Referenced in: none

Automatically associated channels: Slo1 , Slo2

Title: Slo2 sodium-activated K+ channels bind to the PDZ domain of PSD-95.

Authors: Shigeo Uchino, Hidenori Wada, Shizuyo Honda, Takae Hirasawa, Shigeki Yanai, Yasuko Nakamura, Yumiko Ondo, Shinichi Kohsaka

Journal, date & volume: Biochem. Biophys. Res. Commun., 2003 Oct 31 , 310, 1140-7

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/14559234

Abstract
Slo2 channels are a type of sodium-activated K+ channels and possess a typical PDZ binding motif at the carboxy-terminal end. Thus, we investigated whether Slo2 channels bind to PSD-95, because it is well known that other types of K+ channels, voltage-gated and inward rectifier K+ channels, bind to PSD-95 via the PDZ binding motif and are involved in excitatory synaptic transmission. By using an extract prepared from cultured neocortical neurons, we demonstrated a biochemical interaction between mSlo2 channels and PSD-95, and a mutational analysis revealed that mSlo2 channels bound to the first PDZ domain of PSD-95 via the PDZ binding motif. To investigate the expression of mSlo2 protein in primary neocortical neurons, we raised anti-mSlo2 channel antibody and immunostained neocortical neurons. The immunocytochemical study showed that mSlo2 channels partly colocalized with PSD-95 in mouse neocortical neurons.