Desensitization of N-formylpeptide receptor-mediated activation is dependent upon receptor phosphorylation.

The Journal of Biological Chemistry
E R Prossnitz

Abstract

The human N-formylpeptide receptor (FPR) represents one of the most thoroughly studied leukocyte chemoattractant receptors. Despite this, little is known about the molecular mechanisms involved in the activation and desensitization of this receptor. To assess the role of phosphorylation in receptor function, U937 promonocytic cells were stably transfected to express the recombinant human FPR. Three mutant forms of the FPR lacking specific serine and threonine residues in the receptor C terminus were studied with respect to activation and desensitization. Replacement of all 11 serine and threonine residues within the C terminus by alanine and glycine residues (DeltaST) resulted in a receptor capable of ligand binding and G protein activation similar to the wild-type receptor. However, whereas the wild-type FPR was phosphorylated on both serine and threonine residues upon exposure to agonist and displayed a significantly reduced ability to stimulate G protein-mediated GTP hydrolysis upon subsequent exposure to agonist, DeltaST demonstrated a complete lack of phosphorylation and displayed little alteration in its ability to stimulate G protein-mediated GTP hydrolysis upon a subsequent exposure to agonist. In addition to desensitiz...Continue Reading

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