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

  • Niethammer M
  • Valtschanoff J
  • Kapoor T
 et al. 
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Abstract

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.

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Authors

  • Martin Niethammer

  • Juli G. Valtschanoff

  • Tarun M. Kapoor

  • Daniel W. Allison

  • Richard J. Weinberg

  • Ann Marie Craig

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