CRIPT, a novel postsynaptic protein that binds to the third PDZ domain of PSD-95/SAP90.

The synaptic protein PSD-95/SAP90 binds to and clusters a variety of membrane proteins via its two N-terminal PDZ domains. We report a novel protein, CRIPT, which is highly conserved from mammals to plants and binds selectively to the third PDZ domain (PDZ3) of PSD-95 via its C terminus. While conforming ...
to the consensus PDZ-binding C-terminal sequence (X-S/T-X-V-COOH), residues at the -1 position and upstream of the last four amino acids of CRIPT determine its specificity for PDZ3. In heterologous cells, CRIPT causes a redistribution of PSD-95 to microtubules. In brain, CRIPT colocalizes with PSD-95 in the postsynaptic density and can be coimmunoprecipitated with PSD-95 and tubulin. These findings suggest that CRIPT may regulate PSD-95 interaction with a tubulin-based cytoskeleton in excitatory synapses.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Animals, Arabidopsis, Arabidopsis Proteins, Binding Sites, Brain, Caenorhabditis, Caenorhabditis elegans Proteins, Carrier Proteins, Cells, Cultured, Cloning, Molecular, Consensus Sequence, Guanylate Kinase, Hippocampus, Humans, Immunohistochemistry, Intracellular Signaling Peptides and Proteins, Male, Membrane Proteins, Molecular Sequence Data, Nerve Tissue Proteins, Neurons, Rats, Rats, Sprague-Dawley, Recombinant Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Synapses, Synaptosomes, Tumor Suppressor Proteins
Neuron
Date: Apr. 01, 1998
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