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Auxiliary subunits are often needed to tailor K +  channel functional properties and expression levels. Many auxiliary subunits have been identified for mammalian Slo1, a high-conductance K +  channel gated by voltage and Ca 2+ . Experiments with heterologous expression systems show that some of the identified Slo1 auxiliary subunits can also regulate other Slo K +  channels. However, it is unclear whether a single auxiliary subunit may regulate more than one Slo channel in native tissues. BKIP-1, an auxiliary subunit of  C. elegans  SLO-1, facilitates SLO-1 membrane trafficking and regulates SLO-1 function in neurons and muscle cells. Here we show that BKIP-1 also serves as an auxiliary subunit of  C. elegans  SLO-2, a high-conductance K +  channel gated by membrane voltage and cytosolic Cl −  and Ca 2+ . Comparisons of whole-cell and single-channel SLO-2 currents in native neurons and muscle cells between worm strains with and without BKIP-1 suggest that BKIP-1 reduces chloride sensitivity, activation rate, and single-channel open probability of SLO-2. Bimolecular fluorescence complementation assays indicate that BKIP-1 interacts with SLO-2 carboxyl terminal. Thus, BKIP-1 may serve as an auxiliary subunit of SLO-2. BKIP-1 appears to be the first example that a single auxiliary subunit exerts opposite effects on evolutionarily related channels in the same cells.

BKIP-1, an auxiliary subunit critical to SLO-1 function, inhibits SLO-2 potassium channel in vivo