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Updated: Aug 30, 2026

Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes
Published on: January 10, 2011
An interaction domain in Slob necessary for its binding to the slowpoke calcium-dependent potassium channel
Yi Zhou1, Hong Fei, Irwin B Levitan
1Department of Neuroscience, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. yzhou@nrc.uab.edu
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.
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