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Arrestins - Pharmacology and Therapeutic Potential by Eugenia V. Gurevich, Vsevolod V. Gurevich (auth.), Vsevolod

By Eugenia V. Gurevich, Vsevolod V. Gurevich (auth.), Vsevolod V. Gurevich (eds.)

This quantity describes our present knowing of the organic function of visible and non-visual arrestins in numerous cells and tissues, concentrating on the mechanisms of arrestin-mediated legislation of GPCRs and non-receptor signaling proteins in overall healthiness and sickness. The publication covers wide variety of arrestin services, emphasizing healing strength of concentrating on arrestin interactions with person partners.

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Since GRK-mediated phosphorylation of receptors is relatively slow, it often dominates the kinetics of β-arrestin binding to receptors in intact cells. The recognition of phosphorylated receptors by β-arrestins is more complex than in the visual system, because of the diversity of recognition sites both in terms of the active conformation and of the phosphorylation. J. Lohse and C. Hoffmann β-arrestin docking site. This is a problem that has so far not been solved—neither for the β-arrestins nor for G proteins.

2008; Lohse and Klenk 2008). And finally, further adapters, such as the sodium/protein exchanger regulatory factor, NHERF1, may regulate the binding of β-arrestins to receptors (Wheeler et al. 2007; Klenk et al. 2010). 3 Nonclassical Signaling Pathways Internalization of receptors does not only remove them from the cell surface and target them to either recycling or degradation, it also triggers new signaling pathways (see chapters “Arrestin-Dependent Activation of ERK and Src Family Kinases,” “Arrestin-Dependent Activation of JNK Family Kinases,” and “ArrestinMediated Activation of p38 MAPK: Molecular Mechanisms and Behavioral Consequences”).

2012b). These data show that the relative position of the N- and C-domains remains largely unchanged, which contradicts the model of a large, “clamshell”-like conformational change. In addition, a number of movements were observed around the polar core, notably of the “finger loop” (amino acids 67–79) and unexpectedly of a loop containing residue 139. The latter movement was subsequently confirmed in mutagenesis experiments (Vishnivetskiy et al. 2013). Several mutants in this loop showed a loss in selectivity for the phosphorylated, activated form of rhodopsin, indicating that the 139-loop stabilizes the inactive conformation of arrestin and reduces its binding to non-preferred forms of rhodopsin.

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