메뉴 건너뛰기




Volumn 88, Issue 4, 2003, Pages 636-643

Nuclear export inhibitor leptomycin B induces the appearance of novel forms of human Mdm2 protein

Author keywords

Human Mdm2; Leptomycin B; Limited proteolysis; p53; Proteasome

Indexed keywords

LEPTOMYCIN B; PROTEASOME; PROTEASOME INHIBITOR; PROTEIN MDM2; PROTEIN P53;

EID: 0037463228     PISSN: 00070920     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.bjc.6600752     Document Type: Article
Times cited : (9)

References (42)
  • 1
    • 0035868386 scopus 로고    scopus 로고
    • The contribution of the acidic domain of MDM2 to p53 and MDM2 stability
    • Argentini M, Barboule N, Wasylyk B (2001) The contribution of the acidic domain of MDM2 to p53 and MDM2 stability. Oncogene 20: 1267-1275
    • (2001) Oncogene , vol.20 , pp. 1267-1275
    • Argentini, M.1    Barboule, N.2    Wasylyk, B.3
  • 2
    • 0027459198 scopus 로고
    • Mdm2 expression is induced by wildtype p53 activity
    • Barak Y, Juven T, Haffner R, Oren M (1993) mdm2 expression is induced by wildtype 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
  • 4
    • 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
  • 5
    • 0029913730 scopus 로고    scopus 로고
    • Mdm-2 inhibits the G1 arrest and apoptosis functions of the p53 tumor suppressor protein
    • Chen J, Wu X, Lin J, Levine AJ (1996) mdm-2 inhibits the G1 arrest and apoptosis functions of the p53 tumor suppressor protein. Mol Cell Biol 16: 2445-2452
    • (1996) Mol Cell Biol , vol.16 , pp. 2445-2452
    • Chen, J.1    Wu, X.2    Lin, J.3    Levine, A.J.4
  • 6
    • 0034708458 scopus 로고    scopus 로고
    • Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53
    • Fang S, Jensen JP, Ludwig RL, Vousden KH, Weissman AM (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
  • 7
    • 0031724593 scopus 로고    scopus 로고
    • Nuclear export is required for degradation of endogenous p53 by MDM2 and human papillomavirus E6
    • Freedman DA, Levine AJ (1998) Nuclear export is required for degradation of endogenous p53 by MDM2 and human papillomavirus E6. Mol Cell Biol 18: 7288-7293
    • (1998) Mol Cell Biol , vol.18 , pp. 7288-7293
    • Freedman, D.A.1    Levine, A.J.2
  • 8
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y, Maya R, Kazaz A, Oren M (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
  • 11
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • Honda R, Tanaka H, Yasuda H (1997) Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett 420: 25-27
    • (1997) FEBS Lett , vol.420 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 12
    • 0034624678 scopus 로고    scopus 로고
    • Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase
    • Honda R, Yasuda H (2000) Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase. Oncogene 19: 1473-1476
    • (2000) Oncogene , vol.19 , pp. 1473-1476
    • Honda, R.1    Yasuda, H.2
  • 13
  • 15
    • 0038298110 scopus 로고    scopus 로고
    • An inhibitor of nuclear export activates the p53 response and induces the localization of HDM2 and p53 to U1A-positive nuclear bodies associated with the PODs
    • Lain S, Midgley C, Sparks A, Lane EB, Lane DP (1999a) An inhibitor of nuclear export activates the p53 response and induces the localization of HDM2 and p53 to U1A-positive nuclear bodies associated with the PODs. Exp Cell Res 248: 457-472
    • (1999) Exp Cell Res , vol.248 , pp. 457-472
    • Lain, S.1    Midgley, C.2    Sparks, A.3    Lane, E.B.4    Lane, D.P.5
  • 16
    • 0343938848 scopus 로고    scopus 로고
    • Accumulating active p53 in the nucleus by inhibition of nuclear export: A novel strategy to promote the p53 tumor suppressor function
    • Lain S, Xirodimas D, Lane DP (1999b) Accumulating active p53 in the nucleus by inhibition of nuclear export: a novel strategy to promote the p53 tumor suppressor function. Exp Cell Res 253: 315-324
    • (1999) Exp Cell Res , vol.253 , pp. 315-324
    • Lain, S.1    Xirodimas, D.2    Lane, D.P.3
  • 17
    • 0036219608 scopus 로고    scopus 로고
    • Therapeutic exploitation of the p53 pathway
    • Lane DP, Lain S (2002) Therapeutic exploitation of the p53 pathway. Trends Mol Med 8: S38-S42
    • (2002) Trends Mol Med , vol.8 , pp. S38-S42
    • Lane, D.P.1    Lain, S.2
  • 18
    • 0032549815 scopus 로고    scopus 로고
    • Cotranslational biogenesis of NF-kappaB p50 by the 26S proteasome
    • Lin L, DeMartino GN, Greene WC (1998) Cotranslational biogenesis of NF-kappaB p50 by the 26S proteasome. Cell 92: 819-828
    • (1998) Cell , vol.92 , pp. 819-828
    • Lin, L.1    DeMartino, G.N.2    Greene, W.C.3
  • 19
    • 0034283010 scopus 로고    scopus 로고
    • Cotranslational dimerization of the Rel homology domain of NF-kappaB1 generates p50- p105 heterodimers and is required for effective p50 production
    • Lin L, DeMartino GN, Greene WC (2000) Cotranslational dimerization of the Rel homology domain of NF-kappaB1 generates p50- p105 heterodimers and is required for effective p50 production. EMBO J 19: 4712-4722.
    • (2000) EMBO J , vol.19 , pp. 4712-4722
    • Lin, L.1    DeMartino, G.N.2    Greene, W.C.3
  • 20
    • 0029924035 scopus 로고    scopus 로고
    • Glycine-rich region in NF-kappaB p105 functions as a processing signal for the generation of the p50 subunit
    • Lin L, Ghosh SA (1996) Glycine-rich region in NF-kappaB p105 functions as a processing signal for the generation of the p50 subunit. Mol Cell Biol 16: 2248-2254
    • (1996) Mol Cell Biol , vol.16 , pp. 2248-2254
    • Lin, L.1    Ghosh, S.A.2
  • 21
  • 22
    • 0029788135 scopus 로고    scopus 로고
    • Discordance between accumulated p53 protein level and its transcriptional activity in response to u.v. radiation
    • Lu X, Burbidge SA, Griffin S, Smith HM (1996) Discordance between accumulated p53 protein level and its transcriptional activity in response to u.v. radiation. Oncogene 13: 413-418
    • (1996) Oncogene , vol.13 , pp. 413-418
    • Lu, X.1    Burbidge, S.A.2    Griffin, S.3    Smith, H.M.4
  • 23
    • 0030935858 scopus 로고    scopus 로고
    • The tumor suppressor p53 is subject to both nuclear import and export, and both are fast, energy-dependent and lectin-inhibited
    • Middeler G, Zerf K, Jenovai S, Thulig A, Tschodrich-Rotter M, Kubitscheck U, Peters R (1997) The tumor suppressor p53 is subject to both nuclear import and export, and both are fast, energy-dependent and lectin-inhibited. Oncogene 14: 1407-1417
    • (1997) Oncogene , vol.14 , pp. 1407-1417
    • Middeler, G.1    Zerf, K.2    Jenovai, S.3    Thulig, A.4    Tschodrich-Rotter, M.5    Kubitscheck, U.6    Peters, R.7
  • 24
    • 0034603897 scopus 로고    scopus 로고
    • An N-terminal p14ARF peptide blocks Mdm2-dependent ubiquitination in vitro and can activate p53 in vivo
    • Midgley CA, Desterro JM, Saville MK, Howard S, Sparks A, Hay RT, Lane DP (2000) An N-terminal p14ARF peptide blocks Mdm2-dependent ubiquitination in vitro and can activate p53 in vivo. Oncogene 19: 2312-2323
    • (2000) Oncogene , vol.19 , pp. 2312-2323
    • Midgley, C.A.1    Desterro, J.M.2    Saville, M.K.3    Howard, S.4    Sparks, A.5    Hay, R.T.6    Lane, D.P.7
  • 26
    • 17644444479 scopus 로고    scopus 로고
    • Separation of cathepsin A-like enzyme and the proteasome: Evidence that lactacystin/beta-lactone is not a specific inhibitor of the proteasome
    • Ostrowska H, Wojcik C, Wilk S, Omura S, Kozlowski L, Stoklosa T, Worowski K, Radziwon P (2000) Separation of cathepsin A-like enzyme and the proteasome: evidence that lactacystin/beta-lactone is not a specific inhibitor of the proteasome. Int J Biochem Cell Biol 32: 747-757
    • (2000) Int J Biochem Cell Biol , vol.32 , pp. 747-757
    • Ostrowska, H.1    Wojcik, C.2    Wilk, S.3    Omura, S.4    Kozlowski, L.5    Stoklosa, T.6    Worowski, K.7    Radziwon, P.8
  • 27
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B
    • Palombella VJ, Rando OJ, Goldberg AL, Maniatis T (1994) The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B. Cell 78: 773-785
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 28
    • 0027964904 scopus 로고
    • Immunochemical analysis of the interaction of p53 with MDM2; fine mapping of the MDM2 binding site on p53 using synthetic peptides
    • Picksley SM, Vojtesek B, Sparks A, Lane DP (1994) Immunochemical analysis of the interaction of p53 with MDM2; fine mapping of the MDM2 binding site on p53 using synthetic peptides. Oncogene 9: 2523-2529
    • (1994) Oncogene , vol.9 , pp. 2523-2529
    • Picksley, S.M.1    Vojtesek, B.2    Sparks, A.3    Lane, D.P.4
  • 29
    • 0033851133 scopus 로고    scopus 로고
    • Does p53 status influence tumor response to anticancer therapies?
    • Pirollo KF, Bouker KB, Chang EH (2000) Does p53 status influence tumor response to anticancer therapies? Anticancer Drugs 11: 419-432
    • (2000) Anticancer Drugs , vol.11 , pp. 419-432
    • Pirollo, K.F.1    Bouker, K.B.2    Chang, E.H.3
  • 30
    • 0033591433 scopus 로고    scopus 로고
    • Activation of an MDM2-specific caspase by p53 in the absence of apoptosis
    • Pochampally R, Fodera B, Chen L, Lu W, Chen J (1999) Activation of an MDM2-specific caspase by p53 in the absence of apoptosis. J Biol Chem 274: 15271-15277
    • (1999) J Biol Chem , vol.274 , pp. 15271-15277
    • Pochampally, R.1    Fodera, B.2    Chen, L.3    Lu, W.4    Chen, J.5
  • 31
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner M, Rogers SW (1996) PEST sequences and regulation by proteolysis. Trends Biochem Sci 21: 267-271
    • (1996) Trends Biochem Sci , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 32
    • 0022647482 scopus 로고
    • In vivo and in vitro anticancer activity of the structurally novel and highly potent antibiotic CI-940 and its hydroxy analog (PD 114, 721)
    • Roberts BJ, Hamelehle KL, Sebolt JS, Leopold WR (1986) In vivo and in vitro anticancer activity of the structurally novel and highly potent antibiotic CI-940 and its hydroxy analog (PD 114, 721). Cancer Chemother Pharmacol 16: 95-101
    • (1986) Cancer Chemother Pharmacol , vol.16 , pp. 95-101
    • Roberts, B.J.1    Hamelehle, K.L.2    Sebolt, J.S.3    Leopold, W.R.4
  • 33
    • 0032518917 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein
    • Roth J, Dobbelstein M, Freedman DA, Shenk T, Levine AJ (1998) Nucleocytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein. EMBO J 17: 554-564
    • (1998) EMBO J , vol.17 , pp. 554-564
    • Roth, J.1    Dobbelstein, M.2    Freedman, D.A.3    Shenk, T.4    Levine, A.J.5
  • 34
    • 0343044332 scopus 로고    scopus 로고
    • Effects on normal fibroblasts and neuroblastoma cells of the activation of the p53 response by the nuclear export inhibitor leptomycin B
    • Smart P, Lane EB, Lane DP, Midgley C, Vojtesek B, Lain S (1999) Effects on normal fibroblasts and neuroblastoma cells of the activation of the p53 response by the nuclear export inhibitor leptomycin B. Oncogene 18: 7378-7386.
    • (1999) Oncogene , vol.18 , pp. 7378-7386
    • Smart, P.1    Lane, E.B.2    Lane, D.P.3    Midgley, C.4    Vojtesek, B.5    Lain, S.6
  • 35
    • 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 NY Acad Sci 910: 121-137
    • (2000) Ann NY Acad Sci , vol.910 , pp. 121-137
    • Soussi, T.1
  • 36
    • 0028915250 scopus 로고
    • Characterisation of epitopes on human p53 using phage-displayed peptide libraries: Insights into antibody-peptide interactions
    • Stephen CW, Helminen P, Lane DP (1995) Characterisation of epitopes on human p53 using phage-displayed peptide libraries: insights into antibody-peptide interactions. J Mol Biol 248: 58-78
    • (1995) J Mol Biol , vol.248 , pp. 58-78
    • Stephen, C.W.1    Helminen, P.2    Lane, D.P.3
  • 37
    • 0033559256 scopus 로고    scopus 로고
    • A leucine-rich nuclear export signal in the p53 tetramerization domain: Regulation of subcellular localization and p53 activity by NES masking
    • Stommel JM, Marchenko ND, Jimenez GS, Moll UM, Hope TJ, Wahl GM (1999) A leucine-rich nuclear export signal in the p53 tetramerization domain: regulation of subcellular localization and p53 activity by NES masking. EMBO J 18: 1660-1672
    • (1999) EMBO J , vol.18 , pp. 1660-1672
    • Stommel, J.M.1    Marchenko, N.D.2    Jimenez, G.S.3    Moll, U.M.4    Hope, T.J.5    Wahl, G.M.6
  • 38
    • 0032980646 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of oncoprotein Hdm2 is required for Hdm2-mediated degradation of p53
    • Tao W, Levine AJ (1999) Nucleocytoplasmic shuttling of oncoprotein Hdm2 is required for Hdm2-mediated degradation of p53. Proc Natl Acad Sci USA 96: 3077-3080
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3077-3080
    • Tao, W.1    Levine, A.J.2
  • 39
    • 0037075898 scopus 로고    scopus 로고
    • Activation of the p53 tumor suppressor protein
    • Vousden KH (2002) Activation of the p53 tumor suppressor protein. Biochim Biophys Acta 1602: 47-59
    • (2002) Biochim Biophys Acta , vol.1602 , pp. 47-59
    • Vousden, K.H.1
  • 40
    • 0035899468 scopus 로고    scopus 로고
    • Different effects of p14ARF on the levels of ubiquitinated p53 and Mdm2 in vivo
    • Xirodimas D, Saville MK, Edling C, Lane DP, Laín S (2001a) Different effects of p14ARF on the levels of ubiquitinated p53 and Mdm2 in vivo. Oncogene 20: 4972-4983.
    • (2001) Oncogene , vol.20 , pp. 4972-4983
    • Xirodimas, D.1    Saville, M.K.2    Edling, C.3    Lane, D.P.4    Laín, S.5
  • 41
    • 0035887286 scopus 로고    scopus 로고
    • Cocompartmentalization of p53 and Mdm2 is a major determinant for Mdm2-mediated degradation of p53
    • Xirodimas DP, Stephen CW, Lane DP (2001b) 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
  • 42
    • 0035827335 scopus 로고    scopus 로고
    • A p53 amino-terminal nuclear export signal inhibited by DNA damage-induced phosphorylation
    • Zhang Y, Xiong Y (2001) A p53 amino-terminal nuclear export signal inhibited by DNA damage-induced phosphorylation. Science 292: 1910-1915.
    • (2001) Science , vol.292 , pp. 1910-1915
    • Zhang, Y.1    Xiong, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.