Positive or negative MARE-dependent transcriptional regulation is determined by the abundance of small maf proteins
Article Abstract:
Results show that the Maf transcription factor binding to Maf recognition elements following dimerization with or without Cap-N-Collar proteins contributes to the gene transcription in erythroid and megakaryocytic cells. Data suggest that transcription regulation through Maf recognition element is dependent on activating Cap-N-Collar proteins and Maf proteins.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2000
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Impaired megakaryopoiesis and behavioral defects in mafG-null mutant mice
Article Abstract:
The small Maf proteins, MafG, MafK and MafF, act as heterodimeric partner molecules of CNC family proteins for binding in vitro to MARE sites. They have been implicated in regulation of transcription and chromatin structure, but evidence is lacking for in vivo systems. The mafG and mafK genes have been ablated in mice by replacing the coding sequences in their entirety with the E. coli lacZ gene. Evidence that the small Maf transcription factors are essential in cellular differentiation and embryonic development now has been found.
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 1998
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Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
Article Abstract:
Keap1, a newly identified protein, represses nuclear activation of antioxidant-responsive elements by binding to an amino-terminal domain. Transcription factor Nrf2 is required for the antioxidant responsive element (ARE)-mediated induction of phase II oxidative and detoxifying stress enzyme genes. A new protein has been identified as result of deailed analysis of differential Nrf2 activity seen in transfected cell lines. The protein is called Keap1 and it suppresses Nrf2 transcriptional activity by binding specifically to its evolutionarily conserved amino-terminal regulatory domain. The closest homolog is a Drosophila actin-binding protein. Keap1 may be an Nrf2 cytoplasmic effector. Electrophilic agents antagonize Deap1 inhibition of Nrf2 activity in vivo. Nrf2 can go from the cytoplasm to the nucleus to potentiate ARE response. It seems Keap1 and Nrf2 make up a vital cellular sensor for oxidative stress and mediate a vital step in the signaling pathway leading to transcriptional activation.
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 1999
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