Jack Roos

TL;DR: It is proposed that STIM1, a ubiquitously expressed protein that is conserved from Drosophila to mammalian cells, plays an essential role in SOC influx and may be a common component of SOC and CRAC channels.

TL;DR: It is proposed that STIM1 functions as the missing link between Ca2+ store depletion and SOC influx, serving as aCa2+ sensor that translocates upon store depletion to the plasma membrane to activate CRAC channels.

TL;DR: Using an unbiased genome-wide RNA interference screen in Drosophila S2 cells, 75 hits are identified that strongly inhibited Ca(2+) influx upon store emptying by thapsigargin, including Stim and olf186-F, a member of a highly conserved family of four-transmembrane spanning proteins with homologs from Caenorhabditis elegans to human.

TL;DR: It is shown that STIM1 and Orai1 are recruited to the immunological synapse between primary human T cells and autologous dendritic cells, implying a positive feedback loop in which an initial TCR signal favors up-regulation of STIM 1 and ORAi proteins that would augment Ca2+ signaling during subsequent antigen encounter.

TL;DR: RNA interference screens together with over-expression and site-directed mutagenesis have identified the triggering molecule (Stim) that links store depletion to CRAC channel-mediated Ca(2+) influx and the pore subunit (Orai) of theCRAC channel that allows highly selective entry of Ca( 2+) ions into cells.