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. 1996 Mar 19;93(6):2387–2391. doi: 10.1073/pnas.93.6.2387

p140/c-Abl that binds DNA is preferentially phosphorylated at tyrosine residues.

R Dikstein 1, R Agami 1, D Heffetz 1, Y Shaul 1
PMCID: PMC39806  PMID: 8637883

Abstract

EP is a DNA element found in the enhancer and promoter regions of several cellular and viral genes. Previously, we have identified the DNA binding p140/c-Abl protein that specifically recognizes this element. Here we show that phosphorylation is essential for the p140/c-Abl DNA binding activity and for the formation of DNA-protein complexes. Furthermore, by 32P labeling of cells and protein purification, we demonstrate that in vivo the EP-DNA-associated p140/c-Abl is a tyrosine phosphoprotein. By employing two different c-Abl antibodies, we demonstrate the existence of two distinct c-Abl populations in cellular extracts. p140/c-Abl is quantitatively the minor population, is heavily phosphorylated at both serine and tyrosine residues, and is active in autophosphorylation reactions.

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Selected References

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