CIPP, a Novel Multivalent PDZ Domain Protein, Selectively Interacts with Kir4.0 Family Members, NMDA Receptor Subunits, Neurexins, and Neuroligins
Copyright policy )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.
- St. Jude Children's Research Hospital United States
- University of Tennessee System United States
- University of Tennessee Health Science Center United States
Brain Chemistry, Patch-Clamp Techniques, Potassium Channels, Cell Adhesion Molecules, Neuronal, Molecular Sequence Data, Neuropeptides, Membrane Proteins, Nerve Tissue Proteins, Kidney, Protein Structure, Tertiary, Mice, Receptors, Kainic Acid, COS Cells, Animals, Receptors, AMPA, Cloning, Molecular, Potassium Channels, Inwardly Rectifying, Carrier Proteins, Glycoproteins, Protein Binding
Brain Chemistry, Patch-Clamp Techniques, Potassium Channels, Cell Adhesion Molecules, Neuronal, Molecular Sequence Data, Neuropeptides, Membrane Proteins, Nerve Tissue Proteins, Kidney, Protein Structure, Tertiary, Mice, Receptors, Kainic Acid, COS Cells, Animals, Receptors, AMPA, Cloning, Molecular, Potassium Channels, Inwardly Rectifying, Carrier Proteins, Glycoproteins, Protein Binding
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