Gerald R.V. Hammond

TL;DR: Depletion of both lipids was required to prevent PM targeting of proteins that interact with acidic lipids or activation of the transient receptor potential vanilloid 1 cation channel, and PI4P contributes to the pool of polyanionic lipids that define plasma membrane identity and to some functions previously attributed specifically to PI(4,5)P2, which may be fulfilled by a more generalpolyanionic lipid requirement.

TL;DR: Characterization of a new biosensor for PtdIns4P reveals a wider cellular distribution for the polyphosphoinositide than the Golgi localization reported previously, including pools in both the plasma membrane and late endosomes/lysosomes.

TL;DR: Specific conditions that enable preservation of several organellar membranes for the immunocytochemical detection of PtdIns4P are defined and evidence that the majority of this lipid resides in the plasma membrane is presented, where it is metabolically distinct from the steady-state plasma membrane pool of PTDIns(4,5)P2.

TL;DR: This review discusses current knowledge of the principle types of PPIn-protein interactions, focusing on specific lipid-binding domains, and describes how these domains have been re-tasked by biologists as molecular probes for these lipids in living cells.

TL;DR: Regulation of the ORP5/8 attachment to the PM by both phosphoinositides provides a powerful means to determine the relative flux of PI4P toward the ER for PS transport and Sac1-mediated dephosphorylation and PIP 5-kinase–mediated conversion to PI(4,5)P2.