{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T08:17:30Z","timestamp":1791101850332,"version":"4.1.0"},"reference-count":34,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2007,1,10]],"date-time":"2007-01-10T00:00:00Z","timestamp":1168387200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2007,2]]},"abstract":"<jats:p>The ability of protein kinase\u2003C and casein kinase 2 substrate in neurons (PACSIN)\/syndapin proteins to self\u2010polymerize is crucial for the simultaneous interactions with more than one Src homology 3 domain\u2010binding partner or with lipid membranes. The assembly of this network has profound effects on the neural Wiskott\u2013Aldrich syndrome protein\u2010mediated attachment of the actin polymerization machinery to vesicle membranes as well as on the movement of the corresponding vesicles. Also, the sensing of vesicle membranes and\/or the induction of membrane curvature are more easily facilitated in the presence of larger PACSIN complexes. The N\u2010terminal Fes\u2010CIP homology and Bin\u2010Amphiphysin\u2010Rvs (F\u2010BAR) domains of several PACSIN\u2010related proteins have been shown to mediate self\u2010interactions, whereas studies using deletion mutants derived from closely related proteins led to the view that oligomerization depends on the formation of a trimeric complex via a coiled\u2010coil region present in these molecules. To address whether the model of trimeric complex formation is applicable to PACSIN\u20031, the protein was recombinantly expressed and tested in four different assays for homologous interactions. The results showed that PACSIN\u20031 forms tetramers of about 240\u2003kDa, with the self\u2010interaction having a <jats:italic>K<\/jats:italic><jats:sub>D<\/jats:sub> of 6.4\u2003\u00d7\u200310<jats:sup>\u22128<\/jats:sup>\u2003<jats:sc>m<\/jats:sc>. Ultrastructural analysis of these oligomers after negative staining showed that laterally arranged PACSIN molecules bind to each other via a large globular domain and form a barrel\u2010like structure. Together, these results demonstrate that the N\u2010terminal F\u2010BAR domain of PACSIN\u20031 forms the contact site for a tetrameric structure, which is able to simultanously interact with multiple Src homology 3 binding partners.<\/jats:p>","DOI":"10.1111\/j.1742-4658.2006.05622.x","type":"journal-article","created":{"date-parts":[[2007,1,10]],"date-time":"2007-01-10T17:44:47Z","timestamp":1168451087000},"page":"773-782","source":"Crossref","is-referenced-by-count":28,"title":["PACSIN\u20031 forms tetramers via its N\u2010terminal F\u2010BAR 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