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The binding of ß-arrestins to agonist-occupied GPCRs coincides with the recruitment of Src family tyrosine kinases, including c-Src, Hck and c-Fgr (Src-TK), to the receptor—ß-arrestin complex. Several signaling events have been reported to involve ß-arrestin-dependent Src recruitment. These include the regulation of clathrin-dependent ß2-adrenergic receptor endocytosis by tyrosine phosphorylation of dynamin, Ras-dependent activation of the ERK1/2 MAP kinase cascade and stimulation of cell proliferation by ß2-adrenergic and neurokinin NK1 receptors, and stimulation of chemokine CXCR1 receptor-mediated neutrophil degranulation |
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Kosi Gramatikoff, PhD |
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Andrew J et al. Physiological Regulation of G Protein-Linked Signaling Physiol Rev, Oct 1999; 79: 1373 - 1430.
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KL Pierce and RJ Lefkowitz. Classical and new roles of beta-arrestins in the regulation of G-protein-coupled receptors. Nat Rev Neurosci, Oct 2001; 2(10): 727-33.
Moritz Bünemann and M. Marlene Hosey. G-protein coupled receptor kinases as modulators of G-protein signaling J. Physiol., May 1999; 517: 5 - 23.
Robert J. Lefkowitz. G Protein-coupled Receptors. III. New roles for receptor kinases and -arrestins in receptor signaling and desensitization. J. Biol. Chem., Jul 1998; 273: 18677 - 18680.
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