{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nORAI3 is emerging as a multifunctional Ca²⁺‐permeable channel that contributes to both store‐operated and store‐independent Ca²⁺ entry mechanisms. In several cell types—including a subset of estrogen receptor–positive breast cancer cells—ORAI3 forms channels that couple with STIM proteins to mediate Ca²⁺ release–activated Ca²⁺ (CRAC) currents, yet under certain pharmacological conditions (for example, in response to 2‐aminoethoxydiphenyl borate) these channels can be activated in a store‐independent fashion. In comparison with its homologs, ORAI3 displays distinctive ion selectivity and gating properties, such as reduced Ca²⁺ depotentiation and altered fast Ca²⁺‐dependent inactivation, which together indicate a unique pore architecture and regulatory profile."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the context of cancer, ORAI3 is frequently up‐regulated and its expression levels are closely linked with oncogenic signaling. In estrogen receptor–positive breast cancers, for example, ORAI3 expression is directly regulated by ERα, and its elevated levels are associated with enhanced store‐operated Ca²⁺ influx, activation of downstream effectors such as ERK1/2, focal adhesion kinase, and NFAT, and ultimately increased proliferation, anchorage‐independent growth, and tumorigenesis. Similar dysregulation of ORAI3 has also been observed in prostate, non–small cell lung, and pancreatic cancers, where ORAI3 not only influences cell cycle progression and survival but in some settings alters the balance of heteromeric channel assembly with ORAI1 to shift Ca²⁺ entry toward pro‐survival and antiapoptotic outcomes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "15"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its role in regulating Ca²⁺ influx amplitude and kinetics, ORAI3 contributes to determining the redox responsiveness and fine‐tuning of Ca²⁺ channel activity. Unlike ORAI1, ORAI3 is relatively resistant to oxidative inhibition, a property that has significant functional implications in immune cell activation and redox‐challenged environments. Structural determinants within ORAI3—notably within its cytosolic domains—modulate its interaction with STIM proteins and shape channel inactivation and ion selectivity. These molecular features not only account for its diminished ability to trigger nuclear factor of activated T cells (NFAT) activation compared to ORAI1 but also underlie its participation in phenomena such as the 2‐APB–induced endoplasmic reticulum Ca²⁺ leak."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "16", "end_ref": "22"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdditional layers of regulation of ORAI3 involve post‐transcriptional mechanisms and unique roles in cell motility and stemness. MicroRNAs—such as miR18a/miR18b that up‐regulate ORAI3 and miR34a that represses it—modulate its expression, providing potential avenues for therapeutic intervention. In differentiated epithelia like the airway and in bladder tumors, altered ORAI3 levels have been linked to changes in ciliary beating and favorable prognostic outcomes, respectively. Moreover, in cancer stem cell populations (for instance, in oral/oropharyngeal carcinomas), ORAI3 promotes stemness through up‐regulation of key transcription factors, thereby contributing to tumor progression and chemoresistance."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "23", "end_ref": "28"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Wayne I DeHaven, Jeremy T Smyth, Rebecca R Boyles, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Calcium inhibition and calcium potentiation of Orai1, Orai2, and Orai3 calcium release-activated calcium channels."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M611374200"}], "href": "https://doi.org/10.1074/jbc.M611374200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17452328"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17452328"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Olivier Mignen, Jill L Thompson, Trevor J Shuttleworth "}, {"type": "b", "children": [{"type": "t", "text": "Both Orai1 and Orai3 are essential components of the arachidonate-regulated Ca2+-selective (ARC) channels."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Physiol (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1113/jphysiol.2007.146258"}], "href": "https://doi.org/10.1113/jphysiol.2007.146258"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17991693"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17991693"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Christine Peinelt, Annette Lis, Andreas Beck, et al. "}, {"type": "b", "children": [{"type": "t", "text": "2-Aminoethoxydiphenyl borate directly facilitates and indirectly inhibits STIM1-dependent gating of CRAC channels."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Physiol (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1113/jphysiol.2008.151365"}], "href": "https://doi.org/10.1113/jphysiol.2008.151365"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18403424"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18403424"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Shenyuan L Zhang, J Ashot Kozak, Weihua Jiang, et al. 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