Background: Extracellular acidification promotes structural rearrangements in the ectodomain of ASIC1a that result in activation and desensitization. Results: Glu-79 and Glu-416 cooperatively facilitate proton gating. The lower palm domain contracts upon extracellular acidification.
Conclusion:The lower palm domain mediates conformational changes that drive pore opening and closing events. Significance: This study provides insight into the molecular mechanism of gating of epithelial sodium/degenerin channels.
Background:The mechanisms of ion selectivity and permeation of acid-sensing ion channels are not solved. Results: Substitutions at selected sites altered cation discrimination. Conclusion: Ion selectivity is achieved by discrimination of ions on the basis of size and by selective coordination at restricted sites in the pore of ASIC1a. Significance: Elucidating the mechanisms of ion permeation and selectivity of ASIC1a is important to understand its function and physiological role.
Our previous FRET and functional studies suggest AKAP (A-kinase-anchoring-protein) 79/150 to be crucial in modulation of ion channel activity and neuronal function, by orchestrating important molecules such as protein kinases, phosphatases, G protein-coupled receptors and ion channels into signaling complexes in the plasma membrane. In this study, to directly visualize these AKAP79/150 signaling complexes and interactions between AKAP79/150, ion channels and receptors in sympathetic neurons, we utilized stochastic optical reconstruction microscopy (STORM) with sub-diffraction (~20 nm half width) resolution. STORM uses dyes that can cycle between a dark and a fluorescent state thousands of times, thus enabling detection of the precise localization of the center of these scattered spots given by cumulative integration of each cycle. Consistent with previous immunostaining/confocal studies, STORM imaging of fixed Chinese hamster ovary (CHO) cells using fluores
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