The c-terminus of PI3K plays a key role in regulating kinase activity, with c-terminal disease-linked mutations leading to either activation or inhibition, which reveal a path to specific inhibitors.

Regulation of phosphoinositide 3 kinase (PI3Kγ) is essential in immune function, and stimuli that modulate the dynamics of the PI3Kγ helical domain can activate or inhibit kinase activity.

Two of the most commonly mutated growth factor pathways induce a deadly feature of lung adenocarcinoma.

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

Paired analysis of gene expression and chromatin accessibility in SOX9+ lung progenitor cells identifies a requirement for PI3K in proximal-distal patterning of the mouse lung epithelium.

PIK3R1 mutations that cause immunodeficiency through PI3-kinase hyperactivation also cause SHORT syndrome, due to PI3-kinase hypofunction, attributable to PI3-kinase destabilisation and outcompetition by mutant PIK3R1.

High PI3K-Akt-mTORC1 activity inhibits Schwann cell differentiation, while after onset of myelination, residual PI3K-Akt-mTORC1 activity promotes myelin growth.

Embryonic PI3K-Yap activity regulates apical adhesion and proliferation of neural progenitors lining the lateral ventricular surface, to maintain the smooth, non-folded mouse brain and to prevent developmental hydrocephalus.

A unique two-step mechanism of plasma membrane recruitment and activation governs G-protein-coupled receptor mediated PI3K signaling.

Akt phosphorylates insulin receptor substrate to engage negative feedback and limit signal propagation.