{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSLC26A9 is an epithelial anion transporter that functions predominantly as a chloride channel and electrogenic Cl⁻/HCO₃⁻ exchanger. In a variety of experimental systems—including Xenopus oocytes, HEK293 cells, and polarized human bronchial epithelial cells—SLC26A9 mediates a constitutive Cl⁻ current and contributes to both basal and stimulated transmembrane chloride flux. Its ion‐selectivity (with a preference for I⁻, Br⁻, and Cl⁻ over other anions) and its modulation by intracellular second messengers and kinases (such as the WNK family) underscore its role in maintaining epithelial ion homeostasis. These studies also reveal minimal permeability to hydroxide and bicarbonate under resting conditions, though HCO₃⁻ may act as a modulator of its channel activity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nA substantial body of evidence demonstrates that SLC26A9 interacts functionally and physically with the CF transmembrane conductance regulator (CFTR), thereby modifying its processing, plasma membrane expression, and channel activity. In cystic fibrosis (CF), SLC26A9 variants have been associated not only with meconium ileus and altered pancreatic or lung disease severity but also with differential responses to CFTR‐targeted therapies such as ivacaftor and correctors (e.g., VX‐809). In systems expressing wild‐type CFTR, SLC26A9 enhances cAMP‐stimulated chloride currents, whereas its activity is compromised (or even mislocalized) when co‐expressed with the F508del‐CFTR mutant. Moreover, genetic studies have implicated SLC26A9 variants as modifiers of CF-related diabetes and other aspects of epithelial dysfunction, emphasizing its clinical relevance as both a disease modifier and a potential therapeutic target."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "16"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRegulation of SLC26A9’s ion transport activity is complex and involves its cytoplasmic domains, including the STAS domain and the C-terminus, as well as interactions with PDZ-domain proteins. Mutations within the STAS domain can markedly reduce SLC26A9-mediated currents and disrupt the positive influence it exerts on CFTR activity. In addition, studies have shown that aberrant protein folding and enhanced proteasomal degradation—mechanisms modulated through chaperones such as Hsp70 and via the endoplasmic reticulum quality control machinery—can diminish SLC26A9’s plasma membrane expression. These findings underscore the importance of SLC26A9’s structural integrity and its dynamic intracellular interactions in governing effective anion transport."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "17", "end_ref": "22"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond the airways, SLC26A9 is highly expressed in other epithelial tissues such as the gastric mucosa and pancreatic duct cells, where it may contribute to acid secretion and bicarbonate buffering. Altered expression or function of SLC26A9 has been linked not only to CF-related pancreatic damage but also to conditions such as asthma—with evidence suggesting that its activation aids in preventing mucus plugging—and even to neoplastic changes in the gastric mucosa. Further, investigations in autoimmune polyendocrine syndromes hint at a broader role for SLC26A9 within networks of solute carriers that together influence epithelial homeostasis and disease susceptibility."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "23", "end_ref": "26"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Michael F Romero, Min-Hwang Chang, Consuelo Plata, et al. 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