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Regulators of Synaptic Vesicle Docking and Priming

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posted on 24.10.2013, 00:00 by Szi-chieh Yu
Synaptic vesicle priming is dependent on the assembly of SNARE (soluble-N- ethylmaleimide-sensitive factor attachment receptor) complexes formed between Synaptobrevin, SNAP-25 and Syntaxin. The subsequent calcium-dependent release of primed vesicles requires the recruitment of the calcium-sensor, Synaptotagmin, a protein also implicated in endocytosis. As a consequence, proteins that regulate SNARE complex formation or stabilization can profoundly alter the synaptic strength. This thesis focuses on four SNARE interacting proteins, Snapin, Synaptotagmin, VPS- 39 as well as Tomosyn, and explores their neuronal function by primarily using high pressure freezing/ freeze substitution (HPF/FS) electron microscope (EM) combined with other techniques. Specifically, the results presented in this thesis establish that Snapin stabilizes the SNARE complex to promote fusion in a Synaptotagmin- independent manner in C. elegans, that C. elegans VPS-39 alters Syntaxin conformation to enable fusogenic SNARE complex assembly, and that Drosophila Tomosyn functions as an important effector in the cAMP signaling pathway.



Featherstone, David E.


Biological Sciences

Degree Grantor

University of Illinois at Chicago

Degree Level


Committee Member

Richmond, Janet E. Gong, Liang-Wei Alford, Simon Biron, David

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