| Autor: |
Karoor, Vijaya, Baltensperger, Kurt, Paul, Hyacinth, Czech, Michael P., Malbon, Craig C. |
| Zdroj: |
Journal of Biological Chemistry; October 1995, Vol. 270 Issue: 43 p25305-25308, 4p |
| Abstrakt: |
Insulin stimulates a loss of function and increased phosphotyrosine content of the β2-adrenergic receptor in intact cells, raising the possibility that the β2-receptor itself is a substrate for the insulin receptor tyrosine kinase. Phosphorylation of synthetic peptides corresponding to cytoplasmic domains of the β2-adrenergic receptor by the insulin receptor in vitroand peptide mapping of the β2-adrenergic receptor phosphorylated in vivoin cells stimulated by insulin reveal tyrosyl residues 350/354 and 364 in the cytoplasmic, C-terminal region of the β2-adrenergic receptor as primary targets. Mutation of tyrosyl residues 350, 354 (double mutation) to phenylalanine abolishes the ability of insulin to counterregulate β-agonist stimulation of cyclic AMP accumulation. Phenylalanine substitution of tyrosyl reside 364, in contrast, abolishes β-adrenergic stimulation itself. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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