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Oncogenic and transcriptional cooperation with Ha-Ras requires phosphorylation of c-Jun on serines 63 and 73
Abstract
Recent advances indicate a link between tumour promoters, transformation, and AP-1 activity. Protein kinase C activation increases AP-1 DNA-binding activity independently of new protein synthesis. AP-1 is also stimulated by transforming oncoproteins and growth factors. These proteins are thought to participate in a signalling cascade affecting the nuclear AP-1 complex composed of the Jun and Fos proteins. Because c-Jun is the most potent transactivator in the AP-1 complex and is elevated in Ha-ras-transformed cells, in which c-Fos is downregulated, we focused on it as a potential target. c-Jun could convert input from an oncogenic signalling cascade into changes in gene expression. Indeed, transformation of rat embryo fibroblasts by c-Jun requires an intact transcriptional activation domain and cooperation with oncogenic Ha-ras. Expression of oncogenic Ha-ras augments transactivation by c-Jun and stimulates its phosphorylation. Here we describe the mapping of the Ha-ras-responsive phosphorylation sites to serines 63 and 73 of c-Jun. Site-directed mutagenesis indicates that phosphorylation of these serines is essential for stimulation of c-Jun activity and for cooperation with Ha-ras in ocogenic transformation.
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“The transcriptional activity of c-Jun is increased following phosphorylation on Ser-63 and -73 by JNK (34,46).”
From c-Jun Is a JNK-independent Coactivator of the PU.1 Transcription Factor (1999) · cites this paper as [34]
In the citing paper
“Usually, the transcriptional activity of c-Jun is increased following phosphorylation on Ser-63 and -73 by JNK (34,46).”
From c-Jun Is a JNK-independent Coactivator of the PU.1 Transcription Factor (1999) · cites this paper as [34]
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Metadata
- Authors
- Smeal, T., Binetruy, B., Mercola, D. A., Birrer, M., & Karin, M.
- Affiliations
- University of California San Diego (US)
- National Institutes of Health (US)
- Venue
- Nature
- Published
- 1991-12
- Volume
- 354
- Issue
- 6353
- Pages
- 494-496
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2042260090
- Cited by
- 789
- References
- 23
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 7 · 2023: 3 · 2022: 4 · 2021: 11 · 2020: 11 · 2019: 12 · 2018: 9 · 2017: 7 · 2016: 10 · 2015: 8 · 2014: 12 · 2013: 21 · 2012: 12
- FWCI
- 15.61
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Melanoma and MAPK Pathways
- Keywords
- c-Jun, Ha-ras, AP-1 transcription factor, oncogenic transformation, transactivation domain, c-fos, protein kinase C, oncogene cooperation, rat embryo fibroblasts, tumor promoters
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Cell Transformation, Neoplastic, Molecular Sequence Data, Phosphorylation, Serine, Transcription, Genetic, Transcriptional Activation, Oncogene Protein p21(ras), Gene Expression Regulation, Neoplastic, Mutagenesis, Site-Directed, 3T3 Cells, Proto-Oncogene Proteins c-jun, Mice, Rats
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