期刊
EMBO JOURNAL
卷 34, 期 17, 页码 2291-2305出版社
WILEY-BLACKWELL
DOI: 10.15252/embj.201591565
关键词
membrane contact sites; Orai1; PLC; STIM1; tricalbin
资金
- Swedish Research Council [D0029801]
- Goran Gustafsson foundation
- NIH [NS36251, DK082700, DK45735]
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+.
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