Distinct G protein-coupled receptor phosphorylation motifs modulate arrestin affinity and activation and global conformation
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry
Link
http://www.nature.com/articles/s41467-019-09204-y.pdf
Reference66 articles.
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2. Kuhn, H., Hall, S. W. & Wilden, U. Light-induced binding of 48-kDa protein to photoreceptor membranes is highly enhanced by phosphorylation of rhodopsin. FEBS Lett. 176, 473–478 (1984).
3. Lohse, M. J., Benovic, J. L., Codina, J., Caron, M. G. & Lefkowitz, R. J. beta-Arrestin: a protein that regulates beta-adrenergic receptor function. Science 248, 1547–1550 (1990).
4. Wilden, U., Hall, S. W. & Kuhn, H. Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments. Proc. Natl. Acad. Sci. USA 83, 1174–1178 (1986).
5. Ferguson, S. S. et al. Role of beta-arrestin in mediating agonist-promoted G protein-coupled receptor internalization. Science 271, 363–366 (1996).
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