Author(s): Salido GM, Sage SO, Rosado JA
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Abstract Store-operated calcium entry (SOCE) is a major mechanism for Ca(2+) entry in excitable and non-excitable cells. The best-characterised store-operated current is I(CRAC), but other currents activated by Ca(2+) store depletion have also been reported. The recent identification of the proteins stromal interaction molecule 1 (STIM1) and Orai1 has shed new light on the nature and regulation of SOC channels. STIM1 has been presented as the endoplasmic reticulum (ER) Ca(2+) sensor that communicates the content of the Ca(2+) stores to the store-operated channels, a mechanism that involves redistribution of STIM1 to peripheral ER sites and co-clustering with the Ca(2+) channel subunit, Orai1. Interestingly, TRPC1, which has long been proposed as a SOC channel candidate, associates with Orai1 and STIM1 in a ternary complex that appears to increase the variability of SOC currents available to modulate cell function.
This article was published in Cell Signal
and referenced in Journal of Clinical & Experimental Ophthalmology