메뉴 건너뛰기




Volumn 112, Issue 6, 2003, Pages 779-791

Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN MDM2; PROTEIN P53; PROTEIN PIRH2; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 0037459377     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(03)00193-4     Document Type: Article
Times cited : (628)

References (42)
  • 2
    • 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
  • 3
    • 0022483186 scopus 로고
    • Isolation of human-p53-specific monoclonal antibodies and their use in the studies of human p53 expression
    • Banks L., Matlashewski G., Crawford L. Isolation of human-p53-specific monoclonal antibodies and their use in the studies of human p53 expression. Eur. J. Biochem. 159:1986;529-534.
    • (1986) Eur. J. Biochem. , vol.159 , pp. 529-534
    • Banks, L.1    Matlashewski, G.2    Crawford, L.3
  • 4
    • 0027459198 scopus 로고
    • Mdm2 expression is induced by wild type p53 activity
    • Barak Y., Juven T., Haffner R., Oren M. Mdm2 expression is induced by wild type p53 activity. EMBO J. 12:1993;461-468.
    • (1993) EMBO J. , vol.12 , pp. 461-468
    • Barak, Y.1    Juven, T.2    Haffner, R.3    Oren, M.4
  • 6
    • 0034602928 scopus 로고    scopus 로고
    • RING domains: Master builders of molecular scaffolds?
    • Borden K.L.B. RING domains. master builders of molecular scaffolds? J. Mol. Biol. 295:2000;1103-1112.
    • (2000) J. Mol. Biol. , vol.295 , pp. 1103-1112
    • Borden, K.L.B.1
  • 7
    • 0027222956 scopus 로고
    • Mapping of the p53 and mdm-2 interaction domains
    • Chen J., Marechal V., Levine A.J. Mapping of the p53 and mdm-2 interaction domains. Mol. Cell. Biol. 13:1993;4107-4114.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4107-4114
    • Chen, J.1    Marechal, V.2    Levine, A.J.3
  • 9
    • 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., 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
  • 11
    • 0033956689 scopus 로고    scopus 로고
    • Identification of a sequence element from p53 that signals for Mdm2-targeted degradation
    • Gu J., Chen D., Rosenblum J., Rubin R.M., Yuan Z. Identification of a sequence element from p53 that signals for Mdm2-targeted degradation. Mol. Cell. Biol. 20:2000;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.5
  • 12
    • 0019401161 scopus 로고
    • Monoclonal antibodies specific for simian virus 40 tumor antigens
    • Harlow E., Crawford L.V., Pim D.C., Williamson N.M. Monoclonal antibodies specific for simian virus 40 tumor antigens. J. Virol. 39:1981;861-869.
    • (1981) J. Virol. , vol.39 , pp. 861-869
    • Harlow, E.1    Crawford, L.V.2    Pim, D.C.3    Williamson, N.M.4
  • 13
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y., Maya R., Kazaz A., 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
  • 14
    • 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. Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase. Oncogene. 19:2000;1473-1476.
    • (2000) Oncogene , vol.19 , pp. 1473-1476
    • Honda, R.1    Yasuda, H.2
  • 15
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • Honda R., Tanaka H., Yasuda Y. 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, Y.3
  • 16
    • 0033963335 scopus 로고    scopus 로고
    • MdmX protects p53 from Mdm2-mediated degradation
    • Jackson M.W., Berberich S.J. MdmX protects p53 from Mdm2-mediated degradation. Mol. Cell. Biol. 20:2000;1001-1007.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1001-1007
    • Jackson, M.W.1    Berberich, S.J.2
  • 17
    • 0027536952 scopus 로고
    • Growth suppression of friend virus-transformed erythroleukemia cells by p53 protein is accompanied by hemoglobin production and is sensitive to erythropoietin
    • Johnson P., Chung S., Benchimol S. Growth suppression of friend virus-transformed erythroleukemia cells by p53 protein is accompanied by hemoglobin production and is sensitive to erythropoietin. Mol. Cell. Biol. 13:1993;1456-1463.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1456-1463
    • Johnson, P.1    Chung, S.2    Benchimol, S.3
  • 18
    • 0028834902 scopus 로고
    • Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53
    • Jones S.N., Roe A.E., Donehower L.A., 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
  • 19
    • 0027501841 scopus 로고
    • Wild type p53 can mediate sequence-specific transactivation of an internal promoter within the mdm2 gene
    • Juven T., Barak Y., Zauberman A., George D.L., Oren M. Wild type p53 can mediate sequence-specific transactivation of an internal promoter within the mdm2 gene. Oncogene. 8:1993;3411-3416.
    • (1993) Oncogene , vol.8 , pp. 3411-3416
    • Juven, T.1    Barak, Y.2    Zauberman, A.3    George, D.L.4    Oren, M.5
  • 20
    • 1342272916 scopus 로고    scopus 로고
    • How the cyclin became a cyclin: Regulated proteolysis in the cell cycle
    • Koepp D.M., Harper J.W., Elledge S.J. How the cyclin became a cyclin. regulated proteolysis in the cell cycle Cell. 97:1999;431-434.
    • (1999) Cell , vol.97 , pp. 431-434
    • Koepp, D.M.1    Harper, J.W.2    Elledge, S.J.3
  • 21
  • 22
    • 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
  • 24
    • 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.
    • (2000) Nature , vol.408 , pp. 377-381
    • Luo, J.1    Su, F.2    Chen, D.3    Shiloh, A.4    Gu, W.5
  • 26
    • 0026649648 scopus 로고
    • The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation
    • Momand J., Zambetti G.P., Olson D.C., George D., Levine A.J. The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation. Cell. 69:1992;1237-1245.
    • (1992) Cell , vol.69 , pp. 1237-1245
    • Momand, J.1    Zambetti, G.P.2    Olson, D.C.3    George, D.4    Levine, A.J.5
  • 27
    • 0028823020 scopus 로고
    • Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
    • Montes de Oca Luna R., Wagner D.S., 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
  • 29
    • 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., 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
  • 30
    • 0035966316 scopus 로고    scopus 로고
    • Why is p53 acetylated?
    • Prives C., Manley J.L. Why is p53 acetylated? Cell. 107:2001;815-818.
    • (2001) Cell , vol.107 , pp. 815-818
    • Prives, C.1    Manley, J.L.2
  • 32
    • 0032528245 scopus 로고    scopus 로고
    • Identification of a novel class of genomic DNA-binding sites suggests a mechanism for selectivity in target gene activation by the tumor suppressor protein p53
    • Resnick-Silverman L., St. Clair S., Maurer M., Zhao K., Manfredi J.J. Identification of a novel class of genomic DNA-binding sites suggests a mechanism for selectivity in target gene activation by the tumor suppressor protein p53. Genes Dev. 12:1998;2102-2107.
    • (1998) Genes Dev. , vol.12 , pp. 2102-2107
    • Resnick-Silverman, L.1    St. Clair, S.2    Maurer, M.3    Zhao, K.4    Manfredi, J.J.5
  • 33
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • Scheffner M., Huibregtse J.M., Vierstra R.D., Howley P.M. The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell. 75:1993;495-505.
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.D.3    Howley, P.M.4
  • 34
    • 0026446686 scopus 로고
    • Identification of a minimal transforming domain of p53: Negative dominance through abrogation of sequence-specific DNA binding
    • Shaulian E., Zauberman A., Ginsberg D., Oren M. Identification of a minimal transforming domain of p53. negative dominance through abrogation of sequence-specific DNA binding Mol. Cell. Biol. 12:1992;5581-5592.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5581-5592
    • Shaulian, E.1    Zauberman, A.2    Ginsberg, D.3    Oren, M.4
  • 38
    • 0037075898 scopus 로고    scopus 로고
    • Activation of the p53 tumor suppressor protein
    • Vousden K.H. Activation of the p53 tumor suppressor protein. Biochim. Biophys. Acta. 1602:2002;47-59.
    • (2002) Biochim. Biophys. Acta , vol.1602 , pp. 47-59
    • Vousden, K.H.1
  • 39
    • 0027244853 scopus 로고
    • The p53-mdm-2 autoregulatory feedback loop
    • Wu X., Bayle J.H., Olson D., Levine A.J. The p53-mdm-2 autoregulatory feedback loop. Genes Dev. 7:1993;1126-1132.
    • (1993) Genes Dev. , vol.7 , pp. 1126-1132
    • Wu, X.1    Bayle, J.H.2    Olson, D.3    Levine, A.J.4
  • 40
    • 0036468523 scopus 로고    scopus 로고
    • On the shoulders of giants: P63, p73 and the rise of p53
    • Yang A., Kaghad M., Caput D., McKeon F. On the shoulders of giants. p63, p73 and the rise of p53 Trends Genet. 18:2002;90-95.
    • (2002) Trends Genet. , vol.18 , pp. 90-95
    • Yang, A.1    Kaghad, M.2    Caput, D.3    McKeon, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.