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SUMMARY:Functional protein architectures defining presynaptic active zones
  - Stephan Sigrist Freie Universitaet Berlin/NeuroCure
DTSTART:20170519T100000Z
DTEND:20170519T110000Z
UID:TALK72678@talks.cam.ac.uk
CONTACT:50507
DESCRIPTION:The majority of rapid cell-to-cell communication within the ne
 rvous system makes use of chemical synapses. As a basis to understand how 
 synapses process and store information\, the molecular organization of pre
 synaptic active zones\, the places where neurotransmitter filled synaptic 
 vesicles (SVs) get released\, is a focus of intense investigation. We prev
 iously identified two conserved scaffold proteins for presynaptic active z
 one organization\, Bruchpilot (BRP) and Rim-binding protein (RimBP)1\,2\, 
 which are essential for structural organization and efficient neurotransmi
 tter release at active zones in Drosophila. To overcome the resolution lim
 it of standard light microscopy precluding the study of sub-synapse organi
 zation\, we use super-resolution light microscopy (stimulated emission dep
 letion microscopy\, STED). Thus\, functional molecular architectures conne
 cting scaffold proteins with Ca2+ channels and release machinery3 could be
  effectively studied. An evolutionary conserved design emerges where scaff
 old protein based SV  “release slots” operate as unitary building bloc
 ks in the control of SV release regulation. \n\n\n1.	Liu KS\, Siebert M\, 
 Mertel S\, et al. RIM-binding protein\, a central part of the active zone\
 , is essential for neurotransmitter release. Science 2011\;334:1565-9.\n2.
 	Kittel RJ\, Wichmann C\, Rasse TM\, et al. Bruchpilot promotes active zon
 e assembly\, Ca2+ channel clustering\, and vesicle release. Science 2006\;
 312:1051-4.\n3.	Bohme MA\, Beis C\, Reddy-Alla S\, et al. Active zone scaf
 folds differentially accumulate Unc13 isoforms to tune Ca(2+) channel-vesi
 cle coupling. Nature neuroscience 2016\;19:1311-20.\n\n
LOCATION:Klug Seminar Room\, Level 2 2A180\, MRC LMB
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