Upon PDGFRα signaling in mouse embryonic palatal mesenchyme cells, Srsf3 exhibits differential transcript binding, resulting in retention of the receptor in early endosomes and increased downstream PI3K-mediated Akt signaling.

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.

The generation of phosphoinositide 3,4,5-trisphosphate causes an increase in the number of TRPV1 ion channels and insulin receptors in the plasma membrane.

Genetic and proteomic analyses reveal that the SPARK kinase, which is a regulator of key life-cycle transitions in the parasite Toxoplasma gondii, complexes with an elongin-like protein to regulate several important AGC-family kinases.

P-Rex1 adopts an inactive, compact conformation that is stabilized by an abundant intracellular molecule and undergoes dynamic changes to extend upon encountering signaling phospholipids in membranes.

Single molecule reconstitution of PI3Kβ synergistic activation reveals mechanism for rapid PI(3,4,5)P₃ production during immune cell signaling.

Disulfide-bridged fibroblast growth factor 2 (FGF2) dimerization at the inner plasma membrane leaflet produces the building block for higher FGF2 oligomers that drive FGF2 membrane translocation into the extracellular space.

Multiple dynamic protein interactions converge to regulate the catalytic activity of the B cell kinase, BTK.