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Volumn 332, Issue 3, 2005, Pages 702-709

Modification of MDMX by sumoylation

Author keywords

ARF; Degradation; MDM2; MDMX; p53; Sumoylation; Ubiquitination

Indexed keywords

LYSINE; PROTEIN MDM2; PROTEIN P53; SUMO 1 PROTEIN;

EID: 19744363342     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.05.012     Document Type: Article
Times cited : (15)

References (35)
  • 1
    • 0034915032 scopus 로고    scopus 로고
    • Control of p53 ubiquitination and nuclear export by MDM2 and ARF
    • Y. Zhang, and Y. Xiong 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
  • 2
    • 0032931517 scopus 로고    scopus 로고
    • The p53 pathway
    • C. Prives, and P.A. Hall The p53 pathway J. Pathol. 187 1999 112 126
    • (1999) J. Pathol. , vol.187 , pp. 112-126
    • Prives, C.1    Hall, P.A.2
  • 3
    • 0032191393 scopus 로고    scopus 로고
    • Tumor surveillance via the ARF-p53 pathway
    • C.J. Sherr 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
  • 4
    • 0033732303 scopus 로고    scopus 로고
    • MDM2 inhibits p300-mediated p53 acetylation and activation by forming a ternary complex with the two proteins
    • E. Kobet, X. Zeng, Y. Zhu, D. Keller, and H. Lu MDM2 inhibits p300-mediated p53 acetylation and activation by forming a ternary complex with the two proteins Proc. Natl. Acad. Sci. USA 97 2002 12547 12552
    • (2002) 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
  • 5
    • 0035868964 scopus 로고    scopus 로고
    • P300/CBP-mediated p53 acetylation is commonly induced by p53-activating agents and inhibited by MDM2
    • A. Ito, C.H. Lai, X. Zhao, S. Saito, M.H. Hamilton, E. Appella, and T.P. Yao p300/CBP-mediated p53 acetylation is commonly induced by p53-activating agents and inhibited by MDM2 EMBO J. 20 2001 1331 1340
    • (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
  • 9
    • 0037147143 scopus 로고    scopus 로고
    • MdmX is a RING finger ubiquitin ligase capable of synergistically enhancing Mdm2 ubiquitination
    • J.C. Badciong, and A.L. Haas MdmX is a RING finger ubiquitin ligase capable of synergistically enhancing Mdm2 ubiquitination J. Biol. Chem. 277 2002 49668 49675
    • (2002) J. Biol. Chem. , vol.277 , pp. 49668-49675
    • Badciong, J.C.1    Haas, A.L.2
  • 11
    • 0028823020 scopus 로고
    • Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
    • R.M. Oca Luna, D.S. Wagner, and G. Lozano 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
    • Oca Luna, R.M.1    Wagner, D.S.2    Lozano, G.3
  • 12
    • 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
    • J. Parant, A. Chavez-Reyes, N.A. Little, W. Yan, V. Reinke, A.G. Jochemsen, and G. Lozano Rescue of embryonic lethality in Mdm4-null mice by loss of Trp53 suggests a nonoverlapping pathway with MDM2 to regulate p53 Nat. Genet. 29 2002 92 95
    • (2002) 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
  • 21
    • 0035812848 scopus 로고    scopus 로고
    • SP-RING for SUMO: New functions bloom for a ubiquitin-like protein
    • M. Hochstrasser SP-RING for SUMO: new functions bloom for a ubiquitin-like protein Cell 107 2002 5 8
    • (2002) Cell , vol.107 , pp. 5-8
    • Hochstrasser, M.1
  • 22
    • 0035918226 scopus 로고    scopus 로고
    • SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting
    • M.S. Rodriguez, C. Dargemont, and R.T. Hay SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting J. Biol. Chem. 276 2002 12654 12669
    • (2002) J. Biol. Chem. , vol.276 , pp. 12654-12669
    • Rodriguez, M.S.1    Dargemont, C.2    Hay, R.T.3
  • 23
    • 0041353442 scopus 로고    scopus 로고
    • MDM2-ARF complex regulates p53 sumoylation
    • L. Chen, and J. Chen MDM2-ARF complex regulates p53 sumoylation Oncogene 22 2003 5348 5357
    • (2003) Oncogene , vol.22 , pp. 5348-5357
    • Chen, L.1    Chen, J.2
  • 24
    • 0035799530 scopus 로고    scopus 로고
    • Functional analysis and intracellular localization of p53 modified by SUMO-1
    • S.S. Kwek, J. Derry, A.L. Tyner, Z. Shen, and A.V. Gudkov Functional analysis and intracellular localization of p53 modified by SUMO-1 Oncogene 20 2002 2587 2599
    • (2002) Oncogene , vol.20 , pp. 2587-2599
    • Kwek, S.S.1    Derry, J.2    Tyner, A.L.3    Shen, Z.4    Gudkov, A.V.5
  • 25
    • 0034680441 scopus 로고    scopus 로고
    • Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif
    • A. Minty, X. Dumont, M. Kaghad, and D. Caput Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif J. Biol. Chem. 275 2002 36316 36323
    • (2002) J. Biol. Chem. , vol.275 , pp. 36316-36323
    • Minty, A.1    Dumont, X.2    Kaghad, M.3    Caput, D.4
  • 26
    • 0042592947 scopus 로고    scopus 로고
    • MDM2 promotes ubiquitination and degradation of MDMX
    • Y. Pan, and J. Chen MDM2 promotes ubiquitination and degradation of MDMX Mol. Cell. Biol. 23 2003 5113 5121
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5113-5121
    • Pan, Y.1    Chen, J.2
  • 29
    • 0035899468 scopus 로고    scopus 로고
    • Different effects of p14ARF on the levels of ubiquitinated p53 and Mdm2 in vivo
    • D. Xirodimas, M.K. Saville, C. Edling, D.P. Lane, and S. Lain Different effects of p14ARF on the levels of ubiquitinated p53 and Mdm2 in vivo Oncogene 20 2002 4972 4983
    • (2002) Oncogene , vol.20 , pp. 4972-4983
    • Xirodimas, D.1    Saville, M.K.2    Edling, C.3    Lane, D.P.4    Lain, S.5
  • 30
    • 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
    • Y. Zhang, and Y. Xiong 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 1999 579 591
    • (1999) Mol. Cell , vol.3 , pp. 579-591
    • Zhang, Y.1    Xiong, Y.2
  • 31
    • 0034603179 scopus 로고    scopus 로고
    • Differential regulation of sentrinized proteins by a novel sentrin-specific protease
    • L. Gong, S. Millas, G.G. Maul, and E.T. Yeh Differential regulation of sentrinized proteins by a novel sentrin-specific protease J. Biol. Chem. 275 2002 3355 3359
    • (2002) J. Biol. Chem. , vol.275 , pp. 3355-3359
    • Gong, L.1    Millas, S.2    Maul, G.G.3    Yeh, E.T.4
  • 32
    • 0027222956 scopus 로고
    • Mapping of the p53 and mdm-2 interaction domains
    • J. Chen, V. Marechal, and A.J. Levine 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
  • 33
    • 0029171789 scopus 로고
    • Regulation of transcription functions of the p53 tumor suppressor by the mdm-2 oncogene
    • J. Chen, J. Lin, and A.J. Levine Regulation of transcription functions of the p53 tumor suppressor by the mdm-2 oncogene Mol. Med. 1 1995 142 152
    • (1995) Mol. Med. , vol.1 , pp. 142-152
    • Chen, J.1    Lin, J.2    Levine, A.J.3
  • 34
    • 0036837868 scopus 로고    scopus 로고
    • DNA damage induces MDMX nuclear translocation by p53-dependent and -independent mechanisms
    • Changgong Li, Lihong Chen, and Jiandong Chen DNA damage induces MDMX nuclear translocation by p53-dependent and -independent mechanisms Mol. Cell. Biol. 22 2002 7562 7571
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7562-7571
    • Changgong, L.1    Lihong, C.2    Jiandong, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.