Ankyrin-B – through interactions with PI3P lipids, dynactin and RabGAP1L – functions as a critical node in the protein circuitry underlying polarized recycling of α5β1-integrin to enable haptotaxis along fibronectin gradients.
β-adrenergic receptors at the Golgi apparatus activate a local signaling pathway, not accessed by cell surface receptors, to drive cardiac hypertrophy and could represent a target for heart failure therapy.
The G protein subunits Gβγ and the signaling lipid PIP2 are simultaneously needed to activate the potassium ion channel GIRK2 to control the voltage across a lipid bilayer, while sodium ions modulate these molecules' effects.
Phosphorylation of ezrin involves an unusual mechanism requiring coincident binding to PIP2 and involvement of the non-catalytic domain to gain access to the phosphorylation site thereby restricting selective phosphorylation to the plasma membrane.
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.