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Molecular genetic analysis of an int...
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Sandoval, Gisela Maria Rodriguez.
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Molecular genetic analysis of an interaction between the vesicular acetylcholine transporter and synaptobrevin in Caenorhabditis elegans.
紀錄類型:
書目-電子資源 : Monograph/item
正題名/作者:
Molecular genetic analysis of an interaction between the vesicular acetylcholine transporter and synaptobrevin in Caenorhabditis elegans./
作者:
Sandoval, Gisela Maria Rodriguez.
面頁冊數:
248 p.
附註:
Source: Dissertation Abstracts International, Volume: 65-05, Section: B, page: 2282.
Contained By:
Dissertation Abstracts International65-05B.
標題:
Biology, Neuroscience. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3131980
ISBN:
0496792202
Molecular genetic analysis of an interaction between the vesicular acetylcholine transporter and synaptobrevin in Caenorhabditis elegans.
Sandoval, Gisela Maria Rodriguez.
Molecular genetic analysis of an interaction between the vesicular acetylcholine transporter and synaptobrevin in Caenorhabditis elegans.
- 248 p.
Source: Dissertation Abstracts International, Volume: 65-05, Section: B, page: 2282.
Thesis (Ph.D.)--Harvard University, 2004.
Motor function in C. elegans is controlled primarily by the excitatory neurotransmitter acetylcholine. Choline acetyltransferase (ChAT) encoded by the cha-1 gene synthesizes acetylcholine, which is transported into synaptic vesicles by the vesicular acetylcholine transporter (VAChT) encoded by unc-17. Function of these genes is essential for synaptic transmission since null mutations in either gene is lethal. Mutants with residual unc-17 gene function are uncoordinated, slow growing, small, and are resistant to cholinesterase inhibitors. The packaging of transmitter into vesicles is required for release of acetylcholine into the synaptic cleft.
ISBN: 0496792202Subjects--Topical Terms:
1017680
Biology, Neuroscience.
Molecular genetic analysis of an interaction between the vesicular acetylcholine transporter and synaptobrevin in Caenorhabditis elegans.
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Source: Dissertation Abstracts International, Volume: 65-05, Section: B, page: 2282.
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Motor function in C. elegans is controlled primarily by the excitatory neurotransmitter acetylcholine. Choline acetyltransferase (ChAT) encoded by the cha-1 gene synthesizes acetylcholine, which is transported into synaptic vesicles by the vesicular acetylcholine transporter (VAChT) encoded by unc-17. Function of these genes is essential for synaptic transmission since null mutations in either gene is lethal. Mutants with residual unc-17 gene function are uncoordinated, slow growing, small, and are resistant to cholinesterase inhibitors. The packaging of transmitter into vesicles is required for release of acetylcholine into the synaptic cleft.
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Suppressors of the locomotory defect of non-null mutant unc-17 (e245) may enable the elucidation of transport function and isolation of components that interact with vesicular transport and that may participate in the regulation of transmitter release. We have isolated three suppressors of unc-17 (e245) that are linked to chromosome III. We have also identified an intragenic suppressor of unc-17 (e245), unc-17 (mg301), that changes the mutant arginine in unc-17 (e245) to a lysine.
520
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sup-8 (e1563) suppresses the movement defects of unc-17 (e245) but not other unc-17 alleles. We found that sup-8 corresponds to a dominant allele of synaptobrevin (snb-1). sup-8 (e1563) is an isoleucine to aspartate substitution in the single transmembrane domain of synaptobrevin. We find that while overexpressing UNC-17/VAChT facilitates synaptic transmission the mutant synaptobrevin does not.
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Staining of UNC-17 in unc-17 (e245) mutants shows decreased protein levels that are restored by snb-1 (e1563). Genetic analyses demonstrate that the interaction of these two proteins allows for the restoration of unc-17 (e245) function and further suggest that this restoration is due to the charged amino acid found in the SNB-1 transmembrane domain. The importance of this amino acid and its placement is further indicated by the partial restoration of function by transgenic expression of only the transmembrane domain of synaptobrevin bearing the isoleucine to aspartate substitution or by a similar substitution in another vesicular protein, synaptotagmin. Finally, the physical interaction of UNC-17/VAChT and SNB-1 is demonstrated by the co-immunoprecipitation of the two proteins from detergent mammalian cell lysates. This study provides the first link between neurotransmitter vesicular transport and synaptic vesicle fusion.
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School code: 0084.
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http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3131980
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