PIP₂ inhibits the proton-activated chloride (PAC) channel by selectively stabilizing its desensitized state.

Molecular, biophysical, and computational analysis reveals insights on the mechanism of association of birnavirus VP3 with endosomes and its role in the viral life cycle, representing a substantial contribution toward understanding the replication strategy of these 'non-canonical' viruses.

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

Simulations reveal where phosphoinositide lipids bind to voltage-gated sodium channels and how they reduce channel activity.

DCX negatively regulates dynein-mediated retrograde transport through two critical interactions by regulating dynein binding to microtubules and regulating the composition of dynein/dyactin/JIP3 motor complex.

Plasma membrane clusters of the Parkinson's disease protein α-synuclein colocalize with negatively charged phospholipids involved in endocytosis and exocytosis.

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.

Ankyrin-B – through interactions with PI3P lipids, dynactin and RabGAP1L – functions as a critical node in the protein circuitry underlying polarized recycling of α5β1-integrin to enable haptotaxis along fibronectin gradients.

A dual-color TIRFM study reveals a new form of inflammatory regulation, in which a lipid kinase and ion channel reciprocally regulate each other to amplify the response to painful stimuli.

TRPV4 channels in brain capillaries are suppressed by the phosphoinositide PIP2 and activated by receptor agonists implicated in neurovascular coupling.