Receptor-Arrestin Interactions: The GPCR Perspective

Arrestins are a small family of four proteins in most vertebrates that bind hundreds of different G protein-coupled receptors (GPCRs). Arrestin binding to a GPCR has at least three functions: precluding further receptor coupling to G proteins, facilitating receptor internalization, and initiating di...

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Bibliographic Details
Published in:Biomolecules (Basel, Switzerland) Switzerland), 2021-02, Vol.11 (2), p.218
Main Authors: Seyedabadi, Mohammad, Gharghabi, Mehdi, Gurevich, Eugenia V, Gurevich, Vsevolod V
Format: Article
Language:English
Subjects:
Arrestin
conformational change
Crystal structure
G protein-coupled receptors
GPCR
Internalization
Molecular modelling
Proteins
protein–protein interactions
Review
signaling
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Summary:Arrestins are a small family of four proteins in most vertebrates that bind hundreds of different G protein-coupled receptors (GPCRs). Arrestin binding to a GPCR has at least three functions: precluding further receptor coupling to G proteins, facilitating receptor internalization, and initiating distinct arrestin-mediated signaling. The molecular mechanism of arrestin-GPCR interactions has been extensively studied and discussed from the "arrestin perspective", focusing on the roles of arrestin elements in receptor binding. Here, we discuss this phenomenon from the "receptor perspective", focusing on the receptor elements involved in arrestin binding and emphasizing existing gaps in our knowledge that need to be filled. It is vitally important to understand the role of receptor elements in arrestin activation and how the interaction of each of these elements with arrestin contributes to the latter's transition to the high-affinity binding state. A more precise knowledge of the molecular mechanisms of arrestin activation is needed to enable the construction of arrestin mutants with desired functional characteristics.
ISSN:2218-273X
2218-273X
DOI:10.3390/biom11020218