A conserved, lipid-mediated sorting mechanism of yeast Ist2 and mammalian STIM proteins to the peripheral ER
Sorting of yeast Ist2 to the plasma membrane (PM) or the cortical endoplasmic reticulum (ER) requires a cortical sorting signal (CSSIst2) that interacts with lipids including phosphatidylinositol-4,5-bisphosphate (PI(4,5)P2) at the PM. Here, we show that the expression of Ist2 in mammalian cells res...
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| Main Authors: | , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
5 October 2009
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| In: |
Traffic
Year: 2009, Volume: 10, Issue: 12, Pages: 1802-1818 |
| ISSN: | 1600-0854 |
| DOI: | 10.1111/j.1600-0854.2009.00995.x |
| Online Access: | Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1111/j.1600-0854.2009.00995.x Verlag, kostenfrei, Volltext: http://onlinelibrary.wiley.com/doi/10.1111/j.1600-0854.2009.00995.x/abstract 
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| Author Notes: | Ebru Ercan, Frank Momburg, Ulrike Engel, Koen Temmerman, Walter Nickel and Matthias Seedorf |
| Summary: | Sorting of yeast Ist2 to the plasma membrane (PM) or the cortical endoplasmic reticulum (ER) requires a cortical sorting signal (CSSIst2) that interacts with lipids including phosphatidylinositol-4,5-bisphosphate (PI(4,5)P2) at the PM. Here, we show that the expression of Ist2 in mammalian cells resulted in a peripheral patch-like localization without any detection of Ist2 at the cell surface. Attached to C-termini of mammalian integral membrane proteins, the CSSIst2 targeted these proteins to PM-associated domains of the ER and abolished trafficking via the classical secretory pathway. The interaction of integral membrane proteins with PI(4,5)P2 at the PM created ER-PM contacts. This process is similar to the regulated coupling of ER domains to the PM via stromal interaction molecule (STIM) proteins during store-operated Ca2+ entry (SOCE). The CSSIst2 and the C-terminus of the ER-located Ca2+ sensor STIM2 were sufficient to bind PI(4,5)P2 and PI(3,4,5)P3 at the PM, showing that an evolutionarily conserved mechanism is involved in the sorting of integral membrane proteins to PM-associated domains of the ER. Yeast Ist2 and STIM2 share a common basic and amphipathic signal at their extreme C-termini. STIM1 showed binding preference for liposomes containing PI(4,5)P2, suggesting a specific contribution of lipids to the recruitment of ER domains to the PM during SOCE. |
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| Item Description: | Gesehen am 22.05.2017 |
| Physical Description: | Online Resource |
| ISSN: | 1600-0854 |
| DOI: | 10.1111/j.1600-0854.2009.00995.x |