Hypoxia-induced Acidosis Uncouples the STIM-Orai Calcium Signaling Complex *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 286, Issue: 52, Page: 44788-44798
2011
- 54Citations
- 37Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations54
- Citation Indexes54
- 54
- CrossRef43
- Captures37
- Readers37
- 37
Article Description
The endoplasmic reticulum Ca 2+ -sensing STIM proteins mediate Ca 2+ entry signals by coupling to activate plasma membrane Orai channels. We reveal that STIM-Orai coupling is rapidly blocked by hypoxia and the ensuing decrease in cytosolic pH. In smooth muscle cells or HEK293 cells coexpressing STIM1 and Orai1, acute hypoxic conditions rapidly blocked store-operated Ca 2+ entry and the Orai1-mediated Ca 2+ release-activated Ca 2+ current ( I CRAC ). Hypoxia-induced blockade of Ca 2+ entry and I CRAC was reversed by NH 4 + -induced cytosolic alkalinization. Hypoxia and acidification both blocked I CRAC induced by the short STIM1 Orai-activating region. Although hypoxia induced STIM1 translocation into junctions, it did not dissociate the STIM1-Orai1 complex. However, both hypoxia and cytosolic acidosis rapidly decreased Förster resonance energy transfer (FRET) between STIM1-YFP and Orai1-CFP. Thus, although hypoxia promotes STIM1 junctional accumulation, the ensuing acidification functionally uncouples the STIM1-Orai1 complex providing an important mechanism protecting cells from Ca 2+ overload under hypoxic stress conditions.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925820655272; http://dx.doi.org/10.1074/jbc.m111.303081; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84455192438&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/22084246; http://www.jbc.org/lookup/doi/10.1074/jbc.M111.303081; https://syndication.highwire.org/content/doi/10.1074/jbc.M111.303081; https://linkinghub.elsevier.com/retrieve/pii/S0021925820655272; https://dx.doi.org/10.1074/jbc.m111.303081; http://www.jbc.org/article/S0021925820655272/abstract; http://www.jbc.org/article/S0021925820655272/fulltext; http://www.jbc.org/article/S0021925820655272/pdf; https://www.jbc.org/article/S0021-9258(20)65527-2/abstract; http://www.jbc.org/cgi/doi/10.1074/jbc.M111.303081; http://www.jbc.org/content/286/52/44788.abstract; http://www.jbc.org/content/286/52/44788.full; http://www.jbc.org/content/286/52/44788.full.pdf; http://www.jbc.org/content/286/52/44788
American Society for Biochemistry & Molecular Biology (ASBMB)
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