Small Maf proteins in mammalian gene control: Mere dimerization partners or dynamic transcriptional regulators?

被引:123
作者
Blank, Volker [1 ,2 ,3 ]
机构
[1] Lady Davis Inst Med Res, Montreal, PQ H3T 1E2, Canada
[2] McGill Univ, Dept Med, Montreal, PQ, Canada
[3] McGill Univ, Dept Physiol, Montreal, PQ, Canada
基金
加拿大健康研究院;
关键词
Maf transcription factor; CNC; Nrf2; oxidative stress; inflammation;
D O I
10.1016/j.jmb.2007.11.074
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The small Maf basic leucine zipper (bZIP) proteins MafF, MafG and MafK, while modest in size, have emerged as crucial regulators of mammalian gene expression. Intriguingly, small Mats do not contain an obvious transcriptional activation domain. However, previously perceived as "mere" partner molecules conferring DNA binding specificity to complexes with larger bZIP proteins, such as the CNC family member Nrf2, it has become clear that small Maf proteins are essential and dynamically regulated transcription factors. Current data suggest stringent control of small Maf protein function through transcriptional and post-translational mechanisms. Initial gene targeting experiments revealed considerable functional redundancy among small Maf proteins in vivo. This was not unexpected, due to the high level of homology among the three small Mafs. Nevertheless, further studies showed that these transcription factors have critical roles in various cellular processes, including stress signaling, hematopoiesis, CNS function and oncogenesis. Recent data provide a possible link between small Maf-mediated transcription and the inflammatory response. (c) 2007 Elsevier Ltd. All rights reserved.
引用
收藏
页码:913 / 925
页数:13
相关论文
共 121 条
  • [41] Small Maf proteins interact with the human transcription factor TCF11/Nrf1/LCR-F1
    Johnsen, O
    Skammelsrud, N
    Luna, L
    Nishizawa, M
    Prydz, H
    Kolsto, AB
    [J]. NUCLEIC ACIDS RESEARCH, 1996, 24 (21) : 4289 - 4297
  • [42] Molecular mechanism of Nrf2 activation by oxidative stress
    Kang, KW
    Lee, SJ
    Kim, SG
    [J]. ANTIOXIDANTS & REDOX SIGNALING, 2005, 7 (11-12) : 1664 - 1673
  • [43] MAF NUCLEAR ONCOPROTEIN RECOGNIZES SEQUENCES RELATED TO AN AP-1 SITE AND FORMS HETERODIMERS WITH BOTH FOS AND JUN
    KATAOKA, K
    NODA, M
    NISHIZAWA, M
    [J]. MOLECULAR AND CELLULAR BIOLOGY, 1994, 14 (01) : 700 - 712
  • [44] STRUCTURE-FUNCTION ANALYSIS OF THE MAF ONCOGENE PRODUCT, A MEMBER OF THE B-ZIP PROTEIN FAMILY
    KATAOKA, K
    NISHIZAWA, M
    KAWAI, S
    [J]. JOURNAL OF VIROLOGY, 1993, 67 (04) : 2133 - 2141
  • [45] KATAOKA K, 1995, MOL CELL BIOL, V15, P2180
  • [46] Maf and Jun nuclear oncoproteins share downstream target genes for inducing cell transformation
    Kataoka, K
    Shioda, S
    Yoshitomo-Nakagawa, K
    Handa, H
    Nishizawa, M
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (39) : 36849 - 36856
  • [47] A set of Hox proteins interact with the Maf oncoprotein to inhibit its DNA binding, transactivation, and transforming activities
    Kataoka, K
    Yoshitomo-Nakagawa, K
    Shioda, S
    Nishizawa, M
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (01) : 819 - 826
  • [48] Kataoka K, 1996, ONCOGENE, V12, P53
  • [49] Multiple mechanisms and functions of Maf transcription factors in the regulation of tissue-specific genes
    Kataoka, Kohsuke
    [J]. JOURNAL OF BIOCHEMISTRY, 2007, 141 (06) : 775 - 781
  • [50] Genetic evidence that small Maf proteins are essential for the activation of antioxidant response element-dependent genes
    Katsuoka, F
    Motohashi, H
    Ishii, T
    Aburatani, H
    Engel, JD
    Yamamoto, M
    [J]. MOLECULAR AND CELLULAR BIOLOGY, 2005, 25 (18) : 8044 - 8051