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MBC in Press, published online ahead of print November 5, 2008
Mol. Biol. Cell 10.1091/mbc.E07-11-1132

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Submitted on November 12, 2007
Revised on September 12, 2008
Accepted on October 29, 2008

Molecular Clustering of STIM1 with Orai1/CRACM1 at the Plasma Membrane Depends Dynamically on Depletion of Ca2+ Stores and on Electrostatic Interactions

Nathaniel Calloway,* Monika Vig,{dagger} Jean-Pierre Kinet,{dagger} David Holowka,* and Barbara Baird*

*Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY, 14850; {dagger}Beth Israel-Deaconess Medical Center, Harvard Medical School, Boston, MA, 02215

Monitoring Editor: Jennifer Lippincott-Schwartz

Activation of store operated Ca2+ entry involves stromal interaction molecule 1 (STIM1), localized to the endoplasmic reticulum (ER), and calcium channel subunit (Orai1/CRACM1), localized to the plasma membrane. Confocal microscopy shows that thapsigargin-mediated depletion of ER Ca2+ stores in RBL mast cells causes a redistribution of STIM1, labeled with monomeric red fluorescent protein mRFP, to micron-scale ER-plasma membrane junctions that contain Orai1/CRACM1, labeled with monomeric green fluorescent protein AcGFP. Using fluorescence resonance energy transfer (FRET), we determine that this visualized coredistribution is accompanied by nanoscale interaction of STIM1-mRFP and AcGFP-Orai1/CRACM1. We find that antigen stimulation of IgE receptors causes much less Orai1/CRACM1 and STIM1 association, but strong interaction is observed under conditions that prevent refilling of ER stores. Stimulated association monitored by FRET is inhibited by sphingosine derivatives in parallel with inhibition of Ca2+ influx. Similar structural and functional effects are caused by mutation of acidic residues in the cytoplasmic segment of Orai1/CRACM1, suggesting a role for electrostatic interactions via these residues in the coupling of Orai1/CRACM1 to STIM1. Our results reveal dynamic molecular interactions between STIM1 and Orai1/CRACM1 that depend quantitatively on electrostatic interactions and on the extent of store depletion.

Address correspondence to: Barbara Baird (bab13{at}cornell.edu)




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