메뉴 건너뛰기




Volumn 23, Issue 6, 2003, Pages 2171-2181

Stabilization of p53 by CP-31398 inhibits ubiquitination without altering phosphorylation at serine 15 or 20 or MDM2 binding

Author keywords

[No Author keywords available]

Indexed keywords

4 (3 DIMETHYLAMINOPROPYLAMINO) 2 (4 METHOXYSTYRYL)QUINAZOLINE; DOXORUBICIN; EPITOPE; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 1620; PROTEIN MDM2; PROTEIN P53; QUINAZOLINE DERIVATIVE; SERINE; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 0037370357     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.23.6.2171-2181.2003     Document Type: Article
Times cited : (132)

References (50)
  • 1
    • 0032505719 scopus 로고    scopus 로고
    • Inhibitors of transcription, proteasome inhibitors, and DNA-damaging drugs differentially affect feedback of p53 degradation
    • An, W. G., Y. Chuman, T. Fojo, and M. V. Blagosklonny. 1998. Inhibitors of transcription, proteasome inhibitors, and DNA-damaging drugs differentially affect feedback of p53 degradation. Exp. Cell Res. 244:54-60.
    • (1998) Exp. Cell Res. , vol.244 , pp. 54-60
    • An, W.G.1    Chuman, Y.2    Fojo, T.3    Blagosklonny, M.V.4
  • 2
    • 0034003005 scopus 로고    scopus 로고
    • Stress signals utilize multiple pathways to stabilize p53
    • Ashcroft, M., Y. Taya, and K. H. Vousden. 2000. Stress signals utilize multiple pathways to stabilize p53. Mol. Cell. Biol. 20:3224-3233.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3224-3233
    • Ashcroft, M.1    Taya, Y.2    Vousden, K.H.3
  • 3
    • 0035572083 scopus 로고    scopus 로고
    • Potential of the proteasomal inhibitor MG-132 as an anticancer agent, alone and in combination
    • Banerjee, D., and A. Liefshitz. 2001. Potential of the proteasomal inhibitor MG-132 as an anticancer agent, alone and in combination. Anticancer Res. 21:3941-3947.
    • (2001) Anticancer Res. , vol.21 , pp. 3941-3947
    • Banerjee, D.1    Liefshitz, A.2
  • 4
    • 0027459198 scopus 로고
    • mdm2 expression is induced by wild type p53 activity
    • Barak, Y., T. Juven, R. Haffner, and M. Oren. 1993. mdm2 expression is induced by wild type p53 activity. EMBO J. 12:461-468.
    • (1993) EMBO J. , vol.12 , pp. 461-468
    • Barak, Y.1    Juven, T.2    Haffner, R.3    Oren, M.4
  • 5
    • 0035280982 scopus 로고    scopus 로고
    • Phosphorylation of serines 15 and 37 is necessary for efficient accumulation of p53 following irradiation with UV
    • Bean, L. J., and G. R. Stark. 2001. Phosphorylation of serines 15 and 37 is necessary for efficient accumulation of p53 following irradiation with UV. Oncogene 20:1076-1084.
    • (2001) Oncogene , vol.20 , pp. 1076-1084
    • Bean, L.J.1    Stark, G.R.2
  • 6
    • 0030705168 scopus 로고    scopus 로고
    • Loss of function and p53 protein stabilization
    • Blagosklonny, M. V. 1997. Loss of function and p53 protein stabilization. Oncogene 15:1889-1893.
    • (1997) Oncogene , vol.15 , pp. 1889-1893
    • Blagosklonny, M.V.1
  • 7
    • 0033522143 scopus 로고    scopus 로고
    • DNA damage induced p53 stabilization: No indication for an involvement of p53 phosphorylation
    • Blattner, C., E. Tobiasch, M. Litfen, H. J. Rahmsdorf, and P. Herrlich. 1999. DNA damage induced p53 stabilization: no indication for an involvement of p53 phosphorylation. Oncogene 18:1723-1732.
    • (1999) Oncogene , vol.18 , pp. 1723-1732
    • Blattner, C.1    Tobiasch, E.2    Litfen, M.3    Rahmsdorf, H.J.4    Herrlich, P.5
  • 9
    • 0033598754 scopus 로고    scopus 로고
    • Phosphorylation of Ser-20 mediates stabilization of human p53 in response to DNA damage
    • Chehab, N. H., A. Malikzay, E. S. Stavridi, and T. D. Halazonetis. 1999. Phosphorylation of Ser-20 mediates stabilization of human p53 in response to DNA damage. Proc. Natl. Acad. Sci. USA 96:13777-13782.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13777-13782
    • Chehab, N.H.1    Malikzay, A.2    Stavridi, E.S.3    Halazonetis, T.D.4
  • 10
    • 0035887213 scopus 로고    scopus 로고
    • Critical roles for the serine 20, but not the serine 15, phosphorylation site and for the polyproline domain in regulating p53 turnover
    • Dumaz, N., D. M. Milne, L. J. Jardine, and D. W. Meek. 2001. Critical roles for the serine 20, but not the serine 15, phosphorylation site and for the polyproline domain in regulating p53 turnover. Biochem. J. 359:459-464.
    • (2001) Biochem. J. , vol.359 , pp. 459-464
    • Dumaz, N.1    Milne, D.M.2    Jardine, L.J.3    Meek, D.W.4
  • 11
    • 0035313706 scopus 로고    scopus 로고
    • DNA-PK, ATM and ATR as sensors of DNA damage: Variations on a theme?
    • Durocher, D., and S. P. Jackson. 2001. DNA-PK, ATM and ATR as sensors of DNA damage: variations on a theme? Curr. Opin. Cell Biol. 13:225-231.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 225-231
    • Durocher, D.1    Jackson, S.P.2
  • 12
    • 0031987277 scopus 로고    scopus 로고
    • Regulation of p53 downstream genes
    • El-Deiry, W. S. 1998. Regulation of p53 downstream genes. Semin. Cancer Biol. 8:345-357.
    • (1998) Semin. Cancer Biol. , vol.8 , pp. 345-357
    • El-Deiry, W.S.1
  • 13
    • 0034708458 scopus 로고    scopus 로고
    • Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53
    • Fang, S., J. P. Jensen, R. L. Ludwig, K. H. Vousden, and A. M. Weissman. 2000. Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53. J. Biol. Chem. 275:8945-8951.
    • (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
  • 14
    • 0033601370 scopus 로고    scopus 로고
    • Pharmacological rescue of mutant p53 conformation and function
    • Foster, B. A., H. A. Coffey, M. J. Morin, and F. Rastinejad. 1999. Pharmacological rescue of mutant p53 conformation and function. Science 286:2507-2510.
    • (1999) Science , vol.286 , pp. 2507-2510
    • Foster, B.A.1    Coffey, H.A.2    Morin, M.J.3    Rastinejad, F.4
  • 16
    • 0034282220 scopus 로고    scopus 로고
    • The MDM2 RING-finger domain is required to promote p53 nuclear export
    • Geyer, R. K., Z. K. Yu, and C. G. Maki. 2000. The MDM2 RING-finger domain is required to promote p53 nuclear export. Nat. Cell Biol. 2:569-573.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 569-573
    • Geyer, R.K.1    Yu, Z.K.2    Maki, C.G.3
  • 17
    • 0033956689 scopus 로고    scopus 로고
    • Identification of a sequence element from p53 that signals for Mdm2-targeted degradation
    • Gu, J., D. Chen, J. Rosenblum, R. M. Rubin, and Z. M. Yuan. 2000. Identification of a sequence element from p53 that signals for Mdm2-targeted degradation. Mol. Cell. Biol. 20:1243-1253.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1243-1253
    • Gu, J.1    Chen, D.2    Rosenblum, J.3    Rubin, R.M.4    Yuan, Z.M.5
  • 18
    • 0035196861 scopus 로고    scopus 로고
    • Identification of p53 sequence elements that are required for MDM2-mediated nuclear export
    • Gu, J., L. Nie, D. Wiederschain, and Z. M. Yuan. 2001. Identification of p53 sequence elements that are required for MDM2-mediated nuclear export. Mol. Cell. Biol. 21:8533-8546.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 8533-8546
    • Gu, J.1    Nie, L.2    Wiederschain, D.3    Yuan, Z.M.4
  • 19
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt, Y., R. Maya, A. Kazaz, and M. Oren. 1997. Mdm2 promotes the rapid degradation of p53. Nature 387:296-299.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 23
    • 0033521621 scopus 로고    scopus 로고
    • Association of p19(ARF) with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53
    • Honda, R., and H. Yasuda. 1999. Association of p19(ARF) with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53. EMBO J, 18:22-27.
    • (1999) EMBO J. , vol.18 , pp. 22-27
    • Honda, R.1    Yasuda, H.2
  • 25
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • Kubbutat, M. H., S. N. Jones, and K. H. Vousden. 1997. Regulation of p53 stability by Mdm2. Nature 387:299-303.
    • (1997) Nature , vol.387 , pp. 299-303
    • Kubbutat, M.H.1    Jones, S.N.2    Vousden, K.H.3
  • 26
    • 0031014946 scopus 로고    scopus 로고
    • Proteolytic cleavage of human p53 by calpain: A potential regulator of protein stability
    • Kubbutat, M. H., and K. H. Vousden. 1997. Proteolytic cleavage of human p53 by calpain: a potential regulator of protein stability. Mol. Cell. Biol. 17:460-468.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 460-468
    • Kubbutat, M.H.1    Vousden, K.H.2
  • 27
    • 0035845853 scopus 로고    scopus 로고
    • UV-radiation induces dose-dependent regulation of p53 response and modulates p53-HDM2 interaction in human fibroblasts
    • Latonen, L., Y. Taya, and M. Laiho. 2001. UV-radiation induces dose-dependent regulation of p53 response and modulates p53-HDM2 interaction in human fibroblasts. Oncogene 20:6784-6793.
    • (2001) Oncogene , vol.20 , pp. 6784-6793
    • Latonen, L.1    Taya, Y.2    Laiho, M.3
  • 28
    • 0037061508 scopus 로고    scopus 로고
    • Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization
    • Li, M., D. Chen, A. Shiloh, J. Luo, A. Y. Nikolaev, J. Qin, and W. Gu. 2002. Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization. Nature 416:648-653.
    • (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
  • 29
    • 0035958574 scopus 로고    scopus 로고
    • Hdmx and Mdm2 can repress transcription activation by p53 but not by p63
    • Little, N. A., and A. G. Jochemsen. 2001. Hdmx and Mdm2 can repress transcription activation by p53 but not by p63. Oncogene 20:4576-4580.
    • (2001) Oncogene , vol.20 , pp. 4576-4580
    • Little, N.A.1    Jochemsen, A.G.2
  • 31
    • 0036352592 scopus 로고    scopus 로고
    • The p53 stabilizing compound CP-31398 induces apoptosis by activating the intrinsic Bax/mitochondrial/caspase-9 pathway
    • Luu, Y., J. Bush, K. J. Cheung, Jr., and G. Li. 2002. The p53 stabilizing compound CP-31398 induces apoptosis by activating the intrinsic Bax/mitochondrial/caspase-9 pathway. Exp. Cell Res. 276:214-222.
    • (2002) Exp. Cell Res. , vol.276 , pp. 214-222
    • Luu, Y.1    Bush, J.2    Cheung K.J., Jr.3    Li, G.4
  • 32
    • 0029952441 scopus 로고    scopus 로고
    • In vivo ubiquitination and proteasome-mediated degradation of p53(1)
    • Maki, C. G., J. M. Huibregtse, and P. M. Howley. 1996. In vivo ubiquitination and proteasome-mediated degradation of p53(1). Cancer Res. 56:2649-2654.
    • (1996) Cancer Res. , vol.56 , pp. 2649-2654
    • Maki, C.G.1    Huibregtse, J.M.2    Howley, P.M.3
  • 34
    • 0031596434 scopus 로고    scopus 로고
    • p73beta, unlike p53, suppresses growth and induces apoptosis of human papillomavirus E6-expressing cancer cells
    • Prabhu, N. S., K. Somasundaram, K. Satyamoorthy, M. Herlyn, and W. S. El-Deiry. 1998. p73beta, unlike p53, suppresses growth and induces apoptosis of human papillomavirus E6-expressing cancer cells. Int. J. Oncol. 13:5-9.
    • (1998) Int. J. Oncol. , vol.13 , pp. 5-9
    • Prabhu, N.S.1    Somasundaram, K.2    Satyamoorthy, K.3    Herlyn, M.4    El-Deiry, W.S.5
  • 35
    • 0037192628 scopus 로고    scopus 로고
    • Characterization of the p53-rescue drug CP-31398 in vitro and in living cells
    • Rippin, T. M., V. J. Bykov, S. M. Freund, G. Selivanova, K. G. Wiman, and A. R. Fersht. 2002. Characterization of the p53-rescue drug CP-31398 in vitro and in living cells. Oncogene 21:2119-2129.
    • (2002) Oncogene , vol.21 , pp. 2119-2129
    • Rippin, T.M.1    Bykov, V.J.2    Freund, S.M.3    Selivanova, G.4    Wiman, K.G.5    Fersht, A.R.6
  • 36
    • 0034683566 scopus 로고    scopus 로고
    • P53 null mice: Damaging the hypothesis?
    • Sansom, O. J., and A. R. Clarke. 2000. P53 null mice: damaging the hypothesis? Mutat. Res. 452:149-162.
    • (2000) Mutat. Res. , vol.452 , pp. 149-162
    • Sansom, O.J.1    Clarke, A.R.2
  • 37
    • 0032911047 scopus 로고    scopus 로고
    • Reactivation of mutant p53 through interaction of a C-terminal peptide with the core domain
    • Selivanova, G., L. Ryahchenko, E. Jansson, V. Iotsova, and K. G. Wiman. 1999. Reactivation of mutant p53 through interaction of a C-terminal peptide with the core domain. Mol. Cell. Biol. 19:3395-3402.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3395-3402
    • Selivanova, G.1    Ryahchenko, L.2    Jansson, E.3    Iotsova, V.4    Wiman, K.G.5
  • 38
    • 0030667702 scopus 로고    scopus 로고
    • DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
    • Shieh, S. Y., M. Ikeda, Y. Taya, and C. Prives. 1997. DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2. Cell 91:325-334.
    • (1997) Cell , vol.91 , pp. 325-334
    • Shieh, S.Y.1    Ikeda, M.2    Taya, Y.3    Prives, C.4
  • 39
    • 0037047345 scopus 로고    scopus 로고
    • The conformationally flexible S9-S10 linker region in the core domain of p53 contains a novel MDM2 binding site whose mutation increases ubiquitination of p53 in vivo
    • Shimizu, H., L. R. Burch, A. J. Smith, D. Dornan, M. Wallace, K. L. Ball, and T. R. Hupp. 2002. The conformationally flexible S9-S10 linker region in the core domain of p53 contains a novel MDM2 binding site whose mutation increases ubiquitination of p53 in vivo. J. Biol. Chem. 277:28446-28458.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28446-28458
    • Shimizu, H.1    Burch, L.R.2    Smith, A.J.3    Dornan, D.4    Wallace, M.5    Ball, K.L.6    Hupp, T.R.7
  • 41
    • 0033931447 scopus 로고    scopus 로고
    • The p53 tumor suppressor gene: From molecular biology to clinical investigation
    • Soussi, T. 2000. The p53 tumor suppressor gene: from molecular biology to clinical investigation. Ann. N. Y. Acad. Sci. 910:121-139.
    • (2000) Ann. N. Y. Acad. Sci. , vol.910 , pp. 121-139
    • Soussi, T.1
  • 42
    • 85047687410 scopus 로고    scopus 로고
    • The mutant p53-conformation modifying drug, CP-31398, can induce apoptosis of human cancer cells and can stabilize wild-type p53 protein
    • Takimoto, R., W. Wang, D. T. Dicker, F. Rastinejad, J. Lyssikatos, and W. S. El-Deiry. 2002. The mutant p53-conformation modifying drug, CP-31398, can induce apoptosis of human cancer cells and can stabilize wild-type p53 protein. Cancer Biol. Ther. 1:47-57.
    • (2002) Cancer Biol. Ther. , vol.1 , pp. 47-57
    • Takimoto, R.1    Wang, W.2    Dicker, D.T.3    Rastinejad, F.4    Lyssikatos, J.5    El-Deiry, W.S.6
  • 44
    • 0035974798 scopus 로고    scopus 로고
    • Achilles' heel of cancer?
    • Vogelstein, B., and K. W. Kinzler. 2001. Achilles' heel of cancer? Nature 412:865-866.
    • (2001) Nature , vol.412 , pp. 865-866
    • Vogelstein, B.1    Kinzler, K.W.2
  • 45
    • 0034703742 scopus 로고    scopus 로고
    • p53: Death star
    • Vousden, K. H. 2000. p53: death star. Cell 103:691-694.
    • (2000) Cell , vol.103 , pp. 691-694
    • Vousden, K.H.1
  • 47
    • 0035887286 scopus 로고    scopus 로고
    • Cocompartmentalization of p53 and Mdm2 is a major determinant for Mdm2-mediated degradation of p53
    • Xirodimas, D. P., C. W. Stephen, and D. P. Lane. 2001. Cocompartmentalization of p53 and Mdm2 is a major determinant for Mdm2-mediated degradation of p53. Exp. Cell Res. 270:66-77.
    • (2001) Exp. Cell Res. , vol.270 , pp. 66-77
    • Xirodimas, D.P.1    Stephen, C.W.2    Lane, D.P.3
  • 48
    • 0035895895 scopus 로고    scopus 로고
    • The plant isoflavenoid genistein activates p53 and Chk2 in an ATM-dependent manner
    • Ye, R., A. Bodero, B. B. Zhou, K. K. Khanna, M. F. Lavin, and S. P. Lees-Miller. 2001. The plant isoflavenoid genistein activates p53 and Chk2 in an ATM-dependent manner. J. Biol. Chem. 276:4828-4833.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4828-4833
    • Ye, R.1    Bodero, A.2    Zhou, B.B.3    Khanna, K.K.4    Lavin, M.F.5    Lees-Miller, S.P.6
  • 49
    • 0034735904 scopus 로고    scopus 로고
    • MDM2-dependent ubiquitination of nuclear and cytoplasmic P53
    • Yu, Z. K., R. K. Geyer, and C. G. Maki. 2000. MDM2-dependent ubiquitination of nuclear and cytoplasmic P53. Oncogene 19:5892-5897.
    • (2000) Oncogene , vol.19 , pp. 5892-5897
    • Yu, Z.K.1    Geyer, R.K.2    Maki, C.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.