Replacement of the conserved tyrosine 1210 by phenylalanine in the insulin receptor affects insulin-induced dephosphorylation of focal adhesion kinase but leaves other responses intact

Experiments are performed to determine whether tyrosine 1210 contributes to the generation of tyrosine kinase-specific responses and stimulation of DNA synthesis. Tyrosine 1210 in a mutant receptor is replaced by phenylalanine. Results indicate that tyrosine 1210 is not essential for the induction of tyrosine kinase-specific responses, although it is involved in the coupling of the activated of receptor to some downstream targets.