Densin-180 interacts with delta-catenin/neural plakophilin-related armadillo repeat protein at synapses.
Densin-180, a protein purified from the postsynaptic density fraction of the rat forebrain, is the founding member of a newly described family of proteins termed the LAP (leucine-rich repeats and PSD-95/Dlg-A/ZO-1 (PDZ) domains) family that plays essential roles in establishment of cell polarity. To identify Densin-180-binding proteins, we screened a ... yeast two-hybrid library using the carboxyl-terminal fragment of Densin-180 containing PDZ domain as bait, and we isolated delta-catenin/neural plakophilin-related armadillo repeat protein (NPRAP) as a Densin-180-interacting protein. delta-catenin/NPRAP, a member of the armadillo repeat family, is a nervous system-specific adherens junction protein originally discovered as an interactor with presenilin-1, a protein involved in Alzheimer's disease. Densin-180 PDZ domain binds the COOH terminus of delta-catenin/NPRAP containing the PDZ domain-binding sequence. Endogenous Densin-180 was co-immunoprecipitated with delta-catenin/NPRAP and N-cadherin. Although Densin-180 was reported to be a transmembrane protein, Densin-180 was not accessible to surface biotinylation in dissociated hippocampal neurons; hence Densin-180 may be a cytosolic protein. Densin-180 co-localized with delta-catenin/NPRAP at synapses in delta-catenin/NPRAP and may be involved in organization of the synaptic cell-cell junction through interaction with the delta-catenin/NPRAP-N-cadherin complex.
Mesh Terms:
Animals, Armadillo Domain Proteins, Biotinylation, Brain, Cadherins, Catenins, Cell Adhesion Molecules, Cell Membrane, Cells, Cultured, Cloning, Molecular, Cytoskeletal Proteins, Cytosol, DNA, Complementary, Gene Library, Hippocampus, Humans, Immunoblotting, Microscopy, Fluorescence, Molecular Sequence Data, Nerve Tissue Proteins, Neurons, Phosphoproteins, Precipitin Tests, Protein Binding, Protein Biosynthesis, Protein Structure, Tertiary, Rats, Recombinant Fusion Proteins, Recombinant Proteins, Sialoglycoproteins, Synapses, Transfection, Two-Hybrid System Techniques
Animals, Armadillo Domain Proteins, Biotinylation, Brain, Cadherins, Catenins, Cell Adhesion Molecules, Cell Membrane, Cells, Cultured, Cloning, Molecular, Cytoskeletal Proteins, Cytosol, DNA, Complementary, Gene Library, Hippocampus, Humans, Immunoblotting, Microscopy, Fluorescence, Molecular Sequence Data, Nerve Tissue Proteins, Neurons, Phosphoproteins, Precipitin Tests, Protein Binding, Protein Biosynthesis, Protein Structure, Tertiary, Rats, Recombinant Fusion Proteins, Recombinant Proteins, Sialoglycoproteins, Synapses, Transfection, Two-Hybrid System Techniques
J. Biol. Chem.
Date: Feb. 15, 2002
PubMed ID: 11729199
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