Referenced in: none

Automatically associated channels: KChIP1 , Kv1.4 , Kv3.1 , Kv4.2

Title: Evidence showing an intermolecular interaction between KChIP proteins and Taiwan cobra cardiotoxins.

Authors: Ya-Ling Lin, Shinne-Ren Lin, Tony T Wu, Long-Sen Chang

Journal, date & volume: Biochem. Biophys. Res. Commun., 2004 Jul 2 , 319, 720-4

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/15184042

Abstract
Direct protein-protein interaction between Taiwan cobra cardiotoxin3 (CTX3) and potassium channel-interacting proteins (KChIPs) was investigated in the present study. It was found that KChIPs bound with CTX3, in which KChIP and CTX3 formed a 1:1 complex as evidenced by the results of chemical cross-linking. Pull-down assay revealed that the intact EF-hands 3 and 4 of KChIP1 were critical for CTX3-binding. Likewise, removal of EF-hands 3 and 4 distorted the ability of KChIP1 to bind with Kv4.2 N-terminal fragment (KvN) as well as fluorescent probe 8-anilinonaphthalene-1-sulfonate (ANS). In contrast to the interaction between KChIP1 and KvN, the binding of CTX3 to KChIP1 showed a Ca(2+)-independent manner. Fluorescence measurement revealed that CTX3 affected the binding of ANS to Ca(2+)-bound KChIP1, but not Ca(2+)-free KChIP1. Alternatively, KChIP1 simultaneously bound with KvN and CTX3, and the interaction between KChIP1 and KvN was enhanced by CTX3. In terms of the fact that KChIPs regulate the electrophysiological properties of Kv K(+) channel, the potentiality of CTX for this biomedical application could be considered.