{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Collins MD"],"funding":["NEI NIH HHS","NCRR NIH HHS","NIGMS NIH HHS"],"pagination":["2485-94"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3853087"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["105(11)"],"pubmed_abstract":["Phosphoinositides are vital for many cellular signaling processes, and therefore a number of approaches to manipulating phosphoinositide levels in cells or excised patches of cell membranes have been developed. Among the most common is the use of \"short-chain\" phosphoinositides, usually dioctanoyl phosphoinositol phosphates. We use isothermal titration calorimetry to determine partitioning of the most abundant phosphoinositol phosphates, PI(4)P and PI(4,5)P2 into models of the intracellular and extracellular facing leaflets of neuronal plasma membranes. We show that phosphoinositide mole fractions in the lipid membrane reach physiological levels at equilibrium with reasonable solution concentrations. Finally we explore the consequences of our results for cellular electrophysiology. In particular, we find that TRPV1 is more selective for PI(4,5)P2 than PI(4)P and activated by extremely low membrane mole fractions of PIPs. We conclude by discussing how the logic of our work extends to other experiments with short-chain phosphoinositides. For delayed rectifier K(+) channels, consideration of the membrane mole fraction of PI(4,5)P2 lipids with different acyl chain lengths suggests a different mechanism for PI(4,5)P2 regulation than previously proposed. Inward rectifier K(+) channels apparent lack of selectivity for certain short-chain PIPs may require reinterpretation in view of the PIPs different membrane partitioning."],"journal":["Biophysical journal"],"pubmed_title":["Short-chain phosphoinositide partitioning into plasma membrane models."],"pmcid":["PMC3853087"],"funding_grant_id":["R01 GM100718","R01EY017564","S10 RR025429","R01 EY013007","R01 EY017564","R01GM100718"],"pubmed_authors":["Collins MD","Gordon SE"],"additional_accession":[]},"is_claimable":false,"name":"Short-chain phosphoinositide partitioning into plasma membrane models.","description":"Phosphoinositides are vital for many cellular signaling processes, and therefore a number of approaches to manipulating phosphoinositide levels in cells or excised patches of cell membranes have been developed. Among the most common is the use of \"short-chain\" phosphoinositides, usually dioctanoyl phosphoinositol phosphates. We use isothermal titration calorimetry to determine partitioning of the most abundant phosphoinositol phosphates, PI(4)P and PI(4,5)P2 into models of the intracellular and extracellular facing leaflets of neuronal plasma membranes. We show that phosphoinositide mole fractions in the lipid membrane reach physiological levels at equilibrium with reasonable solution concentrations. Finally we explore the consequences of our results for cellular electrophysiology. In particular, we find that TRPV1 is more selective for PI(4,5)P2 than PI(4)P and activated by extremely low membrane mole fractions of PIPs. We conclude by discussing how the logic of our work extends to other experiments with short-chain phosphoinositides. For delayed rectifier K(+) channels, consideration of the membrane mole fraction of PI(4,5)P2 lipids with different acyl chain lengths suggests a different mechanism for PI(4,5)P2 regulation than previously proposed. Inward rectifier K(+) channels apparent lack of selectivity for certain short-chain PIPs may require reinterpretation in view of the PIPs different membrane partitioning.","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Dec","modification":"2025-04-22T16:27:58.871Z","creation":"2019-03-27T03:09:52Z"},"accession":"S-EPMC3853087","cross_references":{"pubmed":["24314079"],"doi":["10.1016/j.bpj.2013.09.035"]}}