 879-886
    • (2004) Mol. Cell , vol.13 , pp. 879-886
    • Li, M.1    Brooks, C.L.2    Kon, N.3    Gu, W.4
  • 80
    • 0018760324 scopus 로고
    • Characterization of a 54K dalton cellular SV40 tumor antigen present in SV40-transformed cells and uninfected embryonal carcinoma cells
    • Linzer D.I., and Levine A.J. Characterization of a 54K dalton cellular SV40 tumor antigen present in SV40-transformed cells and uninfected embryonal carcinoma cells. Cell 17 (1979) 43-52
    • (1979) Cell , vol.17 , pp. 43-52
    • Linzer, D.I.1    Levine, A.J.2
  • 82
    • 22144452221 scopus 로고    scopus 로고
    • Facilitated search for specific genomic targets by p53 C-terminal basic DNA binding domain
    • Liu Y., Lagowski J.P., Vanderbeek G.E., and Kulesz-Martin M.F. Facilitated search for specific genomic targets by p53 C-terminal basic DNA binding domain. Cancer Biol. Ther. 3 (2004) 1102-1108
    • (2004) Cancer Biol. Ther. , vol.3 , pp. 1102-1108
    • Liu, Y.1    Lagowski, J.P.2    Vanderbeek, G.E.3    Kulesz-Martin, M.F.4
  • 83
    • 0034744224 scopus 로고    scopus 로고
    • Stabilization of p53 by p14(ARF) without relocation of MDM2 to the nucleolus
    • Llanos S., Clark P.A., Rowe J., and Peters G. Stabilization of p53 by p14(ARF) without relocation of MDM2 to the nucleolus. Nat. Cell Biol. 3 (2001) 445-452
    • (2001) Nat. Cell Biol. , vol.3 , pp. 445-452
    • Llanos, S.1    Clark, P.A.2    Rowe, J.3    Peters, G.4
  • 86
    • 0037309326 scopus 로고    scopus 로고
    • Tumor suppression by Ink4a-Arf: progress and puzzles
    • Lowe S.W., and Sherr C.J. Tumor suppression by Ink4a-Arf: progress and puzzles. Curr. Opin. Genet. Dev. 13 (2003) 77-83
    • (2003) Curr. Opin. Genet. Dev. , vol.13 , pp. 77-83
    • Lowe, S.W.1    Sherr, C.J.2
  • 87
    • 35148893194 scopus 로고    scopus 로고
    • The Wip1 Phosphatase acts as a gatekeeper in the p53-Mdm2 autoregulatory loop
    • Lu X., Ma O., Nguyen T.A., Jones S.N., Oren M., and Donehower L.A. The Wip1 Phosphatase acts as a gatekeeper in the p53-Mdm2 autoregulatory loop. Cancer Cell 12 (2007) 342-354
    • (2007) Cancer Cell , vol.12 , pp. 342-354
    • Lu, X.1    Ma, O.2    Nguyen, T.A.3    Jones, S.N.4    Oren, M.5    Donehower, L.A.6
  • 88
    • 0034676439 scopus 로고    scopus 로고
    • Deacetylation of p53 modulates its effect on cell growth and apoptosis
    • Luo J., Su F., Chen D., Shiloh A., and Gu W. Deacetylation of p53 modulates its effect on cell growth and apoptosis. Nature 408 (2000) 377-381
    • (2000) Nature , vol.408 , pp. 377-381
    • Luo, J.1    Su, F.2    Chen, D.3    Shiloh, A.4    Gu, W.5
  • 89
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • Luo J., Nikolaev A.Y., Imai S., Chen D., Su F., Shiloh A., Guarente L., and Gu W. Negative control of p53 by Sir2alpha promotes cell survival under stress. Cell 107 (2001) 137-148
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.3    Chen, D.4    Su, F.5    Shiloh, A.6    Guarente, L.7    Gu, W.8
  • 91
    • 34548256424 scopus 로고    scopus 로고
    • The role of ubiquitination in the direct mitochondrial death program of p53
    • Marchenko N.D., and Moll U.M. The role of ubiquitination in the direct mitochondrial death program of p53. Cell Cycle 6 (2007) 1718-1723
    • (2007) Cell Cycle , vol.6 , pp. 1718-1723
    • Marchenko, N.D.1    Moll, U.M.2
  • 92
    • 33847276654 scopus 로고    scopus 로고
    • Monoubiquitylation promotes mitochondrial p53 translocation
    • Marchenko N.D., Wolff S., Erster S., Becker K., and Moll U.M. Monoubiquitylation promotes mitochondrial p53 translocation. EMBO J. 26 (2007) 923-934
    • (2007) EMBO J. , vol.26 , pp. 923-934
    • Marchenko, N.D.1    Wolff, S.2    Erster, S.3    Becker, K.4    Moll, U.M.5
  • 95
    • 0036710512 scopus 로고    scopus 로고
    • The PTEN, Mdm2, p53 tumor suppressor-oncoprotein network
    • Mayo L.D., and Donner D.B. The PTEN, Mdm2, p53 tumor suppressor-oncoprotein network. Trends Biochem. Sci. 27 (2002) 462-467
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 462-467
    • Mayo, L.D.1    Donner, D.B.2
  • 96
    • 3242883729 scopus 로고    scopus 로고
    • The p53 response to DNA damage
    • Meek D.W. The p53 response to DNA damage. DNA Repair (Amst.) 3 (2004) 1049-1056
    • (2004) DNA Repair (Amst.) , vol.3 , pp. 1049-1056
    • Meek, D.W.1
  • 98
    • 34547669249 scopus 로고    scopus 로고
    • The ARF/oncogene pathway activates p53 acetylation within the DNA binding domain
    • Mellert H., Sykes S.M., Murphy M.E., and McMahon S.B. The ARF/oncogene pathway activates p53 acetylation within the DNA binding domain. Cell Cycle 6 (2007) 1304-1306
    • (2007) Cell Cycle , vol.6 , pp. 1304-1306
    • Mellert, H.1    Sykes, S.M.2    Murphy, M.E.3    McMahon, S.B.4
  • 99
    • 25444478027 scopus 로고    scopus 로고
    • ATM-mediated phosphorylations inhibit Mdmx/Mdm2 stabilization by HAUSP in favor of p53 activation
    • Meulmeester E., Pereg Y., Shiloh Y., and Jochemsen A.G. ATM-mediated phosphorylations inhibit Mdmx/Mdm2 stabilization by HAUSP in favor of p53 activation. Cell Cycle 4 (2005) 1166-1170
    • (2005) Cell Cycle , vol.4 , pp. 1166-1170
    • Meulmeester, E.1    Pereg, Y.2    Shiloh, Y.3    Jochemsen, A.G.4
  • 100
    • 0037329056 scopus 로고    scopus 로고
    • The p53-Mdm2 module and the ubiquitin system
    • Michael D., and Oren M. The p53-Mdm2 module and the ubiquitin system. Semin. Cancer Biol. 13 (2003) 49-58
    • (2003) Semin. Cancer Biol. , vol.13 , pp. 49-58
    • Michael, D.1    Oren, M.2
  • 103
    • 8844232663 scopus 로고    scopus 로고
    • The RING domain of Mdm2 mediates histone ubiquitylation and transcriptional repression
    • Minsky N., and Oren M. The RING domain of Mdm2 mediates histone ubiquitylation and transcriptional repression. Mol. Cell 16 (2004) 631-639
    • (2004) Mol. Cell , vol.16 , pp. 631-639
    • Minsky, N.1    Oren, M.2
  • 104
    • 0028823020 scopus 로고
    • Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
    • Montes de Oca Luna R., Wagner D.S., and Lozano G. 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
    • Montes de Oca Luna, R.1    Wagner, D.S.2    Lozano, G.3
  • 105
    • 33745194153 scopus 로고    scopus 로고
    • Excess HDM2 impacts cell cycle and apoptosis and has a selective effect on p53-dependent transcription
    • Ohkubo S., Tanaka T., Taya Y., Kitazato K., and Prives C. Excess HDM2 impacts cell cycle and apoptosis and has a selective effect on p53-dependent transcription. J. Biol. Chem. 281 (2006) 16943-16950
    • (2006) J. Biol. Chem. , vol.281 , pp. 16943-16950
    • Ohkubo, S.1    Tanaka, T.2    Taya, Y.3    Kitazato, K.4    Prives, C.5
  • 106
    • 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
    • Parant J., Chavez-Reyes A., Little N.A., Yan W., Reinke V., Jochemsen A.G., and Lozano G. 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
    • (2001) Nat. Genet. , vol.29 , 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
  • 108
    • 33846239416 scopus 로고    scopus 로고
    • The Mdm2 RING domain C-terminus is required for supramolecular assembly and ubiquitin ligase activity
    • Poyurovsky M.V., Priest C., Kentsis A., Borden K.L., Pan Z.Q., Pavletich N., and Prives C. The Mdm2 RING domain C-terminus is required for supramolecular assembly and ubiquitin ligase activity. EMBO J. 26 (2007) 90-101
    • (2007) EMBO J. , vol.26 , pp. 90-101
    • Poyurovsky, M.V.1    Priest, C.2    Kentsis, A.3    Borden, K.L.4    Pan, Z.Q.5    Pavletich, N.6    Prives, C.7
  • 109
    • 33845185824 scopus 로고    scopus 로고
    • Mdm2 is critically and continuously required to suppress lethal p53 activity in vivo
    • Ringshausen I., O'Shea C.C., Finch A.J., Swigart L.B., and Evan G.I. Mdm2 is critically and continuously required to suppress lethal p53 activity in vivo. Cancer Cell 10 (2006) 501-514
    • (2006) Cancer Cell , vol.10 , pp. 501-514
    • Ringshausen, I.1    O'Shea, C.C.2    Finch, A.J.3    Swigart, L.B.4    Evan, G.I.5
  • 113
    • 65249100143 scopus 로고    scopus 로고
    • Small-molecule inhibitors of the MDM2-p53 protein-protein interaction to reactivate p53 function: a novel approach for cancer therapy
    • Shangary S., and Wang S. Small-molecule inhibitors of the MDM2-p53 protein-protein interaction to reactivate p53 function: a novel approach for cancer therapy. Annu. Rev. Pharmacol. Toxicol. 49 (2009) 223-241
    • (2009) Annu. Rev. Pharmacol. Toxicol. , vol.49 , pp. 223-241
    • Shangary, S.1    Wang, S.2
  • 114
    • 33747819484 scopus 로고    scopus 로고
    • Divorcing ARF and p53: an unsettled case
    • Sherr C.J. Divorcing ARF and p53: an unsettled case. Nat. Rev. Cancer 6 (2006) 663-673
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 663-673
    • Sherr, C.J.1
  • 116
    • 0030667702 scopus 로고    scopus 로고
    • DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
    • Shieh S.Y., Ikeda M., Taya Y., and Prives C. DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2. Cell 91 (1997) 325-334
    • (1997) Cell , vol.91 , pp. 325-334
    • Shieh, S.Y.1    Ikeda, M.2    Taya, Y.3    Prives, C.4
  • 117
    • 0034142034 scopus 로고    scopus 로고
    • The human homologs of checkpoint kinases Chk1 and Cds1 (Chk2) phosphorylate p53 at multiple DNA damage-inducible sites
    • Shieh S.Y., Ahn J., Tamai K., Taya Y., and Prives C. The human homologs of checkpoint kinases Chk1 and Cds1 (Chk2) phosphorylate p53 at multiple DNA damage-inducible sites. Genes Dev. 14 (2000) 289-300
    • (2000) Genes Dev. , vol.14 , pp. 289-300
    • Shieh, S.Y.1    Ahn, J.2    Tamai, K.3    Taya, Y.4    Prives, C.5
  • 118
    • 1642458412 scopus 로고    scopus 로고
    • Phosphorylation of serine 18 regulates distinct p53 functions in mice
    • Sluss H.K., Armata H., Gallant J., and Jones S.N. Phosphorylation of serine 18 regulates distinct p53 functions in mice. Mol. Cell. Biol. 24 (2004) 976-984
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 976-984
    • Sluss, H.K.1    Armata, H.2    Gallant, J.3    Jones, S.N.4
  • 119
    • 46949093338 scopus 로고    scopus 로고
    • The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex
    • Song M.S., Song S.J., Kim S.Y., Oh H.J., and Lim D.S. The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex. EMBO J. 27 (2008) 1863-1874
    • (2008) EMBO J. , vol.27 , pp. 1863-1874
    • Song, M.S.1    Song, S.J.2    Kim, S.Y.3    Oh, H.J.4    Lim, D.S.5
  • 120
    • 2342567852 scopus 로고    scopus 로고
    • Accelerated MDM2 auto-degradation induced by DNA-damage kinases is required for p53 activation
    • Stommel J.M., and Wahl G.M. Accelerated MDM2 auto-degradation induced by DNA-damage kinases is required for p53 activation. EMBO J. 23 (2004) 1547-1556
    • (2004) EMBO J. , vol.23 , pp. 1547-1556
    • Stommel, J.M.1    Wahl, G.M.2
  • 123
    • 0035028599 scopus 로고    scopus 로고
    • Kinetics of p53 binding to promoter sites in vivo
    • Szak S.T., Mays D., and Pietenpol J.A. Kinetics of p53 binding to promoter sites in vivo. Mol. Cell. Biol. 21 (2001) 3375-3386
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3375-3386
    • Szak, S.T.1    Mays, D.2    Pietenpol, J.A.3
  • 125
    • 33845668241 scopus 로고    scopus 로고
    • Tip60-dependent acetylation of p53 modulates the decision between cell-cycle arrest and apoptosis
    • Tang Y., Luo J., Zhang W., and Gu W. Tip60-dependent acetylation of p53 modulates the decision between cell-cycle arrest and apoptosis. Mol. Cell 24 (2006) 827-839
    • (2006) Mol. Cell , vol.24 , pp. 827-839
    • Tang, Y.1    Luo, J.2    Zhang, W.3    Gu, W.4
  • 126
    • 43049163953 scopus 로고    scopus 로고
    • Acetylation is indispensable for p53 activation
    • Tang Y., Zhao W., Chen Y., Zhao Y., and Gu W. Acetylation is indispensable for p53 activation. Cell 133 (2008) 612-626
    • (2008) Cell , vol.133 , pp. 612-626
    • Tang, Y.1    Zhao, W.2    Chen, Y.3    Zhao, Y.4    Gu, W.5
  • 127
    • 34547956843 scopus 로고    scopus 로고
    • hCAS/CSE1L associates with chromatin and regulates expression of select p53 target genes
    • Tanaka T., Ohkubo S., Tatsuno I., and Prives C. hCAS/CSE1L associates with chromatin and regulates expression of select p53 target genes. Cell 130 (2007) 638-650
    • (2007) Cell , vol.130 , pp. 638-650
    • Tanaka, T.1    Ohkubo, S.2    Tatsuno, I.3    Prives, C.4
  • 129
    • 0028922929 scopus 로고
    • p53 transcriptional activation mediated by coactivators TAFII40 and TAFII60
    • Thut C.J., Chen J.L., Klemm R., and Tjian R. p53 transcriptional activation mediated by coactivators TAFII40 and TAFII60. Science 267 (1995) 100-104
    • (1995) Science , vol.267 , pp. 100-104
    • Thut, C.J.1    Chen, J.L.2    Klemm, R.3    Tjian, R.4
  • 130
    • 67349221185 scopus 로고    scopus 로고
    • KRAB-type zinc-finger protein Apak specifically regulates p53-dependent apoptosis
    • 10.1038/ncb1864 in press Published online April 19, 2009
    • Tian C., Xing G., Xie P., Lu K., Nie J., Wang J., Li L., Gao M., Zhang L., and He F. KRAB-type zinc-finger protein Apak specifically regulates p53-dependent apoptosis. Nat. Cell Biol. (2009) 10.1038/ncb1864 in press Published online April 19, 2009
    • (2009) Nat. Cell Biol.
    • Tian, C.1    Xing, G.2    Xie, P.3    Lu, K.4    Nie, J.5    Wang, J.6    Li, L.7    Gao, M.8    Zhang, L.9    He, F.10
  • 131
    • 33845270990 scopus 로고    scopus 로고
    • Regulating the p53 pathway: in vitro hypotheses, in vivo veritas
    • Toledo F., and Wahl G.M. Regulating the p53 pathway: in vitro hypotheses, in vivo veritas. Nat. Rev. Cancer 6 (2006) 909-923
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 909-923
    • Toledo, F.1    Wahl, G.M.2
  • 134
    • 33644555840 scopus 로고    scopus 로고
    • ASPP [corrected] and cancer
    • Trigiante G., and Lu X. ASPP [corrected] and cancer. Nat. Rev. Cancer 6 (2006) 217-226
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 217-226
    • Trigiante, G.1    Lu, X.2
  • 135
    • 33846193699 scopus 로고    scopus 로고
    • An essential function of the extreme C-terminus of MDM2 can be provided by MDMX
    • Uldrijan S., Pannekoek W.J., and Vousden K.H. An essential function of the extreme C-terminus of MDM2 can be provided by MDMX. EMBO J. 26 (2007) 102-112
    • (2007) EMBO J. , vol.26 , pp. 102-112
    • Uldrijan, S.1    Pannekoek, W.J.2    Vousden, K.H.3
  • 138
  • 140
    • 33646787483 scopus 로고    scopus 로고
    • Mouse bites dogma: how mouse models are changing our views of how P53 is regulated in vivo
    • Wahl G.M. Mouse bites dogma: how mouse models are changing our views of how P53 is regulated in vivo. Cell Death Differ. 13 (2006) 973-983
    • (2006) Cell Death Differ. , vol.13 , pp. 973-983
    • Wahl, G.M.1
  • 142
    • 1542358136 scopus 로고    scopus 로고
    • Inhibition of p53 degradation by Mdm2 acetylation
    • Wang X., Taplick J., Geva N., and Oren M. Inhibition of p53 degradation by Mdm2 acetylation. FEBS Lett. 56 (2004) 195-201
    • (2004) FEBS Lett. , vol.56 , pp. 195-201
    • Wang, X.1    Taplick, J.2    Geva, N.3    Oren, M.4
  • 146
    • 3142570737 scopus 로고    scopus 로고
    • Mdm2-mediated NEDD8 conjugation of p53 inhibits its transcriptional activity
    • Xirodimas D.P., Saville M.K., Bourdon J.C., Hay R.T., and Lane D.P. Mdm2-mediated NEDD8 conjugation of p53 inhibits its transcriptional activity. Cell 118 (2004) 83-97
    • (2004) Cell , vol.118 , pp. 83-97
    • Xirodimas, D.P.1    Saville, M.K.2    Bourdon, J.C.3    Hay, R.T.4    Lane, D.P.5
  • 149
    • 0242721592 scopus 로고    scopus 로고
    • Ribosomal protein L11 negatively regulates oncoprotein MDM2 and mediates a p53-dependent ribosomal-stress checkpoint pathway
    • Zhang Y., Wolf G.W., Bhat K., Jin A., Allio T., Burkhart W.A., and Xiong Y. Ribosomal protein L11 negatively regulates oncoprotein MDM2 and mediates a p53-dependent ribosomal-stress checkpoint pathway. Mol. Cell. Biol. 23 (2003) 8902-8912
    • (2003) Mol. Cell. Biol. , vol.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
  • 150
    • 38749132992 scopus 로고    scopus 로고
    • Negative regulation of the deacetylase SIRT1 by DBC1
    • Zhao W., Kruse J.P., Tang Y., Jung S.Y., Qin J., and Gu W. Negative regulation of the deacetylase SIRT1 by DBC1. Nature 451 (2008) 587-590
    • (2008) Nature , vol.451 , pp. 587-590
    • Zhao, W.1    Kruse, J.P.2    Tang, Y.3    Jung, S.Y.4    Qin, J.5    Gu, W.6


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