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WFRF:(Limbach Christoph)
 

Sökning: WFRF:(Limbach Christoph) > Molecular in situ t...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003304naa a2200409 4500
001oai:DiVA.org:uu-157245
003SwePub
008110822s2011 | |||||||||||000 ||eng|
024a https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-1572452 URI
024a https://doi.org/10.1073/pnas.11017071082 DOI
040 a (SwePub)uu
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
100a Limbach, Christophu Uppsala universitet,Institutionen för neurovetenskap,Molecular cell biology4 aut
2451 0a Molecular in situ topology of Aczonin/Piccolo and associated proteins at the mammalian neurotransmitter release site
264 c 2011-06-28
264 1b Proceedings of the National Academy of Sciences,c 2011
338 a print2 rdacarrier
520 a The 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.
653 a scaffolding protein
653 a protein structure
653 a MEDICINE
653 a MEDICIN
700a Laue, Michael M.4 aut
700a Wang, Xiaolu4 aut
700a Hu, Bin4 aut
700a Thiede, Nadineu Uppsala universitet,Molekylär cellbiologi4 aut
700a Hultqvist, Gretau Uppsala universitet,Institutionen för neurovetenskap,Molekylär cellbiologi4 aut0 (Swepub:uu)grhul102
700a Kilimann, Manfred W.u Uppsala universitet,Institutionen för neurovetenskap,Molekylär cellbiologi4 aut0 (Swepub:uu)makil021
710a Uppsala universitetb Institutionen för neurovetenskap4 org
773t Proceedings of the National Academy of Sciences of the United States of Americad : Proceedings of the National Academy of Sciencesg 108:31, s. E392-E401q 108:31<E392-E401x 0027-8424x 1091-6490
856u http://21712437
856u https://www.pnas.org/content/pnas/108/31/E392.full.pdf
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-157245
8564 8u https://doi.org/10.1073/pnas.1101707108

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