An interaction domain in Slob necessary for its binding to the slowpoke calcium-dependent potassium channel

Abstract

Slob modulates the activity of the Drosophila Slowpoke calcium-dependent potassium channel (dSlo) via its direct binding to the channel. To characterize the molecular detail of the protein–protein interaction between Slob and dSlo, we constructed a series of Slob mutants that are progressively truncated at either the carboxyl or amino terminal end, and examined the binding of these Slob mutants to dSlo using a co-immunoprecipitation approach. Our data suggest that a small region of 42 amino acids (residues 191–233) in Slob is essential for Slob to interact with the dSlo channel.