{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,27]],"date-time":"2026-02-27T02:56:10Z","timestamp":1772160970407,"version":"3.50.1"},"reference-count":113,"publisher":"Wiley","issue":"10","license":[{"start":{"date-parts":[[2017,3,23]],"date-time":"2017-03-23T00:00:00Z","timestamp":1490227200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100001736","name":"German-Israeli Foundation for Scientific Research and Development","doi-asserted-by":"publisher","award":["I\u20101210\u2010286.13\/2012"],"award-info":[{"award-number":["I\u20101210\u2010286.13\/2012"]}],"id":[{"id":"10.13039\/501100001736","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["SFB 894"],"award-info":[{"award-number":["SFB 894"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["The Journal of Physiology"],"published-print":{"date-parts":[[2017,5,15]]},"abstract":"<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>\n                            \u03b2\u2010Adrenergic stimulation enhances Ca\n                            <jats:sup>2+<\/jats:sup>\n                            entry via L\u2010type Ca\n                            <jats:sub>V<\/jats:sub>\n                            1.2 channels, causing stronger contraction of cardiac muscle cells.\n                          <\/jats:p>\n                        <\/jats:list-item>\n                        <jats:list-item>\n                          <jats:p>\n                            The signalling pathway involves activation of protein kinase A (PKA), but the molecular details of PKA regulation of Ca\n                            <jats:sub>V<\/jats:sub>\n                            1.2 remain controversial despite extensive research.\n                          <\/jats:p>\n                        <\/jats:list-item>\n                        <jats:list-item>\n                          <jats:p>\n                            We show that PKA regulation of Ca\n                            <jats:sub>V<\/jats:sub>\n                            1.2 can be reconstituted in\n                            <jats:italic>Xenopus<\/jats:italic>\n                            oocytes when the distal C\u2010terminus (dCT) of the main subunit, \u03b1\n                            <jats:sub>1C<\/jats:sub>\n                            , is truncated.\n                          <\/jats:p>\n                        <\/jats:list-item>\n                        <jats:list-item>\n                          <jats:p>\n                            The PKA upregulation of Ca\n                            <jats:sub>V<\/jats:sub>\n                            1.2 does not require key factors previously implicated in this mechanism: the clipped dCT, the A kinase\u2010anchoring protein 15 (AKAP15), the phosphorylation sites S1700, T1704 and S1928, or the \u03b2 subunit of Ca\n                            <jats:sub>V<\/jats:sub>\n                            1.2. The gating element within the initial segment of the N\u2010terminus of the cardiac isoform of \u03b1\n                            <jats:sub>1C<\/jats:sub>\n                            is essential for the PKA effect.\n                          <\/jats:p>\n                        <\/jats:list-item>\n                        <jats:list-item>\n                          <jats:p>\n                            We propose that the regulation described here is one of two or several mechanisms that jointly mediate the PKA regulation of Ca\n                            <jats:sub>V<\/jats:sub>\n                            1.2 in the heart.\n                          <\/jats:p>\n                        <\/jats:list-item>\n                      <\/jats:list>\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Abstract<\/jats:title>\n                    <jats:p>\n                      \u03b2\u2010Adrenergic stimulation enhances Ca\n                      <jats:sup>2+<\/jats:sup>\n                      currents via L\u2010type, voltage\u2010gated Ca\n                      <jats:sub>V<\/jats:sub>\n                      1.2 channels, strengthening cardiac contraction. The signalling via \u03b2\u2010adrenergic receptors (\u03b2\u2010ARs) involves elevation of cyclic AMP (cAMP) levels and activation of protein kinase A (PKA). However, how PKA affects the channel remains controversial. Recent studies in heterologous systems and genetically engineered mice stress the importance of the post\u2010translational proteolytic truncation of the distal C\u2010terminus (dCT) of the main (\u03b1\n                      <jats:sub>1C<\/jats:sub>\n                      ) subunit. Here, we successfully reconstituted the cAMP\/PKA regulation of the dCT\u2010truncated Ca\n                      <jats:sub>V<\/jats:sub>\n                      1.2 in\n                      <jats:italic>Xenopus<\/jats:italic>\n                      oocytes, which previously failed with the non\u2010truncated \u03b1\n                      <jats:sub>1C<\/jats:sub>\n                      . cAMP and the purified catalytic subunit of PKA, PKA\u2010CS, injected into intact oocytes, enhanced Ca\n                      <jats:sub>V<\/jats:sub>\n                      1.2 currents by \u223c40% (rabbit \u03b1\n                      <jats:sub>1C<\/jats:sub>\n                      ) to \u223c130% (mouse \u03b1\n                      <jats:sub>1C<\/jats:sub>\n                      ). PKA blockers were used to confirm specificity and the need for dissociation of the PKA holoenzyme. The regulation persisted in the absence of the clipped dCT (as a separate protein), the A kinase\u2010anchoring protein AKAP15, and the phosphorylation sites S1700 and T1704, previously proposed as essential for the PKA effect. The Ca\n                      <jats:sub>V<\/jats:sub>\n                      \u03b2\n                      <jats:sub>2b<\/jats:sub>\n                      subunit was not involved, as suggested by extensive mutagenesis. Using deletion\/chimeric mutagenesis, we have identified the initial segment of the cardiac long\u2010N\u2010terminal isoform of \u03b1\n                      <jats:sub>1C<\/jats:sub>\n                      as a previously unrecognized essential element involved in PKA regulation. We propose that the observed regulation, that exclusively involves the \u03b1\n                      <jats:sub>1C<\/jats:sub>\n                      subunit, is one of several mechanisms underlying the overall PKA action on Ca\n                      <jats:sub>V<\/jats:sub>\n                      1.2 in the heart. We hypothesize that PKA is acting on Ca\n                      <jats:sub>V<\/jats:sub>\n                      1.2, in part, by affecting a structural \u2018scaffold\u2019 comprising the interacting cytosolic N\u2010 and C\u2010termini of \u03b1\n                      <jats:sub>1C<\/jats:sub>\n                      .\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1113\/jp274015","type":"journal-article","created":{"date-parts":[[2017,2,14]],"date-time":"2017-02-14T00:52:46Z","timestamp":1487033566000},"page":"3181-3202","source":"Crossref","is-referenced-by-count":13,"title":["Protein kinase A regulates C\u2010terminally truncated Ca\n                    <sub>V<\/sub>\n                    1.2 in\n                    <i>Xenopus<\/i>\n                    oocytes: roles of N\u2010 and C\u2010termini of the \u03b1\n                    <sub>1C<\/sub>\n                    subunit"],"prefix":"10.1113","volume":"595","author":[{"given":"Shimrit","family":"Oz","sequence":"first","affiliation":[{"name":"Department of Physiology and Pharmacology, Sackler School of Medicine Tel Aviv University Tel Aviv 6997801 Israel"}]},{"given":"Ines","family":"Pankonien","sequence":"additional","affiliation":[{"name":"Max Delbr\u00fcck Center for Molecular Medicine (MDC) D\u201013092, and the German Centre for Cardiovascular Research (DZHK) partner site Berlin Germany"}]},{"given":"Anouar","family":"Belkacemi","sequence":"additional","affiliation":[{"name":"Experimentelle und Klinische Pharmakologie und Toxikologie Universit\u00e4t des Saarlandes 66421 Homburg Germany"}]},{"given":"Veit","family":"Flockerzi","sequence":"additional","affiliation":[{"name":"Experimentelle und Klinische Pharmakologie und Toxikologie Universit\u00e4t des Saarlandes 66421 Homburg Germany"}]},{"given":"Enno","family":"Klussmann","sequence":"additional","affiliation":[{"name":"Max Delbr\u00fcck Center for Molecular Medicine (MDC) D\u201013092, and the German Centre for Cardiovascular Research (DZHK) partner site Berlin Germany"}]},{"given":"Hannelore","family":"Haase","sequence":"additional","affiliation":[{"name":"Max Delbr\u00fcck Center for Molecular Medicine (MDC) D\u201013092, and the German Centre for Cardiovascular Research (DZHK) partner site Berlin Germany"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5397-4146","authenticated-orcid":false,"given":"Nathan","family":"Dascal","sequence":"additional","affiliation":[{"name":"Department of Physiology and Pharmacology, Sackler School of Medicine Tel Aviv University Tel Aviv 6997801 Israel"},{"name":"Sagol School of Neuroscience Tel Aviv University Tel Aviv 6997801 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