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• W2329177125 abstract "Endoplasmic reticulum–plasma membrane (ER–PM) contact sites play an integral role in cellular processes such as excitation–contraction coupling and store-operated calcium entry (SOCE). Another ER–PM assembly is one tethered by the extended synaptotagmins (E-Syt). We have discovered that at steady state, E-Syt2 positions the ER and Sac1, an integral ER membrane lipid phosphatase, in discrete ER–PM junctions. Here, Sac1 participates in phosphoinositide homeostasis by limiting PM phosphatidylinositol 4-phosphate (PI(4)P), the precursor of PI(4,5)P2. Activation of G protein–coupled receptors that deplete PM PI(4,5)P2 disrupts E-Syt2–mediated ER–PM junctions, reducing Sac1’s access to the PM and permitting PM PI(4)P and PI(4,5)P2 to recover. Conversely, depletion of ER luminal calcium and subsequent activation of SOCE increases the amount of Sac1 in contact with the PM, depleting PM PI(4)P. Thus, the dynamic presence of Sac1 at ER–PM contact sites allows it to act as a cellular sensor and controller of PM phosphoinositides, thereby influencing many PM processes." @default.
• W2329177125 created "2016-06-24" @default.
• W2329177125 creator A5029129147 @default.
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• W2329177125 date "2016-04-04" @default.
• W2329177125 modified "2023-10-14" @default.
• W2329177125 title "Dynamic formation of ER–PM junctions presents a lipid phosphatase to regulate phosphoinositides" @default.
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• W2329177125 doi "https://doi.org/10.1083/jcb.201508106" @default.
• W2329177125 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4828688" @default.
• W2329177125 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27044890" @default.
• W2329177125 hasPublicationYear "2016" @default.
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