{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,16]],"date-time":"2026-10-16T06:21:18Z","timestamp":1792131678580,"version":"4.4.0"},"reference-count":52,"publisher":"American Society for Cell Biology (ASCB)","issue":"2","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["MBoC"],"published-print":{"date-parts":[[1999,2]]},"abstract":"<jats:p>The GTPase dynamin has been clearly implicated in clathrin-mediated endocytosis of synaptic vesicle membranes at the presynaptic nerve terminal. Here we describe a novel 52-kDa protein in rat brain that binds the proline-rich C terminus of dynamin. Syndapin I (synaptic, dynamin-associated protein I) is highly enriched in brain where it exists in a high molecular weight complex. Syndapin I can be involved in multiple protein\u2013protein interactions via a src homology 3 (SH3) domain at the C terminus and two predicted coiled-coil stretches. Coprecipitation studies and blot overlay analyses revealed that syndapin I binds the brain-specific proteins dynamin I, synaptojanin, and synapsin I via an SH3 domain-specific interaction. Coimmunoprecipitation of dynamin I with antibodies recognizing syndapin I and colocalization of syndapin I with dynamin I at vesicular structures in primary neurons indicate that syndapin I associates with dynamin I in vivo and may play a role in synaptic vesicle endocytosis. Furthermore, syndapin I associates with the neural Wiskott-Aldrich syndrome protein, an actin-depolymerizing protein that regulates cytoskeletal rearrangement. These characteristics of syndapin I suggest a molecular link between cytoskeletal dynamics and synaptic vesicle recycling in the nerve terminal.<\/jats:p>","DOI":"10.1091\/mbc.10.2.501","type":"journal-article","created":{"date-parts":[[2013,7,2]],"date-time":"2013-07-02T23:25:07Z","timestamp":1372807507000},"page":"501-513","source":"Crossref","is-referenced-by-count":273,"title":["Syndapin I, a Synaptic Dynamin-binding Protein that Associates with the Neural Wiskott-Aldrich Syndrome Protein"],"prefix":"10.1091","volume":"10","author":[{"given":"Britta","family":"Qualmann","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Biophysics and the Hormone Research Institute, University of California, San Francisco, California 94143-0534"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jack","family":"Roos","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Biophysics and the Hormone Research Institute, University of California, San Francisco, California 94143-0534"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paul J.","family":"DiGregorio","sequence":"additional","affiliation":[{"name":"Department 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":"Department of Biochemistry and Biophysics and the Hormone Research Institute, University of California, San Francisco, California 94143-0534"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1076","reference":[{"key":"B1","doi-asserted-by":"crossref","first-page":"704","DOI":"10.1038\/326704a0","volume":"326","author":"B\u00e4hler M.","year":"1987","journal-title":"Nature"},{"key":"B2","doi-asserted-by":"crossref","first-page":"8259","DOI":"10.1073\/pnas.92.18.8259","volume":"92","author":"Berger B.","year":"1995","journal-title":"Proc. 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