{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T19:50:36Z","timestamp":1790625036475,"version":"4.1.0"},"reference-count":44,"publisher":"National Academy of Sciences","issue":"6","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2005,2,8]]},"abstract":"<jats:p>\n                    The role of intracellular Ca\n                    <jats:sup>2+<\/jats:sup>\n                    in the regulation of actin filament assembly and disassembly has not been clearly defined. We show that reduction of intracellular free Ca\n                    <jats:sup>2+<\/jats:sup>\n                    concentration ([Ca\n                    <jats:sup>2+<\/jats:sup>\n                    ]\n                    <jats:sub>i<\/jats:sub>\n                    ) to &lt;40 nM in\n                    <jats:italic>Listeria monocytogenes<\/jats:italic>\n                    -infected, EGFP\u2013actin-transfected Madin\u2013Darby canine kidney cells results in a 3-fold lengthening of actin filament tails. This increase in tail length is the consequence of marked slowing of the actin filament disassembly rate, without a significant change in assembly rate. The Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -sensitive actin-severing protein gelsolin concentrates in the\n                    <jats:italic>Listeria<\/jats:italic>\n                    rocket tails at normal resting [Ca\n                    <jats:sup>2+<\/jats:sup>\n                    ]\n                    <jats:sub>i<\/jats:sub>\n                    and disassociates from the tails when [Ca\n                    <jats:sup>2+<\/jats:sup>\n                    ]\n                    <jats:sub>i<\/jats:sub>\n                    is lowered. Reduction in [Ca\n                    <jats:sup>2+<\/jats:sup>\n                    ]\n                    <jats:sub>i<\/jats:sub>\n                    also blocks the severing activity of gelsolin, but not actin-depolymerizing factor (ADF)\/cofilin microinjected into\n                    <jats:italic>Listeria<\/jats:italic>\n                    -infected cells. In\n                    <jats:italic>Xenopus<\/jats:italic>\n                    extracts,\n                    <jats:italic>Listeria<\/jats:italic>\n                    tail lengths are also calcium-sensitive, markedly shortening on addition of calcium. Immunodepletion of gelsolin, but not\n                    <jats:italic>Xenopus<\/jats:italic>\n                    ADF\/cofilin, eliminates calcium-sensitive actin-filament shortening.\n                    <jats:italic>Listeria<\/jats:italic>\n                    tail length is also calcium-insensitive in gelsolin-null mouse embryo fibroblasts. We conclude that gelsolin is the primary Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -sensitive actin filament recycling protein in the cell and is capable of enhancing\n                    <jats:italic>Listeria<\/jats:italic>\n                    actin tail disassembly at normal resting [Ca\n                    <jats:sup>2+<\/jats:sup>\n                    ]\n                    <jats:sub>i<\/jats:sub>\n                    (145 nM). These experiments illustrate the unique and complementary functions of gelsolin and ADF\/cofilin in the recycling of actin filaments.\n                  <\/jats:p>","DOI":"10.1073\/pnas.0409062102","type":"journal-article","created":{"date-parts":[[2005,1,25]],"date-time":"2005-01-25T22:43:38Z","timestamp":1106693018000},"page":"1921-1926","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":36,"title":["Gelsolin mediates calcium-dependent disassembly of\n                    <i>Listeria<\/i>\n                    actin tails"],"prefix":"10.1073","volume":"102","author":[{"given":"Laura","family":"Larson","sequence":"first","affiliation":[{"name":"Department of Medicine, Division of Infectious Diseases, University of Florida College of Medicine, Gainesville, FL 32610; Departments of Physiology and Medicine\/Infectious Diseases, University of Geneva, 1211 Geneva, Switzerland; and Departments of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Serge","family":"Arnaudeau","sequence":"additional","affiliation":[{"name":"Department of Medicine, Division of Infectious Diseases, University of Florida College of Medicine, Gainesville, FL 32610; 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and Departments of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ryoko","family":"Krause","sequence":"additional","affiliation":[{"name":"Department of Medicine, Division of Infectious Diseases, University of Florida College of Medicine, Gainesville, FL 32610; Departments of Physiology and Medicine\/Infectious Diseases, University of Geneva, 1211 Geneva, Switzerland; and Departments of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Binghua","family":"Hao","sequence":"additional","affiliation":[{"name":"Department of Medicine, Division of Infectious Diseases, University of Florida College of Medicine, Gainesville, FL 32610; Departments of Physiology and Medicine\/Infectious Diseases, University of Geneva, 1211 Geneva, Switzerland; and Departments of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James R.","family":"Bamburg","sequence":"additional","affiliation":[{"name":"Department of Medicine, Division of Infectious Diseases, University of Florida College of Medicine, Gainesville, FL 32610; 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