Filamin A organizes γ‑aminobutyric acid type B receptors at the plasma membrane

Marie-Lise Jobin (), Sana Siddig, Zsombor Koszegi, Yann Lanoiselée, Vladimir Khayenko, Titiwat Sungkaworn, Christian Werner, Kerstin Seier, Christin Misigaiski, Giovanna Mantovani, Markus Sauer, Hans M. Maric and Davide Calebiro ()
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Marie-Lise Jobin: University of Würzburg
Sana Siddig: University of Würzburg
Zsombor Koszegi: University of Birmingham
Yann Lanoiselée: University of Birmingham
Vladimir Khayenko: University of Würzburg
Titiwat Sungkaworn: University of Würzburg
Christian Werner: University of Würzburg
Kerstin Seier: University of Würzburg
Christin Misigaiski: University of Würzburg
Giovanna Mantovani: Endocrinology Unit, Fondazione IRCCS Ca’ Granda Ospedale Maggiore Policlinico
Markus Sauer: University of Würzburg
Hans M. Maric: University of Würzburg
Davide Calebiro: University of Würzburg

Nature Communications, 2023, vol. 14, issue 1, 1-14

Abstract: Abstract The γ-aminobutyric acid type B (GABAB) receptor is a prototypical family C G protein-coupled receptor (GPCR) that plays a key role in the regulation of synaptic transmission. Although growing evidence suggests that GPCR signaling in neurons might be highly organized in time and space, limited information is available about the mechanisms controlling the nanoscale organization of GABAB receptors and other GPCRs on the neuronal plasma membrane. Using a combination of biochemical assays in vitro, single-particle tracking, and super-resolution microscopy, we provide evidence that the spatial organization and diffusion of GABAB receptors on the plasma membrane are governed by dynamic interactions with filamin A, which tethers the receptors to sub-cortical actin filaments. We further show that GABAB receptors are located together with filamin A in small nanodomains in hippocampal neurons. These interactions are mediated by the first intracellular loop of the GABAB1 subunit and modulate the kinetics of Gαi protein activation in response to GABA stimulation.

Date: 2023
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DOI: 10.1038/s41467-022-35708-1

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