The amino terminus of Slob, Slowpoke channel binding protein, critically influences its modulation of the channel.

ABSTRACT: The Drosophila Slowpoke calcium-dependent potassium channel (dSlo) binding protein Slob was discovered by a yeast two-hybrid screen using the carboxy-terminal tail region of dSlo as bait. Slob binds to and modulates the dSlo channel. We have found that there are several Slob proteins, resulting from multiple translational start sites and alternative splicing, and have named them based on their molecular weights (in kD). The larger variants, which are initiated at the first translational start site and are called Slob71 and Slob65, shift the voltage dependence of dSlo activation, measured by the whole cell conductance-voltage relationship, to the left (less depolarized voltages). Slob53 and Slob47, initiated at the third translational start site, also shift the dSlo voltage dependence to th

SUBMITTER: Zeng H 

PROVIDER: S-EPMC2234080 | biostudies-literature | 2005 Jun

REPOSITORIES: biostudies-literature