Aug 1, 1989

Biological and biochemical properties of the c-src+ gene product overexpressed in chicken embryo fibroblasts

Molecular and Cellular Biology
J B Levy, J S Brugge

Abstract

The c-src protein isolated from neuronal cells (pp60c-src+) displays a higher level of protein kinase activity than does pp60c-src from nonneural tissues. There are two structural alterations present in the amino-terminal half of pp60c-src+ expressed in neurons which could contribute to the enhanced activity of this form of pp60c-src: (i) a hexapeptide insert located at amino acid 114 of avian pp60c-src+ and (ii) a novel site(s) of serine phosphorylation. We characterized pp60c-src+ expressed in a nonneuronal cell type to identify factors that regulate the activity of the c-src+ protein and the importance of the neuronal environment on this regulation. The c-src+ protein overexpressed in chicken embryo fibroblasts (CEFs) displayed higher kinase activity than did pp60c-src. The major sites of phosphorylation of the c-src+ protein were Ser-17 and Tyr-527. The unique site(s) of serine phosphorylation originally identified in pp60c-src+ expressed in neurons was not detected in the c-src+ protein overexpressed in CEFs. Therefore, the hexapeptide insert is sufficient to cause an elevation in the tyrosine protein kinase activity of pp60c-src+. Our data also indicate that CEFs infected with the Rous sarcoma virus (RSV)c-src+ display ph...Continue Reading

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Mentioned in this Paper

Embryo
SRC gene
Phosphoserine
Specimen Type - Fibroblasts
Entire Embryo
Proteins, Recombinant DNA
Neurons
Brain
Protein Phosphorylation
Proto-Oncogene Protein pp60 (c-src)

About this Paper

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