Single molecule analysis of functionally asymmetric G protein-coupled receptor (GPCR) oligomers reveals diverse spatial and structural assemblies

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Abstract

Background: GPCRs form complex oligomers whose role in signaling is poorly understood. Results: Super-resolution imaging of functionally asymmetric oligomers reveals diverse functional and structural organizations and the ability to alter signal responses. Conclusion: GPCR oligomers may fine-tune receptor signaling by altering the functional role of individual protomers. Significance: Distinct oligomers could be exploited pharmacologically to improve efficacy, selectivity, and/or specificity.

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Jonas, K. C., Fanelli, F., Huhtaniemi, I. T., & Hanyaloglu, A. C. (2015). Single molecule analysis of functionally asymmetric G protein-coupled receptor (GPCR) oligomers reveals diverse spatial and structural assemblies. Journal of Biological Chemistry, 290(7), 3875–3892. https://doi.org/10.1074/jbc.M114.622498

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