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In mGlu heterodimers, an oriented asymmetrical activation revealed complex allosteric interaction between subunits.

Differences in the kinetics of G protein activation can explain why only some receptors can activate potassium ion channels called GIRKs.

A critical regulator of inhibitory neurotransmitter signaling in the hippocampus has been identified in experiments on mice and been shown to play essential role in synaptic plasticity and memory.

Maternal CLAMP functions as a novel pioneer transcription factor to open chromatin and plays a targeted yet essential role in Drosophila zygotic genome activation.

Determining how GIRK2 activity depends on the concentration of Gβγ subunits in lipid membranes at different Na⁺ concentrations has allowed the Gβγ concentration generated during GABA_B activation in neurons to be estimated.

Kiss1^ARH neurons transition from synchronous to burst firing under preovulatory levels of E2, causing a shift from peptidergic to glutamatergic transmission that drives the GnRH surge through enhanced glutamate neurotransmission.

The structural role of PIP2 in opening the G-protein-gated K⁺ channel is revealed.

Ligand binding to the ectodomain of the insulin-like growth factor receptor destabilises an autoinhibitory inter-subunit interaction, which allows the transmembrane domains to associate and the intracellular regions to autophosphorylate.

TRPM3 inhibition is identified as a novel mechanism for G-protein βγ subunit signalling.

A unique two-step mechanism of plasma membrane recruitment and activation governs G-protein-coupled receptor mediated PI3K signaling.