Abstract
β-arrestins are so-called hub proteins: they make complexes with many different partners, assembling functional complexes, and thereby fulfilling their biological function. The importance of this process in G protein-coupled receptor (GPCR) signalling has been fully demonstrated for many different receptors. For direct interactions, determining the interface regions, on β-arrestins and on the partners, is crucial for understanding the function of the complex. Indeed, this brings information on which proteins can interact simultaneously with β-arrestins, or, on the contrary, which partners are exclusive. We present here a method in two steps: protein–protein docking allows finding a limited number of peptides predicted to be involved in the interaction, and then experimental approaches that might be used for validating the prediction.
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Acknowledgments
This publication was funded with support from the French National Research Agency under the program “Investissements d’avenir” Grant Agreement LabEx MabImprove: ANR-10-LABX-53, ANR (Contract no ANR-2011-1619 01), ANR GPCRnet, MABSILICO, and “ARD2020 Biomédicament” grants from Région Centre (32000593 APR Biomedicament).
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Bourquard, T. et al. (2019). Methods to Determine Interaction Interfaces Between β-Arrestins and Their Protein Partners. In: Scott, M., Laporte, S. (eds) Beta-Arrestins. Methods in Molecular Biology, vol 1957. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-9158-7_12
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DOI: https://doi.org/10.1007/978-1-4939-9158-7_12
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