v-maf, a viral oncogene that encodes a "leucine zipper" motif.

Nishizawa, Makoto; Kataoka, Kohsuke; Goto, Naoaki; Fujiwara, Kôsaku; Kawai, Sadaaki

doi:10.1073/pnas.86.20.7711

Cited by 257 publications

(194 citation statements)

References 36 publications

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“…The ®rst member of the Maf gene family, v-maf, was identi®ed in an acutely oncogenic avian retrovirus which induces musculoaponeurotic ®brosarcomas in chicken (Nishizawa et al, 1989). Maf proteins are bZIP transcription factors of the AP1 superfamily, exhibiting high similarity in their DNA binding domain.…”

Section: Introductionmentioning

confidence: 99%

mafA, a novel member of the maf proto-oncogene family, displays developmental regulation and mitogenic capacity in avian neuroretina cells

et al. 1998

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Section: Introductionmentioning

confidence: 99%

mafA, a novel member of the maf proto-oncogene family, displays developmental regulation and mitogenic capacity in avian neuroretina cells

et al. 1998

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“…The Maf transcription factors are basic-leucine zipper (b-Zip) family proteins and are homologues of the v-Maf oncoprotein, which was isolated as a transforming component of the avian musculoaponeurotic fibrosarcoma virus, AS42 [1,2]. Maf family proteins are divided into two subgroups, the large Maf and the small Maf proteins.…”

mentioning

confidence: 99%

Mouse MafA, homologue of zebrafish somite Maf 1, contributes to the specific transcriptional activity through the insulin promoter

Kajihara

Sone

Amemiya

et al. 2003

Biochemical and Biophysical Research Communications

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Large Maf transcription factors, which are members of the basic leucine zipper (b-Zip) superfamily, have been reported to be involved in embryonic development and cell differentiation. Previously, we isolated a novel zebrafish large Maf cDNA, somite Maf1 (SMaf1), which possesses transactivational activity within its N-terminus domain. To elucidate SMaf1 function in mammals, we tried to isolate the mouse homologue of zebrafish SMaf1. We isolated the mouse homologue of zebrafish SMaf1, which is the same molecule as the recently reported MafA. MafA mRNA was detected in formed somites, head neural tube, and liver cells in the embryos. In the adult mouse, MafA transcript was amplified in the brain, lung, spleen, and kidney by RT-PCR. MafA mRNA was also detectable in b-cell line. Next, we analyzed the transcriptional activity of MafA using rat insulin promoters I and II (RIPI and II), since a part of RIP sequence was similar to the Maf recognition element (MARE) and MafA was expressed in pancreatic b-cells. MafA was able to activate transcription from RIPII, but not RIPI, in a dose dependent manner and the activity was dependent on RIPE3b/C1 sequences. In addition, the amount of MafA protein was regulated by glucose concentration. These results indicate that MafA is the homologue of zebrafish SMaf1 and acts as a transcriptional activator of the insulin gene promoter through the RIPE3b element.

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“…Coexpression of Fos and small Mafs could not activate a promoter with tandem repeats of the NF-E2 site. These results raise the possibility that tissue-specific gene expression and differentiation of erythroid cells are regulated by competition among Fos, NF-E2 p45, and Ech for small Maf proteins and for binding sites.The maf oncogene was identified by structural analysis of the genome of the AS42 avian transforming retrovirus (26,40). It encodes a nuclear basic-leucine zipper (bZip) protein which can form a homodimer through its zipper structure (23).…”

mentioning

confidence: 99%

“…The maf oncogene was identified by structural analysis of the genome of the AS42 avian transforming retrovirus (26,40). It encodes a nuclear basic-leucine zipper (bZip) protein which can form a homodimer through its zipper structure (23).…”

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confidence: 99%

Small Maf Proteins Heterodimerize with Fos and May Act as Competitive Repressors of the NF-E2 Transcription Factor

Kataoka

Igarashi

Itoh

et al. 1995

Molecular and Cellular Biology

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The maf oncogene encodes a bZip nuclear protein which recognizes sequences related to an AP-1 site either as a homodimer or as heterodimers with Fos and Jun. We describe here a novel maf-related gene, mafG, which shows extensive homology with two other maf-related genes, mafK and mafF. These three maf-related genes encode small basic-leucine zipper proteins lacking the trans-activator domain of v-Maf. Bacterially expressed small Maf proteins bind to DNA as homodimers with a sequence recognition profile that is virtually identical to that of v-Maf. As we have previously described, the three small Maf proteins also dimerize with the large subunit of NF-E2 (p45) to form an erythroid cell-specific transcription factor, NF-E2, which has distinct DNA-binding specificity. This study shows that the small Maf proteins can also dimerize among themselves and with Fos and a newly identified p45-related molecule (Ech) but not with v-Maf or Jun. Although the small Maf proteins preferentially recognize the consensus NF-E2 sequence as heterodimers with either NF-E2 p45, Ech, or Fos, these heterodimers seemed to be different in their transactivation potentials. Coexpression of Fos and small Mafs could not activate a promoter with tandem repeats of the NF-E2 site. These results raise the possibility that tissue-specific gene expression and differentiation of erythroid cells are regulated by competition among Fos, NF-E2 p45, and Ech for small Maf proteins and for binding sites.The maf oncogene was identified by structural analysis of the genome of the AS42 avian transforming retrovirus (26,40). It encodes a nuclear basic-leucine zipper (bZip) protein which can form a homodimer through its zipper structure (23). Recently, we reported that the v-Maf homodimer specifically recognizes two relatively long palindromic DNA sequences, TGCTGACTCAGCA and TGCTGACGTCAGCA, at roughly equal efficiency (24). The middle parts of the two consensus binding sequences for Maf are identical with two well-characterized binding sequences of the AP-1 transcription factor, the 12-O-tetradecanoylphorbol-13-acetate (TPA)-responsive element (TRE; TGACTCA) and the cyclic AMP-responsive element (CRE; TGACGTCA), respectively. We therefore named the two types of recognition elements TRE-type Maf recognition elements (MAREs) and CRE-type MAREs. It was also recently revealed that Maf forms heterodimers with the two major components of AP-1, Fos and Jun (24, 27, 28). These heterodimers preferably bind to asymmetric DNA sequences consisting of the two consensus binding sequences of Maf homodimer and AP-1 (24). Thus, Maf and the two AP-1 components are suggested to interact with each other in a cooperative or inhibitory way in association with their recognition sequences by forming heterodimers of altered binding specificities.Like many other proto-oncogenes, the c-maf gene is a member of a gene family. To date, four maf-related genes, mafK, mafF, mafB, and nrl, have been reported (14,22,53). Their gene products are closely related to v-Maf especially in the structur...

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v-maf, a viral oncogene that encodes a "leucine zipper" motif.

Abstract: We have molecularly cloned the provirus of the avian musculoaponeurotic fibrosarcoma virus AS42.

Cited by 257 publications

References 36 publications

mafA, a novel member of the maf proto-oncogene family, displays developmental regulation and mitogenic capacity in avian neuroretina cells

mafA, a novel member of the maf proto-oncogene family, displays developmental regulation and mitogenic capacity in avian neuroretina cells

Mouse MafA, homologue of zebrafish somite Maf 1, contributes to the specific transcriptional activity through the insulin promoter

Small Maf Proteins Heterodimerize with Fos and May Act as Competitive Repressors of the NF-E2 Transcription Factor

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