When challenged by energetic stresses triggered by hypoxia and ATP inhibition, plasma membrane PI4P and PIP2 in cells undergo dramatic turnovers that have profound impact on many cellular processes including electrostatic PM targeting of numerous polybasic proteins.

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

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

β-adrenergic receptors at the Golgi apparatus activate a local signaling pathway, not accessed by cell surface receptors, to drive cardiac hypertrophy and could represent a target for heart failure therapy.

SAC9 prevents the accumulation of PI(4,5)P₂ in intracellular compartments, thereby contributing to clathrin-mediated endocytosis at the plasma membrane and regulating the cortical localization of its protein partner SH3P2.

SAC1 is unable to adopt an efficient "trans" mode of action in living cells.

The synthesis of multiple phosphoinositides function in an ordered pathway to promote recycling of some receptors to the plasma membrane.

The pioneering endocytic protein FCHo2 promotes clathrin-coated structures assembly via the formation of phosphoinositide-enriched domains at the boundary of cargo receptors.

Calcium-binding synaptotagmins are involved in ring oligomer formation, which allows synaptotagmins to synchronize neurotransmitter release to Ca²⁺ influx.