Increasing PI(4,5)P2 on a sub-second timescale using a novel, membrane-permeant UV activatable PI(4,5)P2 molecule augments exocytosis which requires the PI(4,5)P2 interacting exocytotic proteins Munc13-2 and synaptotagmin-1.

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

Ca²⁺-free synaptotagmin-1 binds to neuronal SNARE complexes anchored on nanodiscs, and Ca²⁺ releases this interaction to induce tight, specific binding to PIP₂-containing membranes.

A novel innate defense mechanism of cell lysis involves the coordinated oligomerization of a defensin by interaction with the membrane lipid, phosphatidylinositol 4,5-bisphosphate.

The local PI(4,5)P₂ nanodomain promotes the dimerization and activation of EGFR in the plasma membrane, whereas activated EGFR dissolves the nanodomain structure of PI(4,5)P₂ through PLCγ.

Combining live imaging and advanced electron microscopy gives insights into the structural integrity of the nematode epidermis and its intimate connection with the extracellular matrix.

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

Cryo-EM structures of human TPC2 channel in the ligand-bound and apo states reveal the structural mechanism of PI(3,5)P₂ lipid regulated gating of TPC2.

The interplay between the Flower Ca²⁺ channel and PI(4,5)P₂ spatiotemporally couples synaptic vesicle exocytosis to activity-dependent bulk endocytosis and synaptic vesicle reformation from bulk endosomes.

The first reconstitution of an unconventional secretory mechanism uncovered the molecular mechanism by which Fibroblast Growth Factor 2 is secreted from mammalian cells.