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CIPP, a novel multivalent PDZ domain protein, selectively interacts with Kir4.0 family members, NMDA receptor subunits, neurexins, and neuroligins.

We report a novel multivalent PDZ domain protein, CIPP (for channel-interacting PDZ domain protein), which is expressed exclusively in brain and kidney. Within the brain, the highest CIPP mRNA levels were found in neurons of the cerebellum, inferior colliculus, vestibular nucleus, facial nucleus, and thalamus. Furthermore, we identified the inward rectifier K+ (Kir) channel, Kir4.1 (also called "Kir1.2"), as a cellular CIPP ligand. Among several other Kir channels tested, only the closely related Kir4.2 (or "Kir1.3") also interacted with CIPP. In addition, specific PDZ domains within CIPP associated selectively with the C-termini of N-methyl-D-aspartate subtypes of glutamate receptors, as well as neurexins and neuroligins, cell surface molecules enriched in synaptic membranes. Thus, CIPP may serve as a scaffold that brings structurally diverse but functionally connected proteins into close proximity at the synapse. The functional consequences of CIPP expression on Kir4.1 channels were studied using whole-cell voltage clamp techniques in Kir4.1 transfected COS-7 cells. On average, Kir4.1 current densities were doubled by cotransfection with CIPP.

Pubmed ID: 9647694

Authors

  • Kurschner C
  • Mermelstein PG
  • Holden WT
  • Surmeier DJ

Journal

Molecular and cellular neurosciences

Publication Data

June 23, 1998

Associated Grants

  • Agency: NCI NIH HHS, Id: P30 CA21765

Mesh Terms

  • Animals
  • Brain Chemistry
  • COS Cells
  • Carrier Proteins
  • Cell Adhesion Molecules, Neuronal
  • Cloning, Molecular
  • Glycoproteins
  • Kidney
  • Membrane Proteins
  • Mice
  • Molecular Sequence Data
  • Nerve Tissue Proteins
  • Neuropeptides
  • Patch-Clamp Techniques
  • Potassium Channels
  • Potassium Channels, Inwardly Rectifying
  • Protein Binding
  • Protein Structure, Tertiary
  • Receptors, AMPA
  • Receptors, Kainic Acid
  • Receptors, Metabotropic Glutamate
  • Receptors, N-Methyl-D-Aspartate
  • Sequence Homology, Amino Acid
  • Transfection