Ca2+ store depletion causes STIM1 to accumulate in ER regions closely associated with the plasma membrane
Stromal interacting molecule 1 (STIM1), reported to be an endoplasmic reticulum (ER) Ca2+ sensor controlling store-operated Ca2+ entry, redistributes from a diffuse ER localization into puncta at the cell periphery after store depletion. STIM1 redistribution is proposed to be necessary for Ca2+ rele...
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The Rockefeller University Press
2006
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2064335/ |
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pubmed-20643352007-11-29 Ca2+ store depletion causes STIM1 to accumulate in ER regions closely associated with the plasma membrane Wu, Minnie M. Buchanan, JoAnn Luik, Riina M. Lewis, Richard S. Research Articles Stromal interacting molecule 1 (STIM1), reported to be an endoplasmic reticulum (ER) Ca2+ sensor controlling store-operated Ca2+ entry, redistributes from a diffuse ER localization into puncta at the cell periphery after store depletion. STIM1 redistribution is proposed to be necessary for Ca2+ release–activated Ca2+ (CRAC) channel activation, but it is unclear whether redistribution is rapid enough to play a causal role. Furthermore, the location of STIM1 puncta is uncertain, with recent reports supporting retention in the ER as well as insertion into the plasma membrane (PM). Using total internal reflection fluorescence (TIRF) microscopy and patch-clamp recording from single Jurkat cells, we show that STIM1 puncta form several seconds before CRAC channels open, supporting a causal role in channel activation. Fluorescence quenching and electron microscopy analysis reveal that puncta correspond to STIM1 accumulation in discrete subregions of junctional ER located 10–25 nm from the PM, without detectable insertion of STIM1 into the PM. Roughly one third of these ER–PM contacts form in response to store depletion. These studies identify an ER structure underlying store-operated Ca2+ entry, whose extreme proximity to the PM may enable STIM1 to interact with CRAC channels or associated proteins. The Rockefeller University Press 2006-09-11 /pmc/articles/PMC2064335/ /pubmed/16966422 http://dx.doi.org/10.1083/jcb.200604014 Text en Copyright © 2006, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Wu, Minnie M. Buchanan, JoAnn Luik, Riina M. Lewis, Richard S. |
| spellingShingle |
Wu, Minnie M. Buchanan, JoAnn Luik, Riina M. Lewis, Richard S. Ca2+ store depletion causes STIM1 to accumulate in ER regions closely associated with the plasma membrane |
| author_facet |
Wu, Minnie M. Buchanan, JoAnn Luik, Riina M. Lewis, Richard S. |
| author_sort |
Wu, Minnie M. |
| title |
Ca2+ store depletion causes STIM1 to accumulate in ER regions closely associated with the plasma membrane |
| title_short |
Ca2+ store depletion causes STIM1 to accumulate in ER regions closely associated with the plasma membrane |
| title_full |
Ca2+ store depletion causes STIM1 to accumulate in ER regions closely associated with the plasma membrane |
| title_fullStr |
Ca2+ store depletion causes STIM1 to accumulate in ER regions closely associated with the plasma membrane |
| title_full_unstemmed |
Ca2+ store depletion causes STIM1 to accumulate in ER regions closely associated with the plasma membrane |
| title_sort |
ca2+ store depletion causes stim1 to accumulate in er regions closely associated with the plasma membrane |
| description |
Stromal interacting molecule 1 (STIM1), reported to be an endoplasmic reticulum (ER) Ca2+ sensor controlling store-operated Ca2+ entry, redistributes from a diffuse ER localization into puncta at the cell periphery after store depletion. STIM1 redistribution is proposed to be necessary for Ca2+ release–activated Ca2+ (CRAC) channel activation, but it is unclear whether redistribution is rapid enough to play a causal role. Furthermore, the location of STIM1 puncta is uncertain, with recent reports supporting retention in the ER as well as insertion into the plasma membrane (PM). Using total internal reflection fluorescence (TIRF) microscopy and patch-clamp recording from single Jurkat cells, we show that STIM1 puncta form several seconds before CRAC channels open, supporting a causal role in channel activation. Fluorescence quenching and electron microscopy analysis reveal that puncta correspond to STIM1 accumulation in discrete subregions of junctional ER located 10–25 nm from the PM, without detectable insertion of STIM1 into the PM. Roughly one third of these ER–PM contacts form in response to store depletion. These studies identify an ER structure underlying store-operated Ca2+ entry, whose extreme proximity to the PM may enable STIM1 to interact with CRAC channels or associated proteins. |
| publisher |
The Rockefeller University Press |
| publishDate |
2006 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2064335/ |
| _version_ |
1611406571483430912 |