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Ca 2+ ions represent versatile second messengers that regulate a huge diversity of processes throughout the cell's life. One prominent Ca 2+ entry pathway into the cell is the Ca 2+ release-activated Ca 2+ (CRAC) ion channel. It is fully reconstituted by the two molecular key players: the stromal interaction molecule (STIM1) and Orai. STIM1 is a Ca 2+ sensor located in the membrane of the endoplasmic reticulum, and Orai, a highly Ca 2+ selective ion channel embedded in the plasma membrane. Ca 2+ store-depletion leads initially to the activation of STIM1 which subsequently activates Orai channels via direct binding. Authentic CRAC channel hallmarks and biophysical characteristics include high Ca 2+ selectivity with a reversal potential in the range of + 50 mV, small unitary conductance, fast Ca 2+ -dependent inactivation and enhancements in currents upon the switch from a Na + -containing divalent-free to a Ca 2+ -containing solution. This review provides an overview on the critical determinants and structures within the STIM1 and Orai proteins that establish these prominent CRAC channel characteristics.

Critical parameters maintaining authentic CRAC channel hallmarks