Linking synaptotagmin to vesicle fusion

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Publication Type thesis
School or College College of Science
Department Biology
Author Barusch, Nathaniel Morris
Title Linking synaptotagmin to vesicle fusion
Date 2009-05
Description Synaptotagmin 1 is an integral synaptic vesicle protein and is believed to be the major calcium sensor in synaptic vesicle fusion. Loss of synaptotagmin 1 from the nematode C. elegans results in an uncoordinated phenotype and decreased levels of neurotransmitter release. Synaptotagmin consists of two calcium/lipid binding C2 domains (C2A and C2B) separated by a short flexible linker (12 AA). While the role of the C2 domains has been extensively studied, the role of the short linker domain between them has not. It has been proposed that the linker sequence may be important in interacting with the SNAREs and with positioning the C2 domains in relation to each other and the SNARE complex. We explore two models for the role of the linker domain. 1) The sequence of the linker is important for function. To test the effects of the linker sequence the sequence was replaced with a flexible sequence consisting of repeats of glycine-glycine-serine (GGS). 2) The length of the linker is critical for its function. To test the effects of increasing the length of this linker domain the sequence was repeated, doubling the length. Initial results show partial rescue of endocytosis and exocytosis function for the flexible and double linker constructs. This suggests the sequence and length of the linker is important, but not vital, for synaptotagmin function. The next step is to determine whether endocytosis or exocytosis is being affected by these mutations.
Type Text
Publisher University of Utah
Subject Caenorhabditis elegans; Synaptic vesicles; Neural transmission
Dissertation Institution University of Utah
Dissertation Name Honors BFA
Language eng
Relation is Version of Digital reproduction of "Linking synaptotagmin to vesicle fusion" J. Willard Marriott Library Special Collections QP6.5 2009 .B37
Rights Management © Nathaniel Morris Barusch, To comply with copyright, the file for this work may be restricted to The University of Utah campus libraries
Format Medium application/pdf
Format Extent 81,092 bytes
Identifier us-etd2,150470
Source Original: University of Utah J. Willard Marriott Library Special Collections
Conversion Specifications Original scanned on Epson GT-30000 as 400 dpi to pdf using ABBYY FineReader 9.0 Professional Edition.
ARK ark:/87278/s6708fx6
Setname ir_etd
Date Created 2012-04-23
Date Modified 2017-05-11
ID 192385
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