{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,10]],"date-time":"2026-09-10T05:57:36Z","timestamp":1789019856376,"version":"build-2803163510"},"reference-count":56,"publisher":"National Academy of Sciences","issue":"24","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1996,11,26]]},"abstract":"<jats:p>\n                    A previously uncharacterized 22-kDa Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -binding\n protein that also binds guanosine nucleotides was characterized,\n cloned, and analyzed by electrophysiological techniques. The cloned\n protein, calexcitin, contains two EF-hands and also has homology with\n GTP-binding proteins in the ADP ribosylation factor family. In addition\n to binding two molecules of Ca\n                    <jats:sup>2+<\/jats:sup>\n                    , calexcitin bound GTP and\n possessed GTPase activity. Calexcitin is also a high affinity substrate\n for protein kinase C. Application of calexcitin to the inner surface of\n inside-out patches of human fibroblast membranes, in the presence of\n Ca\n                    <jats:sup>2+<\/jats:sup>\n                    and the absence of endogenous\n Ca\n                    <jats:sup>2+<\/jats:sup>\n                    \/calmodulin kinase type II or\n protein kinase C activity, reduced the mean open time and mean open\n probability of 115 \u00b1 6 pS K\n                    <jats:sup>+<\/jats:sup>\n                    channels. Calexcitin\n thus appears to directly regulate K\n                    <jats:sup>+<\/jats:sup>\n                    channels. When\n microinjected into molluscan neurons or rabbit cerebellar Purkinje cell\n dendrites, calexcitin was highly effective in enhancing membrane\n excitability. Because calexcitin translocates to the cell membrane\n after phosphorylation, calexcitin could serve as a\n Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -activated signaling molecule that increases cellular\n excitability, which would in turn increase Ca\n                    <jats:sup>2+<\/jats:sup>\n                    influx through the membrane. This is also the first known instance of a\n GTP-binding protein that binds Ca\n                    <jats:sup>2+<\/jats:sup>\n                    .\n                  <\/jats:p>","DOI":"10.1073\/pnas.93.24.13808","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T10:34:10Z","timestamp":1027679650000},"page":"13808-13813","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":44,"title":["Calexcitin: A signaling protein that binds calcium and GTP, inhibits potassium channels, and enhances\u2009membrane\u2009excitability"],"prefix":"10.1073","volume":"93","author":[{"given":"Thomas\u2009J.","family":"Nelson","sequence":"first","affiliation":[{"name":"Laboratory of Adaptive Systems and Laboratory of\r Neurochemistry, National Institute of Neurological Disorders and\r Stroke, National Institutes of Health, Bethesda, MD 20892;\r Harvard Medical School, McLean Hospital, 115 Mill Street,\r Belmont, MA 02178; 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