The GIRK1 subunit contains a defective Na+-binding site but behaves as if it is permanently bound to a sodium ion, and therefore increases the affinity of Gβγ to GIRK1/4 hetero-tetrameric channels in lipid membranes.
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 GABAB activation in neurons to be estimated.
The G protein subunits Gβγ and the signaling lipid PIP2 are simultaneously needed to activate the potassium ion channel GIRK2 to control the voltage across a lipid bilayer, while sodium ions modulate these molecules' effects.
A computational model of the thalamocortical network explains sleep stages by the coordinated variations in the level of neuromodulators and predicts differences of sleep pattern in human, cat and mouse recordings.
How nuclear pore complexes establish their permeability barrier has been a long-standing question; now, this process can be reconstituted by a surprisingly simple and rapid self-assembly of Nup98 FG domains into selective FG phases.