메뉴 건너뛰기




Volumn 15, Issue 2, 2003, Pages 164-171

Ubiquitination, phosphorylation and acetylation: The molecular basis for p53 regulation

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN P53;

EID: 0037377060     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(03)00003-6     Document Type: Review
Times cited : (660)

References (84)
  • 1
    • 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
  • 3
    • 0035370483 scopus 로고    scopus 로고
    • Regulation and function of the p53 tumor suppressor protein
    • Ryan K.M., Phillips A.C., Vousden K.H. Regulation and function of the p53 tumor suppressor protein. Curr. Opin. Cell Biol. 13:2001;332-337.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 332-337
    • Ryan, K.M.1    Phillips, A.C.2    Vousden, K.H.3
  • 4
    • 0034003005 scopus 로고    scopus 로고
    • Stress signals utilize multiple pathways to stabilize p53
    • Ashcroft M., Taya Y., 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
  • 5
    • 0034818446 scopus 로고    scopus 로고
    • Post-translational modifications and activation of p53 by genotoxic stresses
    • Appella E., 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
  • 6
    • 0034142325 scopus 로고    scopus 로고
    • Chk2/hCds1 functions as a DNA damage checkpoint in G(1) by stabilizing p53
    • Chehab N.H., Malikzay A., Appel M., Halazonetis T.D. Chk2/hCds1 functions as a DNA damage checkpoint in G(1) by stabilizing p53. Genes Dev. 14:2000;278-288.
    • (2000) Genes Dev. , vol.14 , pp. 278-288
    • Chehab, N.H.1    Malikzay, A.2    Appel, M.3    Halazonetis, T.D.4
  • 7
    • 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., 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
  • 10
    • 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., 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 This paper (together with [11]) shows that Mdm2 can inhibit CBP/p300-mediated acetylation of p53 both in vitro and in vivo. This inhibition is specific for p53 acetylation and occurs in response to a variety of stress-inducing agents.
    • (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
  • 11
    • 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. MDM2 inhibits p300-mediated p53 acetylation and activation by forming a ternary complex with the two proteins. Proc. Natl. Acad. Sci. USA. 97:2000;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
  • 12
    • 0033767235 scopus 로고    scopus 로고
    • Multiple C-terminal lysine residues target p53 for ubiquitin-proteasome-mediated degradation
    • Rodriguez M.S., Desterro J.M., Lain S., Lane D.P., Hay R.T. Multiple C-terminal lysine residues target p53 for ubiquitin-proteasome-mediated degradation. Mol. Cell Biol. 20:2000;8458-8467.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 8458-8467
    • Rodriguez, M.S.1    Desterro, J.M.2    Lain, S.3    Lane, D.P.4    Hay, R.T.5
  • 13
    • 0036340096 scopus 로고    scopus 로고
    • Hypophosphorylation of Mdm2 augments p53 stability
    • Blattner C., Hay T., Meek D.W., Lane D.P. Hypophosphorylation of Mdm2 augments p53 stability. Mol. Cell Biol. 22:2002;6170-6182 The authors present strong evidence that Mdm2 is hypophosphorylated within the conserved region II in the central domain in response to ionizing radiation. Mutants of Mdm2 possessing alanine substitutions within this region were able to sufficiently ubiquitinate p53, but not degrade it. These results suggest an interesting model whereby phosphorylated Mdm2 recruits an unidentified factor required for p53 degradation but, upon DNA damage, dephosphorylation prevents this recruitment.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 6170-6182
    • Blattner, C.1    Hay, T.2    Meek, D.W.3    Lane, D.P.4
  • 15
    • 0035868386 scopus 로고    scopus 로고
    • The contribution of the acidic domain of MDM2 to p53 and MDM2 stability
    • Argentini M., Barboule N., Wasylyk B. The contribution of the acidic domain of MDM2 to p53 and MDM2 stability. Oncogene. 20:2001;1267-1275.
    • (2001) Oncogene , vol.20 , pp. 1267-1275
    • Argentini, M.1    Barboule, N.2    Wasylyk, B.3
  • 16
    • 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
    • Zhu Q., Yao J., Wani G., Wani M.A., Wani A.A. 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
  • 17
    • 0036235121 scopus 로고    scopus 로고
    • Cyclin G recruits PP2A to dephosphorylate Mdm2
    • Okamoto K., Li H., Jensen M.R., Zhang T., Taya Y., Thorgeirsson S.S., Prives C. Cyclin G recruits PP2A to dephosphorylate Mdm2. Mol. Cell. 9:2002;761-771 This paper identifies a role for cyclin G in recruiting phosphatase PP2A to dephosphorylate Mdm2 at Tyr216. They also show this specific dephosphorylation event enhances Mdm2 activity on p53.
    • (2002) Mol. Cell , vol.9 , pp. 761-771
    • Okamoto, K.1    Li, H.2    Jensen, M.R.3    Zhang, T.4    Taya, Y.5    Thorgeirsson, S.S.6    Prives, C.7
  • 18
    • 0034915032 scopus 로고    scopus 로고
    • Control of p53 ubiquitination and nuclear export by MDM2 and ARF
    • Zhang Y., Xiong Y. Control of p53 ubiquitination and nuclear export by MDM2 and ARF. Cell Growth Differ. 12:2001;175-186.
    • (2001) Cell Growth Differ. , vol.12 , pp. 175-186
    • Zhang, Y.1    Xiong, Y.2
  • 20
    • 0035827308 scopus 로고    scopus 로고
    • Molecular biology. Getting p53 out of the nucleus
    • Gottifredi V., Prives C. Molecular biology. Getting p53 out of the nucleus. Science. 292:2001;1851-1852.
    • (2001) Science , vol.292 , pp. 1851-1852
    • Gottifredi, V.1    Prives, C.2
  • 21
    • 0036467391 scopus 로고    scopus 로고
    • The p53 and Mdm2 families in cancer
    • Michael D., Oren M. The p53 and Mdm2 families in cancer. Curr. Opin. Genet. Dev. 12:2002;53-59.
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 53-59
    • Michael, D.1    Oren, M.2
  • 23
    • 0035852716 scopus 로고    scopus 로고
    • A TSG101/MDM2 regulatory loop modulates MDM2 degradation and MDM2/p53 feedback control
    • Li L., Liao J., Ruland J., Mak T.W., Cohen S.N. A TSG101/MDM2 regulatory loop modulates MDM2 degradation and MDM2/p53 feedback control. Proc. Natl. Acad. Sci. USA. 98:2001;1619-1624.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1619-1624
    • Li, L.1    Liao, J.2    Ruland, J.3    Mak, T.W.4    Cohen, S.N.5
  • 25
    • 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., Gu W. Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization. Nature. 416:2002;648-653 Deubiquitination of p53 is shown to be an important antagonist of Mdm2-mediated degradation. HAUSP provides a novel pathway for p53 stabilization by directly blocking its ubiquitination, and this suggests a tumor suppressive role for HAUSP.
    • (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
  • 26
    • 0032815930 scopus 로고    scopus 로고
    • The E7 oncoprotein of human papillomavirus type 16 stabilizes p53 through a mechanism independent of p19(ARF)
    • Seavey S.E., Holubar M., Saucedo L.J., Perry M.E. The E7 oncoprotein of human papillomavirus type 16 stabilizes p53 through a mechanism independent of p19(ARF). J. Virol. 73:1999;7590-7598.
    • (1999) J. Virol. , vol.73 , pp. 7590-7598
    • Seavey, S.E.1    Holubar, M.2    Saucedo, L.J.3    Perry, M.E.4
  • 27
    • 0036133649 scopus 로고    scopus 로고
    • P19(ARF) is dispensable for oncogenic stress-induced p53-mediated apoptosis and tumor suppression in vivo
    • Tolbert D., Lu X., Yin C., Tantama M., Van Dyke T. p19(ARF) is dispensable for oncogenic stress-induced p53-mediated apoptosis and tumor suppression in vivo. Mol. Cell. Biol. 22:2002;370-377.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 370-377
    • Tolbert, D.1    Lu, X.2    Yin, C.3    Tantama, M.4    Van Dyke, T.5
  • 28
    • 0036733697 scopus 로고    scopus 로고
    • The candidate tumor suppressor ING1b can stabilize p53 by disrupting the regulation of p53 by MDM2
    • Leung K.M., Po L.S., Tsang F.C., Siu W.Y., Lau A., Ho H.T., Poon R.Y. The candidate tumor suppressor ING1b can stabilize p53 by disrupting the regulation of p53 by MDM2. Cancer Res. 62:2002;4890-4893.
    • (2002) Cancer Res. , vol.62 , pp. 4890-4893
    • Leung, K.M.1    Po, L.S.2    Tsang, F.C.3    Siu, W.Y.4    Lau, A.5    Ho, H.T.6    Poon, R.Y.7
  • 31
    • 0033621415 scopus 로고    scopus 로고
    • Stabilization of the MDM2 oncoprotein by interaction with the structurally related MDMX protein
    • Sharp D.A., Kratowicz S.A., Sank M.J., George D.L. Stabilization of the MDM2 oncoprotein by interaction with the structurally related MDMX protein. J. Biol. Chem. 274:1999;38189-38196.
    • (1999) J. Biol. Chem. , vol.274 , pp. 38189-38196
    • Sharp, D.A.1    Kratowicz, S.A.2    Sank, M.J.3    George, D.L.4
  • 32
    • 0032191393 scopus 로고    scopus 로고
    • Tumor surveillance via the ARF-p53 pathway
    • Sherr C.J. Tumor surveillance via the ARF-p53 pathway. Genes Dev. 12:1998;2984-2991.
    • (1998) Genes Dev. , vol.12 , pp. 2984-2991
    • Sherr, C.J.1
  • 33
    • 0035942177 scopus 로고    scopus 로고
    • Oncogenic ras activates the ARF-p53 pathway to suppress epithelial cell transformation
    • Lin A.W., Lowe S.W. Oncogenic ras activates the ARF-p53 pathway to suppress epithelial cell transformation. Proc. Natl. Acad. Sci. USA. 98:2001;5025-5030.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5025-5030
    • Lin, A.W.1    Lowe, S.W.2
  • 36
    • 0031014946 scopus 로고    scopus 로고
    • Proteolytic cleavage of human p53 by calpain: A potential regulator of protein stability
    • Kubbutat M.H., Vousden K.H. Proteolytic cleavage of human p53 by calpain: a potential regulator of protein stability. Mol. Cell Biol. 17:1997;460-468.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 460-468
    • Kubbutat, M.H.1    Vousden, K.H.2
  • 39
    • 0035021122 scopus 로고    scopus 로고
    • The corepressor mSin3a interacts with the proline-rich domain of p53 and protects p53 from proteasome-mediated degradation
    • Zilfou J.T., Hoffman W.H., Sank M., George D.L., Murphy M. The corepressor mSin3a interacts with the proline-rich domain of p53 and protects p53 from proteasome-mediated degradation. Mol. Cell Biol. 21:2001;3974-3985.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 3974-3985
    • Zilfou, J.T.1    Hoffman, W.H.2    Sank, M.3    George, D.L.4    Murphy, M.5
  • 40
    • 0035969989 scopus 로고    scopus 로고
    • Regulation of p53 stability and p53-dependent apoptosis by NADH quinone oxidoreductase 1
    • Asher G., Lotem J., Cohen B., Sachs L., Shaul Y. Regulation of p53 stability and p53-dependent apoptosis by NADH quinone oxidoreductase 1. Proc. Natl. Acad. Sci. USA. 98:2001;1188-1193.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1188-1193
    • Asher, G.1    Lotem, J.2    Cohen, B.3    Sachs, L.4    Shaul, Y.5
  • 42
    • 0036791010 scopus 로고    scopus 로고
    • Mdm-2 and ubiquitin-independent p53 proteasomal degradation regulated by NQO1
    • Asher G., Lotem J., Sachs L., Kahana C., Shaul Y. Mdm-2 and ubiquitin-independent p53 proteasomal degradation regulated by NQO1. Proc. Natl. Acad. Sci. USA. 99:2002;13125-13130.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13125-13130
    • Asher, G.1    Lotem, J.2    Sachs, L.3    Kahana, C.4    Shaul, Y.5
  • 47
    • 17944379798 scopus 로고    scopus 로고
    • ASPP proteins specifically stimulate the apoptotic function of p53
    • Samuels-Lev Y., O'Connor D.J., Bergamaschi D., Trigiante G., Hsieh J.K., Zhong S., Campargue I., Naumovski L., Crook T., Lu X. ASPP proteins specifically stimulate the apoptotic function of p53. Mol. Cell. 8:2001;781-794 This paper identifies ASPP2, a member of the ASPP family of proteins, and shows that both ASPP1 and ASPP2 can enhance the transcriptional activation functions of p53. Additionally, these proteins augment p53 binding to the promoters of pro-apoptotic genes.
    • (2001) Mol. Cell , vol.8 , pp. 781-794
    • Samuels-Lev, Y.1    O'Connor, D.J.2    Bergamaschi, D.3    Trigiante, G.4    Hsieh, J.K.5    Zhong, S.6    Campargue, I.7    Naumovski, L.8    Crook, T.9    Lu, X.10
  • 50
    • 0036141392 scopus 로고    scopus 로고
    • Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2
    • •] show that homeodomain-interacting protein kinase-2 (HIPK2) is the kinase specifically responsible for phosphorylating Ser46 of p53 in response to UV irradiation. Furthermore, this phosphorylation event selectively promotes an apoptotic response.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 1-10
    • Hofmann, T.G.1    Moller, A.2    Sirma, H.3    Zentgraf, H.4    Taya, Y.5    Droge, W.6    Will, H.7    Schmitz, M.L.8
  • 51
    • 17744384255 scopus 로고    scopus 로고
    • A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1
    • Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H., Goodman R., Lozano G., Zhao Y., Lu H. A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1. Mol. Cell. 7:2001;283-292 This paper describes a protein complex that specifically phosphorylates Ser392 of p53 in response to UV irradiation.
    • (2001) Mol. Cell , vol.7 , pp. 283-292
    • Keller, D.M.1    Zeng, X.2    Wang, Y.3    Zhang, Q.H.4    Kapoor, M.5    Shu, H.6    Goodman, R.7    Lozano, G.8    Zhao, Y.9    Lu, H.10
  • 52
    • 0033485261 scopus 로고    scopus 로고
    • Phosphorylation of human p53 by p38 kinase coordinates N-terminal phosphorylation and apoptosis in response to UV radiation
    • Bulavin D.V., Saito S., Hollander M.C., Sakaguchi K., Anderson C.W., Appella E., Fornace A.J. Jr. Phosphorylation of human p53 by p38 kinase coordinates N-terminal phosphorylation and apoptosis in response to UV radiation. EMBO J. 18:1999;6845-6854.
    • (1999) EMBO J. , vol.18 , pp. 6845-6854
    • Bulavin, D.V.1    Saito, S.2    Hollander, M.C.3    Sakaguchi, K.4    Anderson, C.W.5    Appella, E.6    Fornace A.J., Jr.7
  • 55
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: A regulatory modification to rival phosphorylation?
    • Kouzarides T. Acetylation: a regulatory modification to rival phosphorylation? EMBO J. 19:2000;1176-1179.
    • (2000) EMBO J. , vol.19 , pp. 1176-1179
    • Kouzarides, T.1
  • 56
    • 0030996361 scopus 로고    scopus 로고
    • Synergistic activation of transcription by CBP and p53
    • Gu W., Shi X.L., Roeder R.G. Synergistic activation of transcription by CBP and p53. Nature. 387:1997;819-823.
    • (1997) Nature , vol.387 , pp. 819-823
    • Gu, W.1    Shi, X.L.2    Roeder, R.G.3
  • 59
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu W., 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
  • 60
    • 0034234237 scopus 로고    scopus 로고
    • CBP/p300 in cell growth, transformation, and development
    • Goodman R.H., 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
  • 61
    • 0034051227 scopus 로고    scopus 로고
    • Acetylation of histones and transcription-related factors
    • Sterner D.E., Berger S.L. Acetylation of histones and transcription-related factors. Microbiol. Mol. Biol. Rev. 64:2000;435-459.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 435-459
    • Sterner, D.E.1    Berger, S.L.2
  • 62
    • 0035694469 scopus 로고    scopus 로고
    • Acetylation of p53 activates transcription through recruitment of coactivators/histone acetyltransferases
    • Barlev N.A., Liu L., Chehab N.H., Mansfield K., Harris K.G., Halazonetis T.D., Berger S.L. Acetylation of p53 activates transcription through recruitment of coactivators/histone acetyltransferases. Mol. Cell. 8:2001;1243-1254 The role of p53 acetylation in recruiting transcription factors and HATs to the p21 promoter in vivo is demonstrated here.
    • (2001) Mol. Cell , vol.8 , pp. 1243-1254
    • Barlev, N.A.1    Liu, L.2    Chehab, N.H.3    Mansfield, K.4    Harris, K.G.5    Halazonetis, T.D.6    Berger, S.L.7
  • 63
    • 0026448672 scopus 로고
    • Regulation of the specific DNA binding function of p53
    • Hupp T.R., Meek D.W., Midgley C.A., 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
  • 64
    • 0029055808 scopus 로고
    • Activation of p53 sequence-specific DNA binding by short single strands of DNA requires the p53 C-terminus
    • Jayaraman J., Prives C. Activation of p53 sequence-specific DNA binding by short single strands of DNA requires the p53 C-terminus. Cell. 81:1995;1021-1029.
    • (1995) Cell , vol.81 , pp. 1021-1029
    • Jayaraman, J.1    Prives, C.2
  • 68
    • 0034881964 scopus 로고    scopus 로고
    • Transcriptional regulation by p53 through intrinsic DNA/chromatin binding and site-directed cofactor recruitment
    • Espinosa J.M., Emerson B.M. Transcriptional regulation by p53 through intrinsic DNA/chromatin binding and site-directed cofactor recruitment. Mol. Cell. 8:2001;57-69 This paper suggests that the carboxyl terminus of p53 can act as a positive regulator in p53 transcriptional activation using an artificially reconstituted chromatin assay.
    • (2001) Mol. Cell , vol.8 , pp. 57-69
    • Espinosa, J.M.1    Emerson, B.M.2
  • 69
    • 0028131554 scopus 로고
    • Transcriptional activation by p53 correlates with suppression of growth but not transformation
    • Crook T., Marston N.J., Sara E.A., Vousden K.H. Transcriptional activation by p53 correlates with suppression of growth but not transformation. Cell. 79:1994;817-827.
    • (1994) Cell , vol.79 , pp. 817-827
    • Crook, T.1    Marston, N.J.2    Sara, E.A.3    Vousden, K.H.4
  • 70
    • 0027980357 scopus 로고
    • Interaction of p53 with MDM2 is independent of E6 and does not mediate wild type transformation suppressor function
    • Marston N.J., Crook T., Vousden K.H. Interaction of p53 with MDM2 is independent of E6 and does not mediate wild type transformation suppressor function. Oncogene. 9:1994;2707-2716.
    • (1994) Oncogene , vol.9 , pp. 2707-2716
    • Marston, N.J.1    Crook, T.2    Vousden, K.H.3
  • 71
    • 0036784608 scopus 로고    scopus 로고
    • Efficient specific DNA binding by p53 requires both its central and C-terminal domains as revealed by studies with high-mobility group 1 protein
    • McKinney K., Prives C. Efficient specific DNA binding by p53 requires both its central and C-terminal domains as revealed by studies with high-mobility group 1 protein. Mol. Cell Biol. 22:2002;6797-6808.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 6797-6808
    • McKinney, K.1    Prives, C.2
  • 72
    • 0036709074 scopus 로고    scopus 로고
    • Human Sir2 and the 'silencing' of p53 activity
    • Smith J. Human Sir2 and the 'silencing' of p53 activity. Trends Cell Biol. 12:2002;404-406.
    • (2002) Trends Cell Biol. , vol.12 , pp. 404-406
    • Smith, J.1
  • 73
    • 0034676439 scopus 로고    scopus 로고
    • Deacetylation of p53 modulates its effect on cell growth and apoptosis
    • Luo J., Su F., Chen D., Shiloh A., Gu W. Deacetylation of p53 modulates its effect on cell growth and apoptosis. Nature. 408:2000;377-381 This paper identifies the importance of deacetylase activity on p53. PID/MTA2 is shown to behave as a specific adaptor protein, linking HDAC1 activity with p53 deacetylation. The authors also show that this activity inhibits p53-mediated apoptosis and cell growth arrest.
    • (2000) Nature , vol.408 , pp. 377-381
    • Luo, J.1    Su, F.2    Chen, D.3    Shiloh, A.4    Gu, W.5
  • 74
    • 0034617261 scopus 로고    scopus 로고
    • Histone deacetylases specifically down-regulate p53-dependent gene activation
    • Juan L.J., Shia W.J., Chen M.H., Yang W.M., Seto E., Lin Y.S., Wu C.W. Histone deacetylases specifically down-regulate p53-dependent gene activation. J. Biol. Chem. 275:2000;20436-20443.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20436-20443
    • Juan, L.J.1    Shia, W.J.2    Chen, M.H.3    Yang, W.M.4    Seto, E.5    Lin, Y.S.6    Wu, C.W.7
  • 81
    • 0034193776 scopus 로고    scopus 로고
    • Sir2 links chromatin silencing, metabolism, and aging
    • Guarente L. Sir2 links chromatin silencing, metabolism, and aging. Genes Dev. 14:2000;1021-1026.
    • (2000) Genes Dev. , vol.14 , pp. 1021-1026
    • Guarente, L.1
  • 82
    • 0037087576 scopus 로고    scopus 로고
    • Dynamics of global histone acetylation and deacetylation in vivo: Rapid restoration of normal histone acetylation status upon removal of activators and repressors
    • Katan-Khaykovich Y., Struhl K. Dynamics of global histone acetylation and deacetylation in vivo: rapid restoration of normal histone acetylation status upon removal of activators and repressors. Genes Dev. 16:2002;743-752.
    • (2002) Genes Dev. , vol.16 , pp. 743-752
    • Katan-Khaykovich, Y.1    Struhl, K.2
  • 83
    • 0037184969 scopus 로고    scopus 로고
    • Acetylation of p53 inhibits its ubiquitination by Mdm2M
    • in press
    • Li M, Luo J, Brooks CL, Gu W: Acetylation of p53 inhibits its ubiquitination by Mdm2M. J Biol Chem 2002, in press.
    • (2002) J Biol Chem
    • Li, M.1    Luo, J.2    Brooks, C.L.3    Gu, W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.