Design and characterization of allosteric mutations that recapitulate TRPML1 gating and structural insights into PI(4,5)P₂ and sphingomyelin inhibition of TRPML1.

The anchoring properties of Ca_V β2 subunits to the plasma membrane determine the biophysical states of Ca_V2.2 channels by regulating PIP₂ coupling to the nonspecific phospholipid-binding site in the I–II loop.

Dimerization promotes nonlinear kinetics in PIP5K-dependent lipid phosphorylation reactions.

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.

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

A GPCR activated by the same agonist engages different conformational biosensors at different subcellular locations, suggesting that location-based conformations drive spatial encoding of signaling.

In vitro reconstitution of the core focal adhesion proteins talin and vinculin with actin reveals lipid-dependent release of autoinhibition.

The lysosomal ion channel TPC2 emerges as an example of an ion channel in which ion selectivity is not fixed but rather agonist-selective.

A Tubby protein regulates ciliary membrane morphology and phosphoinositide composition in a context-dependent manner.