Phase state of lipid bilayers modulates ammonia and water permeability through AtTip2; 1

Phase state of lipid bilayers modulates ammonia and water permeability through AtTip2; 1 store-depletion. This binding of SARAF with Orai1 upon store-depletion is important for the inactivation of CRAC currents. We hypothesize S-acylation of SARAF is required for the inactivation of SOCE. Here we show that SARAF is S-acylated in Jurkat T cells upon activation of the T cell receptor (TCR) and subsequent store-depletion. We also show the residue where SARAF undergoes this S-acylation. Importantly, a C320S mutant version of SARAF that cannot undergo S-acylation has deficits in CRAC channel formation and SOCE. Put together, these data suggest SARAF is a crucial component of SOCE.