
Enzymatically inactive p60c-src mutant with altered ATP-binding site is fully phosphorylated in its carboxy-terminal regulatory region.
Cellular src protein, p60c-src, is phosphorylated on tyrosine 527 in chicken embryo fibroblasts, and this phosphorylation is implicated in suppressing the protein-tyrosine kinase activity and transforming potential of p60c-src. To determine whether tyrosine 527 phosphorylation is dependent on p60c-src kinase activity, the ATP-binding site of chicken p60c-src was destroyed by substitution of lysine 295 with methionine. The resultant protein, p60c-src(M295), expressed either in chicken cells or in yeast, lacked detectable kinase activity. Nevertheless, tyrosine and serine phosphorylation of p60c-src(M295) overproduced in chicken cells were indistinguishable from that of authentic p60c-src. By contrast, p60c-src(M295) was not phosphorylated on tyrosine in yeast. These results suggest that a protein kinase present in chicken cells but not in yeast phosphorylates tyrosine 527 in trans, and are consistent with the possibility that this kinase is distinct from p60c-src.
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Related Subject Headings
- Tyrosine
- Saccharomyces cerevisiae
- Recombinant Proteins
- Proto-Oncogene Proteins pp60(c-src)
- Proto-Oncogene Proteins
- Protein-Tyrosine Kinases
- Protein Kinases
- Phosphotyrosine
- Phosphorylation
- Fibroblasts
Citation

Published In
DOI
EISSN
ISSN
Publication Date
Volume
Issue
Start / End Page
Related Subject Headings
- Tyrosine
- Saccharomyces cerevisiae
- Recombinant Proteins
- Proto-Oncogene Proteins pp60(c-src)
- Proto-Oncogene Proteins
- Protein-Tyrosine Kinases
- Protein Kinases
- Phosphotyrosine
- Phosphorylation
- Fibroblasts