Dec 13, 2005

The differential engagement of arrestin surface charges by the various functional forms of the receptor

The Journal of Biological Chemistry
Susan M Hanson, Vsevolod V Gurevich

Abstract

G-protein-coupled receptor signaling is terminated by arrestin proteins that preferentially bind to the activated phosphorylated form of the receptor. Arrestins also bind active unphosphorylated and inactive phosphorylated receptors. Binding to the non-preferred forms of the receptor is important for visual arrestin translocation in rod photoreceptors and the regulation of receptor signaling and trafficking by non-visual arrestins. Given the importance of arrestin interactions with the various functional forms of the receptor, we performed an extensive analysis of the receptor-binding surface of arrestin using site-directed mutagenesis. The data indicated that a large number of surface charges are important for arrestin interaction with all forms of the receptor. Arrestin elements involved in receptor binding are differentially engaged by the various functional forms of the receptor, each requiring a unique subset of arrestin residues in a specific spatial configuration. We identified several additional phosphate-binding elements in the N-domain and demonstrated for the first time that the active receptor preferentially engages the arrestin C-domain. We also found that the interdomain contact surface is important for arrestin i...Continue Reading

Mentioned in this Paper

Rhodopsin
G-Protein-Coupled Receptors
Transcription, Genetic
Mutagenesis, Site-Directed
Tertiary Protein Structure
Phosphate Measurement
Trafficking
Protein Biosynthesis
Plasma Protein Binding Capacity
Arrestin

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