{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPannexin‐1 (PANX1) is a membrane channel assembled as a multimer—most often heptameric—that does not form traditional gap junctions but instead functions as a hemichannel in the nonjunctional plasma membrane. PANX1 channels exhibit unique gating properties that are regulated by a variety of stimuli including caspase‐mediated C‐terminal cleavage, S‐nitrosylation, membrane depolarization, or receptor‐mediated signaling. Such regulatory mechanisms relieve intrinsic inhibition imposed by the C terminus to allow permeation not only of small ions but also of larger signalling molecules like ATP. Structural studies using electron microscopy and biochemical analyses have revealed that PANX1 is glycosylated, displays distinctive extracellular constriction sites (which may act as molecular sieves) and, upon proteolytic or pharmacological activation, undergoes progressive, quantized opening that enables the permeation of ionic and large anionic species. This detailed molecular architecture and gating mechanism have been elucidated in numerous studies that together establish the unique biophysical and regulatory properties of PANX1 channels."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "15"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its fundamental biophysical properties, PANX1 operates as a key ATP‐release conduit that regulates extracellular purinergic signaling in diverse cellular contexts. In erythrocytes and airway epithelial cells, PANX1 channels open in response to mechanical stretch, low oxygen tension, or hypotonic challenge to mediate ATP efflux, thereby contributing to vasodilation, mucociliary clearance, and oxygen sensing. Similarly, in immune cells including T lymphocytes, neutrophils, and macrophages, PANX1‐mediated ATP release orchestrates autocrine and paracrine feedback loops that modulate Ca²⁺ influx, inflammasome activation, interleukin‐1β processing, and chemotactic responses. Additionally, PANX1 activation during apoptosis enables the release of “find‐me” nucleotides that promote phagocyte recruitment, while its involvement in receptor complexes (e.g. with P2X₇ receptors) highlights its role in cell death and pro‐inflammatory signalling cascades. Collectively, these studies underscore a central role for PANX1 in coupling cellular stress and receptor activation to extracellular nucleotide signaling in both homeostatic and pathophysiological settings."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "16", "end_ref": "29"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nPANX1 also plays multifaceted roles in diverse disease processes and developmental programs. Studies have linked dysregulated PANX1 activity or expression to cancer progression and metastasis, aberrant immune responses, epileptogenesis, and even infertility. In several cancers—including metastatic breast cancer and melanoma—increased or mutant forms of PANX1 modulate ATP‐mediated autocrine survival signals and cell–cell communication that favor tumor aggressiveness. In parallel, PANX1-dependent endothelial activation promotes leukocyte adhesion and emigration during vascular inflammation, while PANX1 mutations have been associated with defects in oocyte development and multiorgan syndromes. Furthermore, in skeletal muscle and other tissues, PANX1 contributes to cell differentiation and tissue homeostasis, and its aberrant regulation has been implicated in respiratory disorders such as COPD. These varied roles emphasize PANX1’s importance as a versatile modulator of purinergic signaling and cellular integrity in both health and disease."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "30", "end_ref": "32"}, {"type": "fg_f", "ref": "25"}, {"type": "fg_fs", "start_ref": "33", "end_ref": "35"}, {"type": "fg_f", "ref": "28"}, {"type": "fg_fs", "start_ref": "36", "end_ref": "43"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Fabien Vanden Abeele, Gabriel Bidaux, Dmitri Gordienko, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Pannexin1 is part of the pore forming unit of the P2X(7) receptor death complex."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS Lett (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.febslet.2006.12.056"}], "href": "https://doi.org/10.1016/j.febslet.2006.12.056"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17240370"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17240370"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Daniela Boassa, Cinzia Ambrosi, Feng Qiu, et al. 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