Mittelstaedt, Tobias: RIMs and RIM interacting proteins : localization and function under physiological and pathophysiological conditions. - Bonn, 2011. - Dissertation, Rheinische Friedrich-Wilhelms-Universität Bonn.
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author = {{Tobias Mittelstaedt}},
title = {RIMs and RIM interacting proteins : localization and function under physiological and pathophysiological conditions},
school = {Rheinische Friedrich-Wilhelms-Universität Bonn},
year = 2011,
month = feb,

note = {Neurons transmit signals to their target cells at specialized contact sites called synapses. At chemical synapses the signal propagation is mediated by the fusion of neurotransmitter filled synaptic vesicles with the presynaptic plasma membrane and the subsequent release of transmitter into the synaptic cleft. As compared to other cellular fusion events, the exocytotic release of neurotransmitter is extremely fast, highly regulated and spatially restricted, but also dynamically modulated. Fusion occurs only at a specialized region of the presynaptic plasma membrane, called the active zone. It is precisely aligned with the postsynaptic reception apparatus, and electron microscopic studies clearly show electron-dense structures lining the plasma membrane on both sides of the synaptic cleft. In the presynaptic terminal this electron-dense cytoskeletal matrix is referred to as the cytomatrix at the active zone (CAZ). So far five protein families have been identified to be highly enriched at active zones: Munc13s, RIMs, ELKS, Bassoon/Piccolo and Liprin-α. Additionally, the proteins linking the Active Zone to other functional parts of the presynapse, like the synaptic vesicle cycle or voltage gated calcium channels, play crucial roles in the regulation of transmitter release. In recent years studies using genetic, biochemical, structural and electrophysiological approaches have begun to elucidate how some these proteins are involved in the regulation of synaptic vesicle exocytose, in mediating use-dependent changes during different forms of plasticity and in the structural organization of the active zone.
In this study I concentrated on some of the protein families potentially involved in the process of synaptic vesicle fusion. Besides further biochemical and genetic characterization of the Active Zone proteins RIM1 and RIM2 in double knockout animals as well as the adaptor protein family RIM-BP and the Synaptotagmin family I also quantified the differential regulation of presynaptically expressed genes in response to pathologically increased synaptic activity in an animal model of temporal lobe epilepsy.
The results of my work will help to look further into the function of interesting proteins and protein families identified in this study that potentially play crucial roles in the regulation of synaptic vesicle exocytosis.},

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