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• W2085908732 abstract "The σ-1 receptor is a widely expressed protein that interacts with a variety of ion channels, including the acid-sensing ion channel (ASIC) 1a. Here we used atomic force microscopy to determine the architecture of the ASIC1a/σ-1 receptor complex. When isolated His8-tagged ASIC1a was imaged in complex with anti-His6 antibodies, the angle between pairs of bound antibodies was 135°, consistent with the known trimeric structure of the channel. When ASIC1a was coexpressed with FLAG/His6-tagged σ-1 receptor, ASIC1a became decorated with small particles, and pairs of these particles bound at an angle of 131°. When these complexes were incubated with anti-FLAG antibodies, pairs of antibodies bound at an angle of 134°, confirming that the small particles were σ-1 receptors. Of interest, we found that the σ-1 receptor ligand haloperidol caused an ∼50% reduction in ASIC1a/σ-receptor binding, suggesting a way in which σ-1 ligands might modulate channel properties. For the first time, to our knowledge, we have resolved the structure of a complex between the σ-1 receptor and a target ion channel, and demonstrated that the stoichiometry of the interaction is 1 σ-1 receptor/1 ASIC1a subunit." @default.
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• W2085908732 date "2010-04-01" @default.
• W2085908732 modified "2023-09-28" @default.
• W2085908732 title "Demonstration of a Direct Interaction between σ-1 Receptors and Acid-Sensing Ion Channels" @default.
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• W2085908732 doi "https://doi.org/10.1016/j.bpj.2009.12.4293" @default.
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