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

The SHIP2 inositol phosphatase is an important upstream regulator of the Akt signaling pathway, which requires a catalytic core formed by the phosphatase domain tightly packed to a C2 domain for its function.

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

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.

Single particle cryo-electron microscopy associated with functional studies reveal a critical role of N- and C-terminal tails in the autoinhibition of the disease-related ATP8B1-CDC50A lipid flippase, the possible role of phosphorylation in autoinhibition relief, and strong activation by PI(3,4,5)P₃.

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

Electrophysiological and fluorometric studies of Ci-VSP expressed in Xenopus oocyte revealed two states of the enzyme region with distinct enzyme activity and distinct coupling to the voltage sensor.

A step of contact establishment preceding stable membrane attachment by palmitoylation is identified.

In addition to its role in regulating proliferation and cell death, the PTEN tumor suppressor regulates epithelial morphogenesis through the PDK1 kinase.

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