FIGURE 1.

The ER-associated degradation of αENaC but not β- or γENaC is facilitated by the ER resident molecular chaperone Lhs1. A, cycloheximide chase reactions were performed as described under “Experimental Procedures” in LHS1 (filled circles) or Δlhs1 (open circles) yeast strains expressing a C-terminally HA epitope-tagged form of α-, β-, or γENaC. Chase reactions were performed at 37 °C, and lysates were immunoblotted with anti-HA antisera (ENaC) and with anti-G6P as a loading control. Data represent the means of 3–7 experiments, ±S.E. *, p < 0.05; **, p < 0.001. B, LHS1 and Δlhs1 yeast were grown to log phase, and proteins were precipitated as described under “Experimental Procedures” and immunoblotted with both anti-Lhs1 and anti-G6P antisera.