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Int. J. Mol. Sci. 2017, 18(1), 27; doi:10.3390/ijms18010027

Novel Structural Approaches to Study GPCR Regulation

Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, Ciudad Universitaria, Ciudad de México 04510, Mexico
Author to whom correspondence should be addressed.
Academic Editor: Kathleen Van Craenenbroeck
Received: 4 November 2016 / Revised: 15 December 2016 / Accepted: 21 December 2016 / Published: 23 December 2016
(This article belongs to the Collection G Protein-Coupled Receptor Signaling and Regulation)
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Background: Upon natural agonist or pharmacological stimulation, G protein-coupled receptors (GPCRs) are subjected to posttranslational modifications, such as phosphorylation and ubiquitination. These posttranslational modifications allow protein–protein interactions that turn off and/or switch receptor signaling as well as trigger receptor internalization, recycling or degradation, among other responses. Characterization of these processes is essential to unravel the function and regulation of GPCR. Methods: In silico analysis and methods such as mass spectrometry have emerged as novel powerful tools. Both approaches have allowed proteomic studies to detect not only GPCR posttranslational modifications and receptor association with other signaling macromolecules but also to assess receptor conformational dynamics after ligand (agonist/antagonist) association. Results: this review aims to provide insights into some of these methodologies and to highlight how their use is enhancing our comprehension of GPCR function. We present an overview using data from different laboratories (including our own), particularly focusing on free fatty acid receptor 4 (FFA4) (previously known as GPR120) and α1A- and α1D-adrenergic receptors. From our perspective, these studies contribute to the understanding of GPCR regulation and will help to design better therapeutic agents. View Full-Text
Keywords: G protein-coupled receptors (GPCRs); posttranslational modifications; phosphorylation; ubiquitination; mass spectrometry (MS); GPR120; FFA4; α1-adrenoceptors; protein–protein interactions G protein-coupled receptors (GPCRs); posttranslational modifications; phosphorylation; ubiquitination; mass spectrometry (MS); GPR120; FFA4; α1-adrenoceptors; protein–protein interactions
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Alfonzo-Méndez, M.A.; Alcántara-Hernández, R.; García-Sáinz, J.A. Novel Structural Approaches to Study GPCR Regulation. Int. J. Mol. Sci. 2017, 18, 27.

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