c-Jun is phosphorylated by the DNA-dependent protein kinase in vitro; definition of the minimal kinase recognition motif.

The DNA-dependent protein kinase (DNA-PK) phosphorylates a number of transcription factors. Here, we show that the DNA-PK modifies c-Jun in vitro and that serine residue 249 (Ser-249) is required for phosphorylation to occur. This residue corresponds to one of three sites of c-Jun that are phosphorylated in vivo and which ...
negatively regulate c-Jun DNA binding in vitro. However, we find that phosphorylation of c-Jun by the DNA-PK does not interfere with DNA binding, indicating that phosphorylation at other sites is required for this effect. Mutagenesis of the phosphorylated region of c-Jun reveals that the primary amino acid sequence recognised by the DNA-PK consists of the sequence Ser-Gln, and that adjacent acidic residues potentiate kinase activity. Furthermore, when this site is placed within the context of a second protein, it confers DNA-PK directed phosphorylation upon that protein. Our findings will facilitate identification of DNA-PK phosphorylation sites in other transcription factors.
Mesh Terms:
Amino Acid Sequence, Binding Sites, DNA, DNA-Activated Protein Kinase, DNA-Binding Proteins, HeLa Cells, Humans, Molecular Sequence Data, Mutagenesis, Site-Directed, Nuclear Proteins, Phosphorylation, Protein-Serine-Threonine Kinases, Proto-Oncogene Proteins c-jun, Substrate Specificity
Nucleic Acids Res.
Date: Mar. 11, 1993
Download Curated Data For This Publication
151180
Switch View:
  • Interactions 1