Microtubule binding by CRIPT and its potential role in the synaptic clustering of PSD-95

Nat Neurosci. 1999 Dec;2(12):1063-9. doi: 10.1038/15990.

Abstract

CRIPT is a postsynaptic protein that binds selectively to the third PDZ domain (PDZ3) of PSD-95. Here we show that CRIPT also binds directly to microtubules, thereby linking PSD-95 to the microtubule cytoskeleton. Disrupting the CRIPT-PSD-95 interaction in cultured hippocampal neurons with a PDZ3-specific peptide prevented the association of PSD-95 with microtubules and inhibited the synaptic clustering of PSD-95, chapsyn-110/PSD-93 and GKAP (a PSD-95-binding protein). However, the number of synapses and the synaptic clustering of NMDA receptors were unaffected, suggesting that PSD-95-family proteins are not essential for the maintenance of synapses and the synaptic localization of NMDA receptors.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Amino Acid Substitution
  • Animals
  • COS Cells
  • Calcium-Calmodulin-Dependent Protein Kinases*
  • Carrier Proteins / antagonists & inhibitors
  • Carrier Proteins / chemistry
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Cells, Cultured
  • Guanylate Kinases
  • Hippocampus / cytology
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Microtubule-Associated Proteins / metabolism
  • Microtubules / drug effects
  • Microtubules / metabolism*
  • Molecular Sequence Data
  • Nerve Tissue Proteins / antagonists & inhibitors
  • Nerve Tissue Proteins / chemistry
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / metabolism*
  • Neurons / cytology
  • Neurons / drug effects
  • Neurons / enzymology
  • Neurons / metabolism
  • Nucleoside-Phosphate Kinase / antagonists & inhibitors
  • Nucleoside-Phosphate Kinase / metabolism
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • Peptide Fragments / pharmacology
  • Receptors, N-Methyl-D-Aspartate / metabolism
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / metabolism
  • Recombinant Fusion Proteins / pharmacology
  • SAP90-PSD95 Associated Proteins
  • Synapses / drug effects
  • Synapses / enzymology
  • Synapses / metabolism*
  • Synaptophysin / metabolism

Substances

  • Carrier Proteins
  • Membrane Proteins
  • Microtubule-Associated Proteins
  • Nerve Tissue Proteins
  • Peptide Fragments
  • Receptors, N-Methyl-D-Aspartate
  • Recombinant Fusion Proteins
  • SAP90-PSD95 Associated Proteins
  • Synaptophysin
  • postsynaptic density proteins
  • CASK kinases
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Nucleoside-Phosphate Kinase
  • Guanylate Kinases