Gene knockout in cell lines and mice reveal that store-operated calcium entry is synergistically mediated by Orai1 and Orai3 channel proteins in B cells and is important for signaling to the nucleus and metabolic activity in response to antigenic stimulation.

Electrophysiological and molecular modeling studies identify a sulfur-aromatic interaction between the hydrophobic channel gate and a nearby methionine residue, termed the "gate latch", which is essential for Orai1 pore opening.

A human Orai1 mutation linked to tubular myopathy activates Orai1 channels independently of STIM1 and unmasks calcium-dependent inactivation of Orai1 channels.

ORAI1 ion channel lipid modification is required for a proper immune synapse formation and T cell activation.

α-SNAP mediated rearrangement of Stim1 and Orai1 molecules within CRAC channel clusters is required for store-operated calcium entry.

Orai1 channels activate intermittently in motile T cells, generating calcium transients, detected by a novel genetically encoded indicator and inducing pauses that favor antigen scanning.

Structural and functional analyses show that transverse tubule association with stacks of sarcoplasmic reticulum enhances Orai1-dependent Ca²⁺ entry to replenish Ca²⁺ stores, maintain Ca²⁺ release, and maximize force during exercise.

Binding of the second messenger inositol 1,4,5-trisphosphate to its intracellular receptor drives interaction between the intracellular Ca2+ sensor STIM and the plasma membrane localized Ca2+ channel Orai and raises the level of store-operated Ca2+ entry in mammalian cells.

A potent and selective DYRK2 inhibitor has been developed and used as a chemical tool to reveal eukaryotic translation initiation factor 4E-binding protein 1 (4E-BP1) and stromal interaction molecule 1 (STIM1) are new substrates for DYRK2.

Identification of a pro-tumorigenic and pro-metastatic role of EHD2 protein in triple-negative breast cancer (TNBC) through the store-operated calcium entry (SOCE) pathway provides a rationale for potential targeting of EHD2-overexpressing TNBC with SOCE inhibitors.