Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region.

Moi, Paolo; Chan, Karina; Asunis, Isadora; Cao, Antonio; Kan, Yuet Wai

doi:10.1073/pnas.91.21.9926

Cited by 1,387 publications

(1,028 citation statements)

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“…Whereas Nrf1 and Nrf2 are expressed ubiquitously (Chan et al, 1993b;Moi et al, 1994), our results suggest that their functions depend on the presence of partner molecules. Thus, it is likely that expression of the CNC family of factors and the small Maf family of proteins mutually restricts their activity as functional activators in certain cell lineages.…”

Section: Discussionmentioning

confidence: 51%

“…Recently, new CNC family members, Nrf1 (Caterina et al, 1994;Chan et al, 1993b;Luna et al, 1994) and Nrf2 (Moi et al, 1994) were identi®ed in human erythroleukemic cell lines. Nrf1 has been shown to be a potent transcriptional activator in erythroid cells, as compared with p45 (Caterina et al, 1994).…”

Section: Mafk and Mafg Bind To Nf-e2 Sites By Forming Heterodimers Wimentioning

confidence: 99%

“…MafK has been shown to be an authentic subunit of murine NF-E2 (Andrews et al, 1993a;Igarashi et al, 1995a). In man, two other CNC family proteins, Nrf1/LCR-F1/TCF11 (Caterina et al, 1994;Chan et al, 1993b;Luna et al, 1994) and Nrf2 (Moi et al, 1994) have been identi®ed, although their DNA binding activities have not been characterized in detail.…”

Section: Introductionmentioning

confidence: 99%

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Human small Maf proteins form heterodimers with CNC family transcription factors and recognize the NF-E2 motif

et al. 1997

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The transcription factor NF-E2, a heterodimeric protein complex composed of p45 and small Maf family proteins, is considered crucial for the regulation of erythroid gene expression and platelet formation. To facilitate the characterization of NF-E2 functions in human cells, we isolated cDNAs encoding two members of the small Maf family, MafK and MafG. The human mafK and mafG genes encode proteins of 156 and 162 amino acid residues, respectively, whose deduced amino acid sequences show approximately 95% identity to their respective chicken counterparts. Expression of mafK mRNA is high in heart, skeletal muscle and placenta, whereas mafG mRNA is abundant in skeletal muscle and is moderately expressed in heart and brain. Both are expressed in all hematopoietic cell lines, including those of erythroid and megakaryocytic lineages. In electrophoretic gel mobility shift assays binding to NF-E2 sites was found to depend on formation of homodimers or heterodimers with p45 and p45-related CNC family proteins. The results suggest that the small Maf family proteins function in human cells through interaction with various basic-leucine zipper-type transcription factors.

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Section: Discussionmentioning

confidence: 51%

Section: Mafk and Mafg Bind To Nf-e2 Sites By Forming Heterodimers Wimentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Human small Maf proteins form heterodimers with CNC family transcription factors and recognize the NF-E2 motif

et al. 1997

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“…NRF2 (NF-E2-related factor 2, NFE2L2) is a master transcription factor involved in oxidative and xenobiotic stress responses [1]. NRF2 features a Cap ''n'' collar (CNC) basic leucine zipper (bZIP) structure that enables NRF2 to form heterodimer with the ZIP domain of small MAF proteins [2].…”

Section: Introductionmentioning

confidence: 99%

The NRF2‐related interactome and regulome contain multifunctional proteins and fine‐tuned autoregulatory loops

et al. 2012

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a b s t r a c t NRF2 is a well-known, master transcription factor (TF) of oxidative and xenobiotic stress responses. Recent studies uncovered an even wider regulatory role of NRF2 influencing carcinogenesis, inflammation and neurodegeneration. Prompted by these advances here we present a systems-level resource for NRF2 interactome and regulome that includes 289 protein-protein, 7469 TF-DNA and 85 miRNA interactions. As systems-level examples of NRF2-related signaling we identified regulatory loops of NRF2 interacting proteins (e.g., JNK1 and CBP) and a fine-tuned regulatory system, where 35 TFs regulated by NRF2 influence 63 miRNAs that down-regulate NRF2. The presented network and the uncovered regulatory loops may facilitate the development of efficient, NRF2-based therapeutic agents.

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“…2 Nuclear factor (erythroid-derived 2)-like 2 (NRF2) is a member of the Cap 'n' Collar basic leucine zipper transcription factor family that protects cells from reactive oxygen species through the regulation of a number of cytoprotective genes including heme oxygenase-1 (HO-1) and NAD(P)H dehydrogenase quinone 1 (NQO1). [3][4][5] In cancer, NRF2 activation is pro-tumoural in a spectrum of malignancies through mutations in NRF2 or its cytosolic inhibitor KEAP1. [6][7][8][9] However, we have previously shown that in human AML constitutive activation of the NRF2 signalling pathway is not through somatic mutations of NRF2/Keap1 but as a consequence of upstream constitutive activation by NF-κB.…”

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confidence: 99%

NRF2-driven miR-125B1 and miR-29B1 transcriptional regulation controls a novel anti-apoptotic miRNA regulatory network for AML survival

et al. 2014

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Transcription factor NRF2 is an important regulator of oxidative stress. It is involved in cancer progression, and has abnormal constitutive expression in acute myeloid leukaemia (AML). Posttranscriptional regulation by microRNAs (miRNAs) can affect the malignant phenotype of AML cells. In this study, we identified and characterised NRF2-regulated miRNAs in AML. An miRNA array identified miRNA expression level changes in response to NRF2 knockdown in AML cells. Further analysis of miRNAs concomitantly regulated by knockdown of the NRF2 inhibitor KEAP1 revealed the major candidate NRF2-mediated miRNAs in AML. We identified miR-125B to be upregulated and miR-29B to be downregulated by NRF2 in AML. Subsequent bioinformatic analysis identified putative NRF2 binding sites upstream of the miR-125B1 coding region and downstream of the mir-29B1 coding region. Chromatin immunoprecipitation analyses showed that NRF2 binds to these antioxidant response elements (AREs) located in the 5′ untranslated regions of miR-125B and miR-29B. Finally, primary AML samples transfected with anti-miR-125B antagomiR or miR-29B mimic showed increased cell death responsiveness either alone or co-treated with standard AML chemotherapy. In summary, we find that NRF2 regulation of miR-125B and miR-29B acts to promote leukaemic cell survival, and their manipulation enhances AML responsiveness towards cytotoxic chemotherapeutics.

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Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region.

Abstract: Hypersensitive site 2 located in the f-globin locus control region confers high levels of expression to the genes of the 1-globin cluster. A tandem repeat of the consensus sequence for the transcription factors AP1 and NF-E2 (acti-

Cited by 1,387 publications

References 41 publications

Human small Maf proteins form heterodimers with CNC family transcription factors and recognize the NF-E2 motif

Human small Maf proteins form heterodimers with CNC family transcription factors and recognize the NF-E2 motif

The NRF2‐related interactome and regulome contain multifunctional proteins and fine‐tuned autoregulatory loops

NRF2-driven miR-125B1 and miR-29B1 transcriptional regulation controls a novel anti-apoptotic miRNA regulatory network for AML survival

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