{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T18:15:10Z","timestamp":1791396910436,"version":"4.3.3"},"reference-count":50,"publisher":"Rockefeller University Press","issue":"5","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2000,3,6]]},"abstract":"<jats:p>Syndapin I (SdpI) interacts with proteins involved in endocytosis and actin dynamics and was therefore proposed to be a molecular link between the machineries for synaptic vesicle recycling and cytoskeletal organization. We here report the identification and characterization of SdpII, a ubiquitously expressed isoform of the brain-specific SdpI. Certain splice variants of rat SdpII in other species were named FAP52 and PACSIN 2. SdpII binds dynamin I, synaptojanin, synapsin I, and the neural Wiskott-Aldrich syndrome protein (N-WASP), a stimulator of Arp2\/3 induced actin filament nucleation. In neuroendocrine cells, SdpII colocalizes with dynamin, consistent with a role for syndapin in dynamin-mediated endocytic processes. The src homology 3 (SH3) domain of SdpI and -II inhibited receptor-mediated internalization of transferrin, demonstrating syndapin involvement in endocytosis in vivo. Overexpression of full-length syndapins, but not the NH2-terminal part or the SH3 domains alone, had a strong effect on cortical actin organization and induced filopodia. This syndapin overexpression phenotype appears to be mediated by the Arp2\/3 complex at the cell periphery because it was completely suppressed by coexpression of a cytosolic COOH-terminal fragment of N-WASP. Consistent with a role in actin dynamics, syndapins localized to sites of high actin turnover, such as filopodia tips and lamellipodia. Our results strongly suggest that syndapins link endocytosis and actin dynamics.<\/jats:p>","DOI":"10.1083\/jcb.148.5.1047","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T16:45:41Z","timestamp":1027701941000},"page":"1047-1062","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":281,"title":["Syndapin Isoforms Participate in Receptor-Mediated Endocytosis and Actin Organization"],"prefix":"10.1083","volume":"148","author":[{"given":"Britta","family":"Qualmann","sequence":"first","affiliation":[{"name":"aDepartment of Biochemistry and Biophysics and the Hormone Research Institute, University of California, San Francisco, California 94143-0534"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Regis B.","family":"Kelly","sequence":"additional","affiliation":[{"name":"aDepartment of Biochemistry and Biophysics and the Hormone Research Institute, University of California, San Francisco, California 94143-0534"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"291","published-online":{"date-parts":[[2000,3,6]]},"reference":[{"key":"2023072902160432100_AltankovandGrinnell1993","doi-asserted-by":"crossref","first-page":"1449","DOI":"10.1083\/jcb.120.6.1449","article-title":"Depletion of intracellular potassium disrupts coated pits and reversibly inhibits cell polarization during fibroblast spreading","volume":"120","author":"Altankov","year":"1993","journal-title":"J. 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