Annexin II Light Chain p11 Promotes Functional Expression of Acid-sensing Ion Channel ASIC1a
| Autor: | Francois Rugiero, Kenji Okuse, Emmanuelle Donier, John N. Wood |
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| Rok vydání: | 2005 |
| Předmět: |
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Complementary Patch-Clamp Techniques Blotting Western Green Fluorescent Proteins Nerve Tissue Proteins CHO Cells G protein-gated ion channel Biology Transfection Biochemistry Sodium Channels Mice Dorsal root ganglion Cricetinae Ganglia Spinal Two-Hybrid System Techniques medicine Animals Immunoprecipitation Protein Isoforms Biotinylation Molecular Biology Annexin A2 Acid-sensing ion channel Ion channel Gene Library Glutathione Transferase Ions Mice Knockout Neurons Sodium channel Cell Membrane S100 Proteins Membrane Proteins Cell Biology Hydrogen-Ion Concentration Immunohistochemistry Molecular biology Potassium channel Protein Structure Tertiary Rats Cell biology Acid Sensing Ion Channels Electrophysiology Stretch-activated ion channel medicine.anatomical_structure Gene Expression Regulation Protein Binding |
| Zdroj: | Journal of Biological Chemistry. 280:38666-38672 |
| ISSN: | 0021-9258 |
| Popis: | Acid-sensing ion channels (ASICs) have been implicated in a wide variety of physiological functions. We have used a rat dorsal root ganglion cDNA library in a yeast two-hybrid assay to identify sensory neuron proteins that interact with ASICs. We found that annexin II light chain p11 physically interacts with the N terminus of ASIC1a, but not other ASIC isoforms. Immunoprecipitation studies confirmed an interaction between p11 and ASIC1 in rat dorsal root ganglion neurons in vivo. Coexpression of p11 and ASIC1a in CHO-K1 cells led to a 2-fold increase in expression of the ion channel at the cell membrane as determined by membrane-associated immunoreactivity and cell-surface biotinylation. Consistent with these findings, peak ASIC1a currents in transfected CHO-K1 cells were up-regulated 2-fold in the presence of p11, whereas ASIC3-mediated currents were unaffected by p11 expression. Neither the pH dependence of activation nor the rates of desensitization were altered by p11, suggesting that its primary role in regulating ASIC1a activity is to enhance cell-surface expression of ASIC1a. These data demonstrate that p11, already known to traffic members of the voltage-gated sodium and potassium channel families as well as transient receptor potential and chloride channels, also plays a selective role in enhancing ASIC1a functional expression. |
| Databáze: | OpenAIRE |
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