Receptor-Arrestin Interactions: The GPCR Perspective
| Autor: | Eugenia V. Gurevich, Vsevolod V. Gurevich, Mohammad Seyedabadi, Mehdi Gharghabi |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
Models
Molecular 0301 basic medicine genetic structures Arrestins Protein Conformation G protein lcsh:QR1-502 Review protein–protein interactions Crystallography X-Ray Biochemistry lcsh:Microbiology Receptors G-Protein-Coupled Protein–protein interaction Binding state Mice 03 medical and health sciences GPCR conformational change 0302 clinical medicine Protein Domains Arrestin Animals Humans Protein Isoforms Phosphorylation Receptor Molecular Biology G protein-coupled receptor Binding Sites Chemistry Fishes eye diseases Cell biology Receptor coupling 030104 developmental biology Mutation Molecular mechanism Cattle sense organs signaling Hydrophobic and Hydrophilic Interactions 030217 neurology & neurosurgery Protein Binding Signal Transduction |
| Zdroj: | Biomolecules Biomolecules, Vol 11, Iss 218, p 218 (2021) |
| ISSN: | 2218-273X |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
| Nepřihlášeným uživatelům se plný text nezobrazuje | K zobrazení výsledku je třeba se přihlásit. |