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

Yi Zhou; Hong Fei; Irwin B Levitan

doi:10.1016/s0028-3908(03)00285-5

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

Neuropharmacology. 2003 Nov;45(6):714-9. doi: 10.1016/s0028-3908(03)00285-5.

Authors

Yi Zhou¹, Hong Fei, Irwin B Levitan

Affiliation

¹ Department of Neuroscience, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. yzhou@nrc.uab.edu

PMID: 14529710
DOI: 10.1016/s0028-3908(03)00285-5

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.

Publication types

Research Support, U.S. Gov't, P.H.S.

MeSH terms

Animals
Cell Line
Drosophila Proteins / genetics
Drosophila Proteins / metabolism*
Humans
Large-Conductance Calcium-Activated Potassium Channel alpha Subunits
Large-Conductance Calcium-Activated Potassium Channels
Mutation
Potassium Channels / genetics
Potassium Channels / metabolism*
Potassium Channels, Calcium-Activated / genetics
Potassium Channels, Calcium-Activated / metabolism*
Protein Binding / physiology
Protein Structure, Tertiary / genetics

Substances

Drosophila Proteins
KCNMA1 protein, human
Large-Conductance Calcium-Activated Potassium Channel alpha Subunits
Large-Conductance Calcium-Activated Potassium Channels
Potassium Channels
Potassium Channels, Calcium-Activated
Slob protein, Drosophila