PALMITOYLATION OF THE HUMAN BETA-2-ADRENERGIC RECEPTOR - MUTATION OF CYS-341 IN THE CARBOXYL TAIL LEADS TO AN UNCOUPLED NONPALYMITOYLATED FORM OF THE RECEPTOR

  • 5 May 1989
    • journal article
    • research article
    • Vol. 264  (13) , 7564-7569
Abstract
We report that a cysteine residue in the human .beta.2-adrenergic receptor (.beta.2AR) is covalently modified by thioesterification with palmitic acid. By site-directed mutagenesis of the receptor, we have identified Cys341 in the carboxy tail of the protein as the most likely site of palmitolylation. Mutation of Cys341 to glycine results in a nonpalmitoylated form of the receptor that exhibits a drastically reduced ability to mediate isoproterenol stimulation of adenylyl cyclase. The functional impairment of this mutated .beta.2AR is also reflected in a markedly reduced ability to form a guanyl nucleotide-sensitive high affinity state for agonists, characteristic of wild-type receptor. These results indicate that post-translational modification by palmitate of .beta.2AR may play a crucial role in the normal coupling of the receptor to the adenylyl cyclase signal transduction system.

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