β-Arrestin: a protein that regulates β-adrenergic receptor function
Science, 1990•science.org
Homologous or agonist-specific desensitization of β-adrenergic receptors is thought to be
mediated by a specific kinase, the β-adrenergic receptor kinase (βARK). However, recent
data suggest that a cofactor is required for this kinase to inhibit receptor function. The
complementary DNA for such a cofactor was cloned and found to encode a 418-amino acid
protein homologous to the retinal protein arrestin. The protein, termed β-arrestin, was
expressed and partially purified. It inhibited the signaling function of βARK-phosphorylated β …
mediated by a specific kinase, the β-adrenergic receptor kinase (βARK). However, recent
data suggest that a cofactor is required for this kinase to inhibit receptor function. The
complementary DNA for such a cofactor was cloned and found to encode a 418-amino acid
protein homologous to the retinal protein arrestin. The protein, termed β-arrestin, was
expressed and partially purified. It inhibited the signaling function of βARK-phosphorylated β …
Homologous or agonist-specific desensitization of β-adrenergic receptors is thought to be mediated by a specific kinase, the β-adrenergic receptor kinase (βARK). However, recent data suggest that a cofactor is required for this kinase to inhibit receptor function. The complementary DNA for such a cofactor was cloned and found to encode a 418-amino acid protein homologous to the retinal protein arrestin. The protein, termed β-arrestin, was expressed and partially purified. It inhibited the signaling function of βARK-phosphorylated β-adrenergic receptors by more than 75 percent, but not that of rhodopsin. It is proposed that β-arrestin in concert with βARK effects homologous desensitization of β-adrenergic receptors.
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