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Volumn 2, Issue 9, 2000, Pages 563-568

An intact HDM2 RING-finger domain is required for nuclear exclusion of p53

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN P53;

EID: 0034282102     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/35023500     Document Type: Article
Times cited : (293)

References (33)
  • 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, 323-331 (1997).
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 2
    • 0028303752 scopus 로고
    • Several hydrophobic amino acids in the p53 amino-terminal domain are required for transcriptional activation, binding to mdm-2 and the adenovirus 5E1B 55-kD protein
    • Lin, J., Chen, J., Elenbaas, B. & Levine, A. J. Several hydrophobic amino acids in the p53 amino-terminal domain are required for transcriptional activation, binding to mdm-2 and the adenovirus 5E1B 55-kD protein. Genes Dev. 8, 1235-1246 (1994).
    • (1994) Genes Dev. , vol.8 , pp. 1235-1246
    • Lin, J.1    Chen, J.2    Elenbaas, B.3    Levine, A.J.4
  • 3
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase for tumor suppressor p53
    • Honda, R., Tanaka, H. & Yasuda, H. Oncoprotein MDM2 is a ubiquitin ligase for tumor suppressor p53. FEBS Lett. 420, 25-27 (1997).
    • (1997) FEBS Lett. , vol.420 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 4
    • 0032518917 scopus 로고    scopus 로고
    • Nucleo-cytoplasmic 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, D. A., Shenk, T. & Levine, A. J. Nucleo-cytoplasmic 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).
    • (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
  • 5
    • 0032980646 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of oncoprotein Hdm2 is required for Hdm2-mediated degradation of p53
    • Tao, W. & Levine, A. J. Nucleocytoplasmic shuttling of oncoprotein Hdm2 is required for Hdm2-mediated degradation of p53. Proc. Natl Acad. Sci. USA 96, 3077-3080 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 3077-3080
    • Tao, W.1    Levine, A.J.2
  • 6
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • Fornerod, M., Ohno, M., Yoshida, M. & Mattaj, I. W. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 90, 1051-1060 (1997).
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.W.4
  • 7
    • 0030831534 scopus 로고    scopus 로고
    • CRM1 is responsible for intracellular transport mediated by the nuclear export signal
    • Fukuda, M. et al. CRM1 is responsible for intracellular transport mediated by the nuclear export signal. Nature 390, 308-311 (1997).
    • (1997) Nature , vol.390 , pp. 308-311
    • Fukuda, M.1
  • 8
    • 0030748907 scopus 로고    scopus 로고
    • Evidence for a role of CRM1 in signal-mediated nuclear protein export
    • Ossareh-Nazari, B., Bachelerie, F. & Dargemont, C. Evidence for a role of CRM1 in signal-mediated nuclear protein export. Science 278, 141-144 (1997).
    • (1997) Science , vol.278 , pp. 141-144
    • Ossareh-Nazari, B.1    Bachelerie, F.2    Dargemont, C.3
  • 9
    • 0031724593 scopus 로고    scopus 로고
    • Nuclear export is required for degradation of endogenous p53 by MDM2 and human papillomavirus E6
    • Freedman, D. A. & Levine, A. J. Nuclear export is required for degradation of endogenous p53 by MDM2 and human papillomavirus E6. Mol. Cell Biol. 18, 7288-7293 (1998).
    • (1998) Mol. Cell Biol. , vol.18 , pp. 7288-7293
    • Freedman, D.A.1    Levine, A.J.2
  • 10
    • 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. et al. 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).
    • (1997) Oncogene , vol.14 , pp. 1407-1417
    • Middeler, G.1
  • 11
    • 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, J. M. et al. 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).
    • (1999) EMBO J. , vol.18 , pp. 1660-1672
    • Stommel, J.M.1
  • 12
    • 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, 296-299 (1997).
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 13
    • 0031702817 scopus 로고    scopus 로고
    • Regulation of Mdm2-directed degradation by the C terminus of p53
    • Kubbutat, M. H., Ludwig, R. L., Ashcroft, M. & Vousden, K. H. Regulation of Mdm2-directed degradation by the C terminus of p53. Mol. Cell Biol. 18, 5690-5698 (1998).
    • (1998) Mol. Cell Biol. , vol.18 , pp. 5690-5698
    • Kubbutat, M.H.1    Ludwig, R.L.2    Ashcroft, M.3    Vousden, K.H.4
  • 14
    • 0029031942 scopus 로고
    • Oligomerisation of full length p53 contributes to the interaction with mdm2 but not HPV E6
    • Marston, N. J., Jenkins, J. R. & Vousden, K. H. Oligomerisation of full length p53 contributes to the interaction with mdm2 but not HPV E6. Oncogene 10, 1709-1715 (1995).
    • (1995) Oncogene , vol.10 , pp. 1709-1715
    • Marston, N.J.1    Jenkins, J.R.2    Vousden, K.H.3
  • 15
    • 0029760621 scopus 로고    scopus 로고
    • The MDM2 oncoprotein binds specifically to RNA through its RING finger domain
    • Elenbaas, B., Dobbelstein, M., Roth, J., Shenk, T. & Levine, A. J. The MDM2 oncoprotein binds specifically to RNA through its RING finger domain. Mol. Med. 2, 439-451 (1996).
    • (1996) Mol. Med. , vol.2 , pp. 439-451
    • Elenbaas, B.1    Dobbelstein, M.2    Roth, J.3    Shenk, T.4    Levine, A.J.5
  • 16
    • 0033051322 scopus 로고    scopus 로고
    • MDM2 interacts with MDMX through their RING finger domains
    • Tanimura, S. et al. MDM2 Interacts with MDMX through their RING finger domains. FEBS Lett. 447, 5-9 (1999).
    • (1999) FEBS Lett. , vol.447 , pp. 5-9
    • Tanimura, S.1
  • 17
    • 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, 8945-8951 (2000).
    • (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
  • 18
    • 0028849274 scopus 로고
    • p21 is necessary for the p53-mediated G1 arrest in human cancer cells
    • Waldman, T., Kinzler, K. W. & Vogelstein, B. p21 is necessary for the p53-mediated G1 arrest in human cancer cells. Cancer Res. 55, 5187-5190 (1995).
    • (1995) Cancer Res. , vol.55 , pp. 5187-5190
    • Waldman, T.1    Kinzler, K.W.2    Vogelstein, B.3
  • 19
    • 0028205667 scopus 로고
    • Accumulation of p53 in a mutant cell line defective in the ubiquitin pathway
    • Chowdary, D. R., Dermody, J. J., Jha, K. K. & Ozer, H. L. Accumulation of p53 in a mutant cell line defective in the ubiquitin pathway. Mol. Cell Biol. 14, 1997-2003 (1994).
    • (1994) Mol. Cell Biol. , vol.14 , pp. 1997-2003
    • Chowdary, D.R.1    Dermody, J.J.2    Jha, K.K.3    Ozer, H.L.4
  • 20
    • 0027999512 scopus 로고
    • The ribosomal L5 protein is associated with mdm-2 and mdm-2-p53 complexes
    • Marechal, V., Elenbaas, B., Piette, J., Nicolas, J. C. & Levine, A. J. The ribosomal L5 protein is associated with mdm-2 and mdm-2-p53 complexes. Mol. Cell Biol. 14, 7414-7420 (1994).
    • (1994) Mol. Cell Biol. , vol.14 , pp. 7414-7420
    • Marechal, V.1    Elenbaas, B.2    Piette, J.3    Nicolas, J.C.4    Levine, A.J.5
  • 21
    • 0033567356 scopus 로고    scopus 로고
    • Nuclear export of the small ribosomal subunit requires the Ran-GTPase cycle and certain nucleoporins
    • Moy, T. & Silver, P. A. Nuclear export of the small ribosomal subunit requires the Ran-GTPase cycle and certain nucleoporins. Genes Dev. 13, 2118-2133 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 2118-2133
    • Moy, T.1    Silver, P.A.2
  • 22
    • 0034652143 scopus 로고    scopus 로고
    • Subcellular localization of proteasomes and their regulatory complexes in mammalian cells
    • Brooks, P. et al. Subcellular localization of proteasomes and their regulatory complexes in mammalian cells. Biochem. J. 346, 155-161 (2000).
    • (2000) Biochem. J. , vol.346 , pp. 155-161
    • Brooks, P.1
  • 23
    • 0033597443 scopus 로고    scopus 로고
    • Rbxl, a component of the VHL tumor suppressor complex and SCF ubiquitin ligase
    • Kamura, T. et al. Rbxl, a component of the VHL tumor suppressor complex and SCF ubiquitin ligase. Science 284, 657-661 (1999).
    • (1999) Science , vol.284 , pp. 657-661
    • Kamura, T.1
  • 24
    • 0033596977 scopus 로고    scopus 로고
    • grr and Rbxl
    • grr and Rbxl. Science 284, 662-665 (1999).
    • (1999) Science , vol.284 , pp. 662-665
    • Skowyra, D.1
  • 25
    • 0033600759 scopus 로고    scopus 로고
    • Cytoplasmically 'sequestered' wild type p53 protein is resistant to Mdm2-mediated degradation
    • Zaika, A., Marchenko, N. & Moll, U. M. Cytoplasmically 'sequestered' wild type p53 protein is resistant to Mdm2-mediated degradation. J. Biol. Chem. 274, 27474-27480 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 27474-27480
    • Zaika, A.1    Marchenko, N.2    Moll, U.M.3
  • 26
    • 0031603760 scopus 로고    scopus 로고
    • A function for monoubiquitination in the internalization of a G protein-coupled receptor
    • Terrell, J., Shih, S., Dunn, R. & Hicke, L. A function for monoubiquitination in the internalization of a G protein-coupled receptor. Mol. Cell 1, 193-202 (1998).
    • (1998) Mol. Cell , vol.1 , pp. 193-202
    • Terrell, J.1    Shih, S.2    Dunn, R.3    Hicke, L.4
  • 27
    • 0030700220 scopus 로고    scopus 로고
    • Ubiquitin-dependent internalization and down-regulation of plasma membrane proteins
    • Hicke, L. Ubiquitin-dependent internalization and down-regulation of plasma membrane proteins. FASEB J. 11, 1215-1226 (1997).
    • (1997) FASEB J. , vol.11 , pp. 1215-1226
    • Hicke, L.1
  • 28
    • 0033570892 scopus 로고    scopus 로고
    • Activation of p53 by conjugation to the ubiquitin-like protein SUMO-1
    • Gostissa, M. et al. Activation of p53 by conjugation to the ubiquitin-like protein SUMO-1. EMBO J. 18, 6462-6471 (1999).
    • (1999) EMBO J. , vol.18 , pp. 6462-6471
    • Gostissa, M.1
  • 29
    • 0033571214 scopus 로고    scopus 로고
    • SUMO-1 modification activates the transcriptional response of p53
    • Rodriguez, M. S. et al. SUMO-1 modification activates the transcriptional response of p53. EMBO J. 18, 6455-6461 (1999).
    • (1999) EMBO J. , vol.18 , pp. 6455-6461
    • Rodriguez, M.S.1
  • 32
    • 0033000482 scopus 로고    scopus 로고
    • Mutations in human ARF exon 2 disrupt its nucleolar localization and impair its ability to block nuclear export of MDM2 and p53
    • Zhang, Y. & Xiong, Y. Mutations in human ARF exon 2 disrupt its nucleolar localization and impair its ability to block nuclear export of MDM2 and p53. Mol. Cell 3, 579-591 (1999).
    • (1999) Mol. Cell , vol.3 , pp. 579-591
    • Zhang, Y.1    Xiong, Y.2
  • 33
    • 0033521621 scopus 로고    scopus 로고
    • Association of p19ARF with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53
    • Honda, R. & Yasuda, H. Association of p19ARF with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53. EMBO J. 18, 22-27 (1999).
    • (1999) EMBO J. , vol.18 , pp. 22-27
    • Honda, R.1    Yasuda, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.