메뉴 건너뛰기




Volumn 29, Issue 15, 2010, Pages 2538-2552

MDM2 recruitment of lysine methyltransferases regulates p53 transcriptional output

Author keywords

EHMT1; histone methyltransferases; MDM2; p53; SUV39H1

Indexed keywords

HISTONE H3; HISTONE METHYLTRANSFERASE; METHYLTRANSFERASE; PROTEIN MDM2; PROTEIN MDMX; PROTEIN P53;

EID: 77955415488     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2010.140     Document Type: Article
Times cited : (44)

References (59)
  • 3
    • 33644846509 scopus 로고    scopus 로고
    • Epigenetic gene silencing in cancer\a mechanism for early oncogenic pathway addiction?
    • Baylin SB, Ohm JE (2006) Epigenetic gene silencing in cancer\a mechanism for early oncogenic pathway addiction? Nat Rev Cancer 6: 107-116
    • (2006) Nat Rev Cancer , vol.6 , pp. 107-116
    • Baylin, S.B.1    Ohm, J.E.2
  • 4
    • 34249299791 scopus 로고    scopus 로고
    • The complex language of chromatin regulation during transcription
    • Berger SL (2007) The complex language of chromatin regulation during transcription. Nature 447: 407-412
    • (2007) Nature , vol.447 , pp. 407-412
    • Berger, S.L.1
  • 5
    • 3242715867 scopus 로고    scopus 로고
    • Essential role of ribosomal protein L11 in mediating growth inhibition-induced p53 activation
    • Bhat KP, Itahana K, Jin A, Zhang Y (2004) Essential role of ribosomal protein L11 in mediating growth inhibition-induced p53 activation. EMBO J 23: 2402-2412
    • (2004) EMBO J , vol.23 , pp. 2402-2412
    • Bhat, K.P.1    Itahana, K.2    Jin, A.3    Zhang, Y.4
  • 6
    • 0027222956 scopus 로고
    • Mapping of the p53 and mdm-2 interaction domains
    • Chen J, Marechal V, Levine AJ (1993) Mapping of the p53 and mdm-2 interaction domains. Mol Cell Biol 13: 4107-4114
    • (1993) Mol Cell Biol , vol.13 , pp. 4107-4114
    • Chen, J.1    Marechal, V.2    Levine, A.J.3
  • 7
    • 22544438112 scopus 로고    scopus 로고
    • Regulation of p53-MDMX interaction by casein kinase 1 alpha
    • Chen L, Li C, Pan Y, Chen J (2005) Regulation of p53-MDMX interaction by casein kinase 1 alpha. Mol Cell Biol 25: 6509-6520
    • (2005) Mol Cell Biol , vol.25 , pp. 6509-6520
    • Chen, L.1    Li, C.2    Pan, Y.3    Chen, J.4
  • 9
    • 7244238177 scopus 로고    scopus 로고
    • Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5
    • Dai MS, Lu H (2004) Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5. J Biol Chem 279: 44475-44482
    • (2004) J Biol Chem , vol.279 , pp. 44475-44482
    • Dai, M.S.1    Lu, H.2
  • 11
    • 33751573462 scopus 로고    scopus 로고
    • MDMX regulation of p53 response to ribosomal stress
    • MDM2 recruits histone methyltransferases to regulate p53
    • Gilkes DM, Chen L, Chen J (2006) MDMX regulation of p53 response to ribosomal stress. EMBO J 25: 5614-5625, MDM2 recruits histone methyltransferases to regulate p53
    • (2006) EMBO J , vol.25 , pp. 5614-5625
    • Gilkes, D.M.1    Chen, L.2    Chen, J.3
  • 13
    • 18344377030 scopus 로고    scopus 로고
    • The p53 pathway: Positive and negative feedback loops
    • Harris SL, Levine AJ (2005) The p53 pathway: positive and negative feedback loops. Oncogene 24: 2899-2908
    • (2005) Oncogene , vol.24 , pp. 2899-2908
    • Harris, S.L.1    Levine, A.J.2
  • 19
    • 4344660471 scopus 로고    scopus 로고
    • Inhibition of HDM2 and activation of p53 by ribosomal protein L23
    • Jin A, Itahana K, O'Keefe K, Zhang Y (2004) Inhibition of HDM2 and activation of p53 by ribosomal protein L23. Mol Cell Biol 24: 7669-7680
    • (2004) Mol Cell Biol , vol.24 , pp. 7669-7680
    • Jin, A.1    Itahana, K.2    O'Keefe, K.3    Zhang, Y.4
  • 20
    • 0037163085 scopus 로고    scopus 로고
    • MDM2 inhibits PCAF (p300/CREB-binding protein-associated factor)-mediated p53 acetylation
    • Jin Y, Zeng SX, Dai MS, Yang XJ, Lu H (2002) MDM2 inhibits PCAF (p300/CREB-binding protein-associated factor)-mediated p53 acetylation. J Biol Chem 277: 30838-30843
    • (2002) J Biol Chem , vol.277 , pp. 30838-30843
    • Jin, Y.1    Zeng, S.X.2    Dai, M.S.3    Yang, X.J.4    Lu, H.5
  • 21
    • 0038788827 scopus 로고    scopus 로고
    • Critical contribution of the MDM2 acidic domain to p53 ubiquitination
    • Kawai H, Wiederschain D, Yuan ZM (2003) Critical contribution of the MDM2 acidic domain to p53 ubiquitination. Mol Cell Biol 23: 4939-4947
    • (2003) Mol Cell Biol , vol.23 , pp. 4939-4947
    • Kawai, H.1    Wiederschain, D.2    Yuan, Z.M.3
  • 23
    • 0033732303 scopus 로고    scopus 로고
    • MDM2 inhibits p300-mediated p53 acetylation and activation by forming a ternary complex with the two proteins
    • Kobet E, Zeng X, Zhu Y, Keller D, Lu H (2000) MDM2 inhibits p300-mediated p53 acetylation and activation by forming a ternary complex with the two proteins. Proc Natl Acad Sci USA 97: 12547-12552
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 12547-12552
    • Kobet, E.1    Zeng, X.2    Zhu, Y.3    Keller, D.4    Lu, H.5
  • 24
    • 33746990186 scopus 로고    scopus 로고
    • Mechanistic insights into maintenance of high p53 acetylation by PTEN
    • Li AG, Piluso LG, Cai X, Wei G, Sellers WR, Liu X (2006) Mechanistic insights into maintenance of high p53 acetylation by PTEN. Mol Cell 23: 575-587
    • (2006) Mol Cell , vol.23 , pp. 575-587
    • Li, A.G.1    Piluso, L.G.2    Cai, X.3    Wei, G.4    Sellers, W.R.5    Liu, X.6
  • 25
    • 0036837868 scopus 로고    scopus 로고
    • DNA damage induces MDMX nuclear translocation by p53-dependent and-independent mechanisms
    • Li C, Chen L, Chen J (2002) DNA damage induces MDMX nuclear translocation by p53-dependent and-independent mechanisms. Mol Cell Biol 22: 7562-7571
    • (2002) Mol Cell Biol , vol.22 , pp. 7562-7571
    • Li, C.1    Chen, L.2    Chen, J.3
  • 29
    • 27644589675 scopus 로고    scopus 로고
    • The diverse functions of histone lysine methylation
    • Martin C, Zhang Y (2005) The diverse functions of histone lysine methylation. Nat Rev Mol Cell Biol 6: 838-849
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 838-849
    • Martin, C.1    Zhang, Y.2
  • 31
    • 8844232663 scopus 로고    scopus 로고
    • The RING domain of Mdm2 mediates histone ubiquitylation and transcriptional repression
    • Minsky N, Oren M (2004) The RING domain of Mdm2 mediates histone ubiquitylation and transcriptional repression. Mol Cell 16: 631-639
    • (2004) Mol Cell , vol.16 , pp. 631-639
    • Minsky, N.1    Oren, M.2
  • 32
    • 0028823020 scopus 로고
    • Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
    • Montes De Oca Luna R, Wagner DS, Lozano G (1995) Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53. Nature 378: 203-206
    • (1995) Nature , vol.378 , pp. 203-206
    • Montes De Oca Luna, R.1    Wagner, D.S.2    Lozano, G.3
  • 36
    • 0037052539 scopus 로고    scopus 로고
    • A complex with chromatin modifiers that occupies E2F-and Mycresponsive genes in G0 cells
    • Ogawa H, Ishiguro K, Gaubatz S, Livingston DM, Nakatani Y (2002) A complex with chromatin modifiers that occupies E2F-and Mycresponsive genes in G0 cells. Science 296: 1132-1136
    • (2002) Science , vol.296 , pp. 1132-1136
    • Ogawa, H.1    Ishiguro, K.2    Gaubatz, S.3    Livingston, D.M.4    Nakatani, Y.5
  • 37
    • 0042592947 scopus 로고    scopus 로고
    • MDM2 promotes ubiquitination and degradation of MDMX
    • Pan Y, Chen J (2003) MDM2 promotes ubiquitination and degradation of MDMX. Mol Cell Biol 23: 5113-5121
    • (2003) Mol Cell Biol , vol.23 , pp. 5113-5121
    • Pan, Y.1    Chen, J.2
  • 38
    • 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 NA, Yan W, Reinke V, Jochemsen AG, Lozano G (2001) Rescue of embryonic lethality in Mdm4-null mice by loss of Trp53 suggests a nonoverlapping pathway with MDM2 to regulate p53. Nat Genet 29: 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
  • 40
    • 0032931517 scopus 로고    scopus 로고
    • The p53 pathway
    • Prives C, Hall PA (1999) The p53 pathway. J Pathol 187: 112-126
    • (1999) J Pathol , vol.187 , pp. 112-126
    • Prives, C.1    Hall, P.A.2
  • 47
    • 0037099413 scopus 로고    scopus 로고
    • G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis
    • Tachibana M, Sugimoto K, Nozaki M, Ueda J, Ohta T, Ohki M, Fukuda M, Takeda N, Niida H, Kato H, Shinkai Y (2002) G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis. Genes Dev 16: 1779-1791
    • (2002) Genes Dev , vol.16 , pp. 1779-1791
    • Tachibana, M.1    Sugimoto, K.2    Nozaki, M.3    Ueda, J.4    Ohta, T.5    Ohki, M.6    Fukuda, M.7    Takeda, N.8    Niida, H.9    Kato, H.10    Shinkai, Y.11
  • 49
    • 34249863018 scopus 로고    scopus 로고
    • Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53
    • Teufel DP, Freund SM, Bycroft M, Fersht AR (2007) Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53. Proc Natl Acad Sci USA 104: 7009-7014
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 7009-7014
    • Teufel, D.P.1    Freund, S.M.2    Bycroft, M.3    Fersht, A.R.4
  • 50
    • 0030860911 scopus 로고    scopus 로고
    • Repression of p53-mediated transcription by MDM2: A dual mechanism
    • Thut CJ, Goodrich JA, Tjian R (1997) Repression of p53-mediated transcription by MDM2: a dual mechanism. Genes Dev 11: 1974-1986
    • (1997) Genes Dev , vol.11 , pp. 1974-1986
    • Thut, C.J.1    Goodrich, J.A.2    Tjian, R.3
  • 51
    • 33645769536 scopus 로고    scopus 로고
    • A mouse p53 mutant lacking the proline-rich domain rescues Mdm4 deficiency and provides insight into the Mdm2-Mdm4-p53 regulatory network
    • Toledo F, Krummel KA, Lee CJ, Liu CW, Rodewald LW, Tang M, Wahl GM (2006) A mouse p53 mutant lacking the proline-rich domain rescues Mdm4 deficiency and provides insight into the Mdm2-Mdm4-p53 regulatory network. Cancer Cell 9: 273-285
    • (2006) Cancer Cell , vol.9 , pp. 273-285
    • Toledo, F.1    Krummel, K.A.2    Lee, C.J.3    Liu, C.W.4    Rodewald, L.W.5    Tang, M.6    Wahl, G.M.7
  • 52
    • 23044431656 scopus 로고    scopus 로고
    • Histone H3 lysine 9 methylation and HP1gamma are associated with transcription elongation through mammalian chromatin
    • Vakoc CR, Mandat SA, Olenchock BA, Blobel GA (2005) Histone H3 lysine 9 methylation and HP1gamma are associated with transcription elongation through mammalian chromatin. Mol Cell 19: 381-391
    • (2005) Mol Cell , vol.19 , pp. 381-391
    • Vakoc, C.R.1    Mandat, S.A.2    Olenchock, B.A.3    Blobel, G.A.4
  • 56
  • 57
    • 33645751553 scopus 로고    scopus 로고
    • Mouse double minute 2 associates with chromatin in the presence of p53 and is released to facilitate activation of transcription
    • White DE, Talbott KE, Arva NC, Bargonetti J (2006) Mouse double minute 2 associates with chromatin in the presence of p53 and is released to facilitate activation of transcription. Cancer Res 66: 3463-3470
    • (2006) Cancer Res , vol.66 , pp. 3463-3470
    • White, D.E.1    Talbott, K.E.2    Arva, N.C.3    Bargonetti, J.4
  • 58
    • 0035883954 scopus 로고    scopus 로고
    • Transcription regulation by histone methylation: Interplay between different covalent modifications of the core histone tails
    • Zhang Y, Reinberg D (2001) Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails. Genes Dev 15: 2343-2360
    • (2001) Genes Dev , vol.15 , pp. 2343-2360
    • Zhang, Y.1    Reinberg, D.2
  • 59
    • 0034915032 scopus 로고    scopus 로고
    • Control of p53 ubiquitination and nuclear export by MDM2 and ARF
    • Zhang Y, Xiong Y (2001) Control of p53 ubiquitination and nuclear export by MDM2 and ARF. Cell Growth Differ 12: 175-186
    • (2001) Cell Growth Differ , vol.12 , pp. 175-186
    • Zhang, Y.1    Xiong, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.