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

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 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.

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

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

PI(4,5)P2 plays a much broader role during the HIV-1 particle assembly process than assumed; it is indispensable not only for recruitment of Gag to the plasma membrane but also for the maintenance of Gag assemblies.

Synergistic interactions with PI(4,5)P2 and activated Rho1, which are enriched at the apical membrane of tubular organs, facilitate tight apical targeting of the formin Diaphanous.

Studies of Lowe syndrome patient cells, which lack the inositol 5-phosphatase OCRL, suggest that a defect in endocytosis plays a role in the pathological manifestations of the disease.

Local Mtmr2 activity and PI(3,5)P2 abundance dynamically control Piezo2-dependent mechanotransduction in peripheral sensory neurons.