Abstract
Calcium flux through store operated calcium entry (SOCE) is a major regulator of intracellular calcium homeostasis and various calcium signaling pathways. The two key components of the store operated calcium release activated calcium (CRAC) channel are the Ca2+ sensing protein stromal interaction molecule 1 (STIM1) and the channel pore forming protein Orai1. Following calcium depletion from the endoplasmic reticulum, STIM1 undergoes a series of conformational changes which unmask a minimal Orai1 activating domain called CAD. CAD binds to two sites in Orai1, one in the N’ terminus and one in the C’ terminus. The energetic coupling of binding of the STIM1 ligand to opening of the channel pore is poorly understood. In this study we show that both N’ and C’ terminal domains of Orai1 synergistically contribute to interaction with CAD to allosterically couple STIM1 binding with channel gating and modulation of ion selectivity.
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