A closer look at presynaptic GABAB receptors

Lewis, Sian

doi:10.1038/nrn2925

Research Highlight
Published: 15 September 2010

Synaptic transmission

A closer look at presynaptic GABA_B receptors

Sian Lewis

Nature Reviews Neuroscience volume 11, page 665 (2010)Cite this article

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GABA_B receptors are heterodimers, consisting of a GB1 and a GB2 subunit. To investigate whether the receptors are activated in the absence of neuronal firing, the authors blocked spike-dependent activity with tetrodotoxin and measured GB1–GB2 dimerization through fluorescence resonance energy transfer (FRET) between fluorescently tagged subunits. They showed that receptor dimerization occurred under such basal conditions, and to a variable degree at individual boutons along a single axon.

The intersynapse variability was not observed at non-functional boutons lacking synaptic vesicle release, suggesting that it is not an intrinsic property of the GABA_B receptor. Conversely, heterogeneity of the FRET signal was reduced by pharmacologically inhibiting the GABA_B receptor or by maximally activating the receptor with a saturating dose of the GABA_B agonist baclofen. Local variations in GABA levels therefore seem to underlie the heterogeneity of GABA_B receptor activation across hippocampal boutons.

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ORIGINAL RESEARCH PAPER

Laviv, T. et al. Basal GABA regulates GABABR conformation and release probability at single hippocampal synapses. Neuron 67, 253–267 (2010)
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