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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. Slo2 sodium-activated K+ channels bind to the PDZ domain of PSD-95. Uchino, S., Wada, H., Honda, S., Hirasawa, T., Yanai, S., Nakamura, Y., Ondo, Y., Kohsaka, S. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
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