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Activation Mechanism and Allosteric Properties of the GABAB Receptor

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GABAB Receptor

Part of the book series: The Receptors ((REC,volume 29))

Abstract

The GABAB receptor is quite original within the large G protein-coupled receptor (GPCR) family. When first identified at the molecular level, it was the only GPCR to require two subunits to form a functional receptor, composed of GABAB1 and GABAB2. Although part of the mandatory dimeric class C group of GPCRs that also includes the receptors activated by glutamate, calcium, the sweet and umami taste compounds, the GABAB is unique in that it lacks an essential element, the cysteine-rich domain that interconnects the ligand binding domain to the heptahelical transmembrane domain (7TM) responsible for G protein activation. Here, we will summarize our actual knowledge on the structure, stoichiometry, allosteric properties, and activation mechanism. These reveal some similarities and major differences with the other class C GPCRs and highlight novel possibilities to develop approaches to regulate its activity.

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Authors and Affiliations

  1. Institut de Genomique Fonctionnelle, Universite de Montpellier, CNRS UMR5203, 34094, Montpellier, France

    Julie Kniazeff, Xavier Rovira, Philippe Rondard & Jean-Philippe Pin

  2. INSERM U1191, 34094, Montpellier, France

    Julie Kniazeff, Xavier Rovira, Philippe Rondard & Jean-Philippe Pin

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  1. Julie Kniazeff
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  2. Xavier Rovira
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  3. Philippe Rondard
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  4. Jean-Philippe Pin
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Correspondence to Jean-Philippe Pin .

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Editors and Affiliations

  1. Neuroscience Institute, National Research Council of Italy Neuroscience Institute, Cagliari, Italy

    Giancarlo Colombo

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Kniazeff, J., Rovira, X., Rondard, P., Pin, JP. (2016). Activation Mechanism and Allosteric Properties of the GABAB Receptor. In: Colombo, G. (eds) GABAB Receptor. The Receptors, vol 29. Humana Press, Cham. https://doi.org/10.1007/978-3-319-46044-4_6

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