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Triggered Ca2+ influx is required for extended synaptotagmin 1-induced ER-plasma membrane tethering
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology. Yale Univ, Sch Med, Dept Cell Biol, New Haven, CT 06510 USA.;Yale Univ, Sch Med, Howard Hughes Med Inst, New Haven, CT 06510 USA.;Yale Univ, Sch Med, Program Cellular Neurosci Neurodegenerat & Repair, New Haven, CT 06510 USA..
Yale Univ, Sch Med, Dept Cell Biol, New Haven, CT 06510 USA.;Yale Univ, Sch Med, Howard Hughes Med Inst, New Haven, CT 06510 USA.;Yale Univ, Sch Med, Program Cellular Neurosci Neurodegenerat & Repair, New Haven, CT 06510 USA..
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology.
Yale Univ, Sch Med, Dept Cell Biol, New Haven, CT 06510 USA.;Yale Univ, Sch Med, Howard Hughes Med Inst, New Haven, CT 06510 USA.;Yale Univ, Sch Med, Program Cellular Neurosci Neurodegenerat & Repair, New Haven, CT 06510 USA..
2015 (English)In: EMBO Journal, ISSN 0261-4189, E-ISSN 1460-2075, Vol. 34, no 17, 2291-2305 p.Article in journal (Refereed) Published
Abstract [en]

The extended synaptotagmins (E-Syts) are ER proteins that act as Ca2+-regulated tethers between the ER and the plasma membrane (PM) and have a putative role in lipid transport between the two membranes. Ca2+ regulation of their tethering function, as well as the interplay of their different domains in such function, remains poorly understood. By exposing semi-intact cells to buffers of variable Ca2+ concentrations, we found that binding of E-Syt1 to the PI(4,5)P-2-rich PM critically requires its C2C and C2E domains and that the EC50 of such binding is in the low micromolar Ca2+ range. Accordingly, E-Syt1 accumulation at ER-PM contact sites occurred only upon experimental manipulations known to achieve these levels of Ca2+ via its influx from the extracellular medium, such as store-operated Ca2+ entry in fibroblasts and membrane depolarization in -cells. We also show that in spite of their very different physiological functions, membrane tethering by E-Syt1 (ER to PM) and by synaptotagmin (secretory vesicles to PM) undergo a similar regulation by plasma membrane lipids and cytosolic Ca2+.

Place, publisher, year, edition, pages
2015. Vol. 34, no 17, 2291-2305 p.
Keyword [en]
membrane contact sites, Orai1, PLC, STIM1, tricalbin
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
URN: urn:nbn:se:uu:diva-263437DOI: 10.15252/embj.201591565ISI: 000360760800009PubMedID: 26202220OAI: oai:DiVA.org:uu-263437DiVA: diva2:859416
Funder
Swedish Research Council, D0029801NIH (National Institute of Health), NS36251 DK082700 DK45735
Available from: 2015-10-07 Created: 2015-09-30 Last updated: 2017-12-01Bibliographically approved

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Idevall Hagren, OlofXie, Beichen

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