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2011-06-28Zeitschriftenartikel DOI: 10.1073/pnas.1101707108
Molecular in situ topology of Aczonin/Piccolo and associated proteins at the mammalian neurotransmitter release site
dc.contributor.authorLimbach, Christoph
dc.contributor.authorLaue, Michael
dc.contributor.authorWang, Xiaolu
dc.contributor.authorHu, Bin
dc.contributor.authorThiede, Nadine
dc.contributor.authorHultqvist, Greta
dc.contributor.authorKilimann, Manfred W.
dc.date.accessioned2018-05-07T16:02:00Z
dc.date.available2018-05-07T16:02:00Z
dc.date.created2012-11-05
dc.date.issued2011-06-28none
dc.identifier.otherhttp://edoc.rki.de/oa/articles/re0NnuYd5RLE/PDF/24Z8kFALCiUHg.pdf
dc.identifier.urihttp://edoc.rki.de/176904/1342
dc.description.abstractThe protein machinery of neurotransmitter exocytosis requires efficient orchestration in space and time, for speed and precision of neurotransmission and also for synaptic ontogeny and plasticity. However, its spatial organization in situ is virtually unknown. Aczonin/Piccolo is a putative organizer protein of mammalian active zones. We determined by immunogold electron microscopy (EM) (i) the spatial arrangement (i.e., topology) of 11 segments of the Aczonin polypeptide in situ, and correlated it to (ii) the positioning of Aczonin-interacting domains of Bassoon, CAST/ELKS, Munc13, and RIM and (iii) the ultrastructurally defined presynaptic macromolecular aggregates known as dense projections and synaptic ribbons. At conventional synapses, Aczonin assumes a compact molecular topology within a layer 35 to 80 nm parallel to the plasma membrane (PM), with a "trunk" sitting on the dense projection top and a C-terminal "arm" extending down toward the PM and sideward to the dense projection periphery. At ribbon synapses, Aczonin occupies the whole ribbon area. Bassoon colocalizes with Aczonin at conventional synapses but not at ribbon synapses. At both conventional and ribbon synapses, CAST, Munc13, and RIM are segregated from Aczonin, closer to the PM, and Aczonin is positioned such that it may control the access of neurotransmitter vesicles to the fusion site.eng
dc.language.isoeng
dc.publisherRobert Koch-Institut
dc.subjectAnimalseng
dc.subjectRatseng
dc.subjectProtein Bindingeng
dc.subjectSignal Transducing/metabolismeng
dc.subjectCell Membrane/metabolismeng
dc.subjectBinding Siteseng
dc.subjectAdaptor Proteinseng
dc.subjectCell Membrane/ultrastructureeng
dc.subjectCytoskeletal Proteins/metabolismeng
dc.subjectGTP-Binding Proteins/metabolismeng
dc.subjectImmunoblottingeng
dc.subjectMicroscopy Immunoelectroneng
dc.subjectMultiprotein Complexes/metabolismeng
dc.subjectMultiprotein Complexes/ultrastructureeng
dc.subjectNerve Tissue Proteins/metabolismeng
dc.subjectNeuropeptides/metabolismeng
dc.subjectNeurotransmitter Agents/metabolismeng
dc.subjectRats Sprague-Dawleyeng
dc.subjectSynapses/metabolismeng
dc.subjectSynapses/ultrastructureeng
dc.subject.ddc610 Medizin
dc.titleMolecular in situ topology of Aczonin/Piccolo and associated proteins at the mammalian neurotransmitter release site
dc.typeperiodicalPart
dc.identifier.urnurn:nbn:de:0257-10027742
dc.identifier.doi10.1073/pnas.1101707108
dc.identifier.doihttp://dx.doi.org/10.25646/1267
local.edoc.container-titleProceedings of the National Academy of Sciences
local.edoc.container-textChristoph Limbach, Michael M. Laue, Xiaolu Wang, Bin Hu, Nadine Thiede, Greta Hultqvist, and Manfred W. Kilimann. Molecular in situ topology of Aczonin/Piccolo and associated proteins at the mammalian neurotransmitter release site. (2011) Proceedings of the National Academy of Sciences of the United States of America, 108 (31), pp. 392-401.
local.edoc.fp-subtypeArtikel
local.edoc.type-nameZeitschriftenartikel
local.edoc.container-typeperiodical
local.edoc.container-type-nameZeitschrift
local.edoc.container-urlhttp://www.pnas.org/content/108/31/E392
local.edoc.container-publisher-nameNational Academy of Sciences
local.edoc.container-volume108
local.edoc.container-issue31
local.edoc.container-year2011

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