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β-Arrestin: a Protein that Regulates β-adrenergic Receptor Function
Abstract
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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Metadata
- Authors
- Lohse, M. J., Benovic, J. L., Codina, J., Caron, M. G., & Lefkowitz, R. J.
- Venue
- Science
- Published
- 1990-06-22
- Volume
- 248
- Issue
- 4962
- Pages
- 1547-1550
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2060207881
- Cited by
- 1,220
- References
- 0
- FWCI
- 18.91
- Type
- journal article
- Language
- en
- Open access
- closed
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- Lohse, M. J., Benovic, J. L., Codina, J., Caron, M. G., & Lefkowitz, R. J. (1990). β-Arrestin: a Protein that Regulates β-adrenergic Receptor Function. Science. https://doi.org/10.1126/science.2163110
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