currents in oocytes expressing ASIC2aG430V or ASIC2aG430V+βENaC, which was further increased to approximately four-fold when γENaC or both β and γ subunits were co-expressed with ASIC2aG430V (ASIC2aG430V+γENaC or ASIC2aG430V+β/γENaC). Exposure to acidic pH evoked greater channel activity in oocytes expressing ASIC2aG430V+β/γENaC than ASIC2aG430V alone. In contrast, ENaC β and γ subunits did not alter the channel's permeability to monovalent cations of different sizes. Collectively, our experimental findings and structural modeling suggest that ASIC2a assembles with ENaC β and γ subunits to form mechanosensitive channels.
Shi et al. (Fri,) studied this question.
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