Fos-Associated Protein p39 Is the Product of the
            <i>jun</i>
            Proto-Oncogene

Rauscher, Frank J.; Cohen, Donna R.; Curran, Tom; Bos, Timothy J.; Vogt, Peter K.; Bohmann, Dirk; Tjian, Robert; Franza, B. R.

doi:10.1126/science.3130660

Cited by 636 publications

(268 citation statements)

References 46 publications

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“…GCN4 and the mammalian AP-1, known at that time only as a transcription factor interacting with a specific enhancer sequence, share the same DNA binding specificity (Short, 1987;Haluska et al, 1988). Using this specific piece of DNA for affinity chromatography, the mammalian c-Jun was co-purified with c-Fos, marking the first identification of AP-1 as a heterodimer of c-Jun and c-Fos (Angel et al, 1988a;Harshman et al, 1988;Rauscher et al, 1988aRauscher et al, , 1988b.…”

Section: C-jun a Member Of The Ap-1 Complexmentioning

confidence: 99%

c-Jun, at the crossroad of the signaling network

2011

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Section: C-jun a Member Of The Ap-1 Complexmentioning

confidence: 99%

c-Jun, at the crossroad of the signaling network

2011

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“…In recent years a variety of transcription factors have been shown to bind DNA as heterodimers (Halazonetis et al 1988; Kouzarides and Ziff 1988;Nakabeppu et al 1988;Rauscher et al 1988;Murre et al 1989;Blackwood and Eisenman 1991). Heterodimerization appears necessary for high-affinity binding to DNA, and in the case of c-Fos/c-Jun (Chiu et al 1988;Sassone-Corsi et al 1988) and c-Myc/Max (Amati et al 1992;Kretzner et al 1992), dimerization has been correlated with higher transcriptional activity.…”

Section: Discussionmentioning

confidence: 99%

Heterodimerization of the transcription factors E2F-1 and DP-1 leads to cooperative trans-activation.

Helin¹,

Wu²,

Fattaey³

et al. 1993

Genes Dev.

468

484

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The E2F transcription factor has been implicated in the regulation of genes whose products are involved in cell proliferation. Two proteins have recently been identified with E2F-like properties. One of these proteins, E2F-1, has been shown to mediate E2F-dependent trans-activation and to bind the hypophosphorylated form of the retinoblastoma protein {pRB). The other protein, mudne DP-1, was purified from an E2F DNA-affinity column, and it was subsequently shown to bind the consensus E2F DNA-binding site. To study a possible interaction between E2F-1 and DP-1, we have now isolated a cDNA for the human homolog of DP-1. Human DP-1 and E2F-1 associate both in vivo and in vitro, and this interaction leads to enhanced binding to E2F DNA-binding sites. The association of E2F-1 and DP-1 leads to cooperative activation of an E2F-responsive promoter. Finally, we demonstrate that E2F-1 and DP-1 association is required for stable interaction with pRB in vivo and that trans-activation by E2F-1/DP-1 heterodimers is inhibited by pRB. We suggest that "E2F" is the activity that is formed when an E2F-l-related protein and a DP-l-related protein dimerize.

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“…The AP-1 transcription factor is composed of protein products of the fos and jun gene families, which include c-fos, fra-1, fra-2, fos-B, c-jun, jun-B and jun-D (Bohmann et al, 1987;Chiu et al, 1988;Rauscher et al, 1988). AP-1 has been implicated in the e ects of a number of agents, including serum, peptide growth factors, ultraviolet light and phorbol esters, on cellular growth and di erentiation Curran et al, 1985;Buscher et al, 1988).…”

Section: Introductionmentioning

confidence: 99%

Suppression of c-Fos gene transcription with malignant transformation of human bronchial epithelial cells

et al. 1998

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The Activator Protein-1 (AP-1) complex is a dimeric transcription factor composed of fos and jun proteins that regulates cellular growth and di erentiation. We previously demonstrated a reduction in basal AP-1 transcriptional activity associated with the malignant transformation of human bronchial epithelial (HBE) cells that was, in part, a consequence of decreased c-fos expression. In this study, we investigated the mechanisms underlying the reduction in c-fos expression associated with the malignant transformation of HBE cells. c-Fos gene transcription was lower in tumorigenic HBE cells than in normal HBE cells, and the reduction in transcription involved c-fos gene promoter elements from 7327 to +40. DNaseI footprinting and band shift analyses of motifs within this c-fos promoter region, including a cyclic AMP response element (CRE), serum response element (SRE), sis-inducible element (SIE), and a YY1 site, revealed that binding to these motifs was greater in tumorigenic HBE cells than in normal HBE cells. Site-directed mutagenesis of the CRE partially relieved the repression of c-fos promoter activity in tumorigenic HBE cells. Further, the activity of the Jun N-terminal Kinase (JNK)-dependent pathway, which was a positive regulator of the c-fos promoter, was greater in normal HBE cells than in tumorigenic HBE cells. These ®ndings demonstrate a transcriptionally-mediated suppression of c-fos gene expression associated with the malignant transformation of HBE cells. The decreased activity of the c-fos promoter in tumorigenic 1170I cells appeared to involve suppression through a CRE site and reduced activation by JNK-dependent pathways.

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Fos-Associated Protein p39 Is the Product of the jun Proto-Oncogene

Cited by 636 publications

References 46 publications

c-Jun, at the crossroad of the signaling network

c-Jun, at the crossroad of the signaling network

Heterodimerization of the transcription factors E2F-1 and DP-1 leads to cooperative trans-activation.

Suppression of c-Fos gene transcription with malignant transformation of human bronchial epithelial cells

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