Full Text Available
Note: Clicking the button above will open the full text document at the original institutional repository in a new window.
Structure-Function Analysis of a Neuron-Specific Vesicular ATPase in Neurotransmission
Neurotransmission is central to neuronal communication, through which information is processed, stored, and retrieved. The vesicular ATPase (V-ATPase) protein is a proton pump that is implicated in neurotransmission. It acidifies synaptic vesicles to be consequently loaded with neurotransmitters pri...
Saved in:
| Main Author: | |
|---|---|
| Format: | Thesis |
| Published: |
AUC Knowledge Fountain
2012
|
| Subjects: | |
| Tags: |
No Tags, Be the first to tag this record!
|
| Summary: | Neurotransmission is central to neuronal communication, through which information is processed, stored, and retrieved. The vesicular ATPase (V-ATPase) protein is a proton pump that is implicated in neurotransmission. It acidifies synaptic vesicles to be consequently loaded with neurotransmitters prior to release through exocytosis. V100 is a neuron-specific vesicular ATPase subunit a1, and it is a major subunit that determines where the vesicular ATPase functions intracellularly. Previous studies characterized two putative functions for the V100 in neuronal cell biology; intracellular vesicle acidification, and membrane fusion. In this project, we set out to dissect the function of V100 genetically - using immunolabeling and electrophysiology- to understand acidification-dependent and -independent functions. The results cast some light on a potential regulation of the V100 by Ca2+/Calmodulin. This regulatory mechanism may be specifically required for spontaneous vesicle release independent of the proton pump function of the V-ATPase. |
|---|