Article
Phosphorylation of Src mutants at Tyr 527 in fibroblasts does not correlate with in vitro phosphorylation by CSK.
Oncogene - 1 Jan 1993
MacAuley A, Okada M, Nada S, Nakagawa H, Cooper J A
Abstract excerpt
In normal fibroblasts, the product of the cellular src gene, p60c-src or Src, is repressed by phosphorylation at its C-terminal tyrosine residue, Tyr 527. Mutations in Src that prevent phosphorylation cause enzymatic activation and malignant transformation. The tyrosine kinases that phosphorylate Src at Tyr 527 in vivo have not been identified, but a tyrosine kinase known as CSK is an excellent candidate. CSK has...
Topics
- Amino Acid Sequence
- Cells, Cultured
- Fibroblasts
- Molecular Sequence Data
- Mutation
- Peptide Mapping
- Phosphorylation
- Protein-Tyrosine Kinases
- Proto-Oncogene Proteins pp60(c-src)
- Tyrosine