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

Biochem Biophys Res Commun. 2003 Oct 31;310(4):1140-7. doi: 10.1016/j.bbrc.2003.09.133.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • CHO Cells
  • Cricetinae
  • Disks Large Homolog 4 Protein
  • Guanylate Kinases
  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins
  • Mice
  • Molecular Sequence Data
  • Neocortex / metabolism
  • Nerve Tissue Proteins / chemistry
  • Nerve Tissue Proteins / metabolism*
  • Potassium Channels / chemistry
  • Potassium Channels / metabolism*
  • Potassium Channels, Sodium-Activated
  • Protein Binding
  • Sequence Homology, Amino Acid
  • Sodium / metabolism*

Substances

  • Disks Large Homolog 4 Protein
  • Dlg4 protein, mouse
  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins
  • Nerve Tissue Proteins
  • Potassium Channels
  • Potassium Channels, Sodium-Activated
  • Slo2 protein, mouse
  • postsynaptic density proteins
  • Sodium
  • Guanylate Kinases