Phosphorylation of transcription factor p62TCF by MAP kinase stimulates ternary complex formation at c-fos promoter

TRANSCRIPTION of the proto-oncogene c-fos is stimulated rapidly and transiently by serum growth factors and mitogens 1 . Critical for this response is the serum-response element which is bound in vivo in a ternary complex containing the transcription factors p67 SRF and p62 TCF (ref. 2). Disruption...

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Veröffentlicht in:Nature (London) 1992-07, Vol.358 (6385), p.414-417
Hauptverfasser: Gille, Hendrik, Sharrocks, Andrew D., Shaw, Peter E.
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Sprache:eng
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Zusammenfassung:TRANSCRIPTION of the proto-oncogene c-fos is stimulated rapidly and transiently by serum growth factors and mitogens 1 . Critical for this response is the serum-response element which is bound in vivo in a ternary complex containing the transcription factors p67 SRF and p62 TCF (ref. 2). Disruption of the ternary complex correlates with impaired induction by serum and phorbol ester 3,4 . Mitogen-activated protein (MAP) kinase is a serine/ threonine kinase which is activated 1-5 minutes after treatment of cells with mitogens and growth factors 5–8 that induce re-entry into the cell cycle, making MAP kinase a candidate for the transmission of proliferative signals. Here we show that p62 TCF is phosphorylated by MAP kinase in vitro and that phosphorylation results in enhanced ternary complex formation. Serum-starved Swiss 3T3 cells treated with epidermal growth factor, which induces MAP kinase in these cells 9 , are induced to express c- fos and yield p62 TCF active in ternary complex formation. In contrast, treatment of Swiss 3T3 cells with insulin, which does not activate MAP kinase under these conditions 9 , does not lead to enhanced ternary complex formation nor does it induce c- fos transcription. Our results link the expression of the human c-fos proto-oncogene to signal transduction pathways known to be activated before its own induction.
ISSN:0028-0836
1476-4687
DOI:10.1038/358414a0