{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,18]],"date-time":"2026-05-18T10:21:41Z","timestamp":1779099701749,"version":"3.51.4"},"reference-count":111,"publisher":"Wiley","issue":"12","license":[{"start":{"date-parts":[[2025,6,25]],"date-time":"2025-06-25T00:00:00Z","timestamp":1750809600000},"content-version":"vor","delay-in-days":24,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2025,6,1]],"date-time":"2025-06-01T00:00:00Z","timestamp":1748736000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["physoc.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The Journal of Physiology"],"published-print":{"date-parts":[[2025,6]]},"abstract":"<jats:sec>\n                    <jats:title>Abstract<\/jats:title>\n                    <jats:p>\n                      Parkinson's disease (PD) is a complex, progressive neurodegenerative disorder driven by multiple pathogenetic factors, including oxidative stress, mitochondria dysfunction, neuroinflammation and ion imbalance. Recent evidence highlights the significant role of potassium channels in the pathophysiology of PD. We recently identified a PD\u2010linked genetic mutation in the\n                      <jats:italic>KCNJ15<\/jats:italic>\n                      gene (\n                      <jats:italic>\n                        KCNJ15\n                        <jats:sup>p.R28C<\/jats:sup>\n                      <\/jats:italic>\n                      ), encoding the inwardly rectifying potassium channel Kir4.2, within a four\u2010generation family with familial PD. However, the role of the Kir4.2 channel in neurodegenerative diseases remains largely unexplored. This study aimed to elucidate the impact of the\n                      <jats:italic>\n                        KCNJ15\n                        <jats:sup>p.R28C<\/jats:sup>\n                      <\/jats:italic>\n                      (Kir4.2\n                      <jats:sup>R28C<\/jats:sup>\n                      ) mutation on the biophysical and biochemical properties of Kir4.2. Employing Kir4.2\u2010overexpressing HEK293T cells as a model, we investigated how the mutation affects the channel's functional properties, total protein expression, intracellular processing in the endoplasmic reticulum and lysosomes and plasma membrane trafficking. Patch clamp studies revealed that the Kir4.2\n                      <jats:sup>R28C<\/jats:sup>\n                      mutation results in loss of channel function with significant dominant\u2010negative effects. This dysfunction is partially attributed to the substantial reduction in overall mutant channel protein expression compared to the wild\u2010type (Kir4.2\n                      <jats:sup>WT<\/jats:sup>\n                      ). We observed that both Kir4.2\n                      <jats:sup>WT<\/jats:sup>\n                      and Kir4.2\n                      <jats:sup>R28C<\/jats:sup>\n                      proteins undergo glycosylation during the post\u2010translational modification process, albeit with differing protein turnover efficiencies. Furthermore, the Kir4.2\n                      <jats:sup>R28C<\/jats:sup>\n                      mutant exhibits reduced stability and compromised plasma membrane trafficking capacity compared to Kir4.2\n                      <jats:sup>WT<\/jats:sup>\n                      . These findings suggest that the Kir4.2\n                      <jats:sup>R28C<\/jats:sup>\n                      mutant has unique biomolecular and biophysical characteristics distinct from the Kir4.2\n                      <jats:sup>WT<\/jats:sup>\n                      channel, which potentially elucidates its role in the pathogenesis of PD.\n                      <jats:boxed-text content-type=\"graphic\" position=\"anchor\">\n                        <jats:graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" mimetype=\"image\/png\" position=\"anchor\" specific-use=\"enlarged-web-image\" xlink:href=\"graphic\/tjp16752-gra-0001-m.png\">\n                          <jats:alt-text>image<\/jats:alt-text>\n                        <\/jats:graphic>\n                      <\/jats:boxed-text>\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Key points<\/jats:title>\n                    <jats:p>\n                      <jats:list list-type=\"bullet\">\n                        <jats:list-item>\n                          <jats:p>Inwardly rectifying potassium channels are increasingly recognized for their critical role in the complex pathogenesis of Parkinson's disease (PD).<\/jats:p>\n                        <\/jats:list-item>\n                        <jats:list-item>\n                          <jats:p>\n                            We previously identified a genetic mutation, Kir4.2\n                            <jats:sup>R28C<\/jats:sup>\n                            , in the inwardly rectifying potassium channel Kir4.2, which strongly segregates with familial PD in a multi\u2010generational pedigree.\n                          <\/jats:p>\n                        <\/jats:list-item>\n                        <jats:list-item>\n                          <jats:p>\n                            This study confirms Kir4.2\n                            <jats:sup>R28C<\/jats:sup>\n                            as a loss\u2010of\u2010function mutation with significant dominant\u2010negative effects, impairing channel activity even in heterozygous conditions.\n                          <\/jats:p>\n                        <\/jats:list-item>\n                        <jats:list-item>\n                          <jats:p>\n                            The Kir4.2\n                            <jats:sup>R28C<\/jats:sup>\n                            mutation significantly reduces overall protein levels, impairs protein stability and disrupts plasma membrane trafficking in\n                            <jats:italic>in vitro<\/jats:italic>\n                            cell models.\n                          <\/jats:p>\n                        <\/jats:list-item>\n                      <\/jats:list>\n                    <\/jats:p>\n                  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