id,collection,dc.contributor.author,dc.date.accessioned,dc.date.available,dc.date.issued,dc.description.abstract[de],dc.format.extent,dc.identifier.uri,dc.language,dc.rights.uri,dc.subject.ddc,dc.title,dc.type,dcterms.accessRights.openaire,dcterms.bibliographicCitation,dcterms.bibliographicCitation.doi,dcterms.bibliographicCitation.url,refubium.affiliation[de],refubium.mycore.derivateId,refubium.mycore.fudocsId,refubium.resourceType.isindependentpub "621f8a5d-9478-482b-89de-06e526e59f02","fub188/15","Siebert, Matthias||Böhme, Mathias A.||Driller, Jan H.||Babikir, Husam||Mampell, Malou M.||Rey, Ulises||Ramesh, Niraja||Matkovic, Tanja||Holton, Nicole||Reddy-Alla, Suneel||Göttfert, Fabian||Kamin, Dirk||Quentin, Christine||Klinedinst, Susan||Andlauer, Till F. M.||Hell, Stefan W.||Collins, Catherine A.||Wahl, Markus C.||Loll, Bernhard||Sigrist, Stephan J.","2018-06-08T04:01:11Z","2015-09-07T08:31:29.116Z","2015","Synaptic vesicles (SVs) fuse at active zones (AZs) covered by a protein scaffold, at Drosophila synapses comprised of ELKS family member Bruchpilot (BRP) and RIM-binding protein (RBP). We here demonstrate axonal co-transport of BRP and RBP using intravital live imaging, with both proteins co- accumulating in axonal aggregates of several transport mutants. RBP, via its C-terminal Src-homology 3 (SH3) domains, binds Aplip1/JIP1, a transport adaptor involved in kinesin-dependent SV transport. We show in atomic detail that RBP C-terminal SH3 domains bind a proline-rich (PxxP) motif of Aplip1/JIP1 with submicromolar affinity. Pointmutating this PxxP motif provoked formation of ectopic AZ-like structures at axonal membranes. Direct interactions between AZ proteins and transport adaptors seem to provide complex avidity and shield synaptic interaction surfaces of pre-assembled scaffold protein transport complexes, thus, favouring physiological synaptic AZ assembly over premature assembly at axonal membranes. - See more at: http://elifesciences.org/content/4/e06935#sthash.oVGZ8cdi.dpuf","30 S.","https://refubium.fu-berlin.de/handle/fub188/16412||http://dx.doi.org/10.17169/refubium-20593","eng","http://www.fu-berlin.de/sites/refubium/rechtliches/Nutzungsbedingungen","600 Technik, Medizin, angewandte Wissenschaften::610 Medizin und Gesundheit","A high affinity RIM-binding protein/Aplip1 interaction prevents the formation of ectopic axonal active zones","Wissenschaftlicher Artikel","open access","eLife. - 4 (2015), Artikel Nr. e06935","10.7554/eLife.06935","http://dx.doi.org/10.7554/eLife.06935","Charité - Universitätsmedizin Berlin","FUDOCS_derivate_000000005371","FUDOCS_document_000000023063","no"