Phosphorylation of the solubilized insulin receptor by the gene product of the Rous sarcoma virus, pp60src

✍ Scribed by Morris F. White; C. Ronald Kahn; Diane K. Werth; Ira Pastan

• Book ID: 102878519
• Publisher: John Wiley and Sons
• Year: 1984
• Tongue: English
• Weight: 720 KB
• Volume: 26
• Category: Article
• ISSN: 0730-2312
• DOI: 10.1002/jcb.240260305

✦ Synopsis

Both the insulin receptor and the gene product of the Rous sarcoma virus, pp60Src, are protein kinases which phosphorylate themselves and other proteins on tyrosine residues. Addition of the solubilized insulin receptor to purified pp6OSrC increased the phosphorylation of the &subunit of the insulin receptor. Phosphorylation of the insulin receptor by pp60src occurred both in the absence and presence of insulin but did not alter the insulin dose response for autophosphorylation of the receptor. Increasing concentrations of pp6OSrc increased the phosphorylation of the receptor and at high concentrations equaled the maximal effect produced by insulin. Our observations suggest a possible mechanism by which the metabolically regulated insulin receptor tyrosine kinase could be altered by other tyrosine kinases such as that associated with pp6OSrc. Further studies will be required to determine if the insulin receptor is phosphorylated by pp6OSrc in Rous sarcoma virus-infected cells.