Control of p53 ubiquitination and nuclear export by MDM2 and ARF

被引:0
作者
Zhang, YP
Xiong, Y [1 ]
机构
[1] Univ N Carolina, Sch Med, Lineberger Comprehens Canc Ctr, Chapel Hill, NC 27599 USA
[2] Univ N Carolina, Sch Med, Dept Biochem & Biophys, Chapel Hill, NC 27599 USA
[3] Univ Texas, MD Anderson Canc Ctr, Dept Mol & Cellular Oncol, Houston, TX 77030 USA
来源
CELL GROWTH & DIFFERENTIATION | 2001年 / 12卷 / 04期
关键词
D O I
暂无
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
p53 and ARF-INK4a are the two most frequently altered loci in human tumors. The activity of p53 protein is inhibited during normal cell growth by the proto-oncoprotein MDM2 through either repression of p53-mediated transcription in the nucleus or proteasomal degradation of p53 protein in the cytoplasm. Responding to oncogenic signal-activated cell hyperproliferation, ARF-mediated antagonism of MDM2 inhibition results in p53 becoming active and its protein levels rising. The biochemical mechanisms of ubiquitination and nuclear export that underlie the functions of ARF and MDM2 in p53 control continue to emerge.
引用
收藏
页码:175 / 186
页数:12
相关论文
共 120 条
  • [1] SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box
    Bai, C
    Sen, P
    Hofmann, K
    Ma, L
    Goebl, M
    Harper, JW
    Elledge, SJ
    [J]. CELL, 1996, 86 (02) : 263 - 274
  • [2] Mdm2 binds p73α without targeting degradation
    Bálint, E
    Bates, S
    Vousden, KH
    [J]. ONCOGENE, 1999, 18 (27) : 3923 - 3929
  • [3] p14ARF links the tumour suppressors RB and p53
    Bates, S
    Phillips, AC
    Clark, PA
    Stott, F
    Peters, G
    Ludwig, RL
    Vousden, KH
    [J]. NATURE, 1998, 395 (6698) : 124 - 125
  • [4] An intact HDM2 RING-finger domain is required for nuclear exclusion of p53
    Boyd, SD
    Tsai, KY
    Jacks, T
    [J]. NATURE CELL BIOLOGY, 2000, 2 (09) : 563 - 568
  • [5] Crystal structure of the complex of the cyclin D dependent kinase Cdk6 bound to the cell-cycle inhibitor p19INK4d
    Brotherton, DH
    Dhanaraj, V
    Wick, S
    Brizuela, L
    Domaille, PJ
    Volyanik, E
    Xu, X
    Parisini, E
    Smith, BO
    Archer, SJ
    Serrano, M
    Brenner, SL
    Blundell, TL
    Laue, ED
    [J]. NATURE, 1998, 395 (6699) : 244 - 250
  • [6] RETRACTED: SUMO-1 modification of Mdm2 prevents its self-ubiquitination and increases Mdm2 ability to ubiquitinate p53 (Retracted Article)
    Buschmann, T
    Fuchs, SY
    Lee, CG
    Pan, ZQ
    Ronai, Z
    [J]. CELL, 2000, 101 (07) : 753 - 762
  • [7] To be or not to be in the nucleolus
    Carmo-Fonseca, M
    Mendes-Soares, L
    Campos, I
    [J]. NATURE CELL BIOLOGY, 2000, 2 (06) : E107 - E112
  • [8] TARGETING OF ADENOVIRUS E1A AND E4-ORF3 PROTEINS TO NUCLEAR MATRIX-ASSOCIATED PML BODIES
    CARVALHO, T
    SEELER, JS
    OHMAN, K
    JORDAN, P
    PETTERSSON, U
    AKUSJARVI, G
    CARMOFONSECA, M
    DEJEAN, A
    [J]. JOURNAL OF CELL BIOLOGY, 1995, 131 (01) : 45 - 56
  • [9] MAPPING OF THE P53 AND MDM-2 INTERACTION DOMAINS
    CHEN, JD
    MARECHAL, V
    LEVINE, AJ
    [J]. MOLECULAR AND CELLULAR BIOLOGY, 1993, 13 (07) : 4107 - 4114
  • [10] Cooperative effects of INK4a and ras in melanoma susceptibility in vivo
    Chin, L
    Pomerantz, J
    Polsky, D
    Jacobson, M
    Cohen, C
    CordonCardo, C
    Horner, JW
    DePinho, RA
    [J]. GENES & DEVELOPMENT, 1997, 11 (21) : 2822 - 2834