Semaphorin 4B interacts with the post-synaptic density protein PSD-95/SAP90 and is recruited to synapses through a C-terminal PDZ-binding motif

FEBS Lett. 2005 Jul 4;579(17):3821-8. doi: 10.1016/j.febslet.2005.05.079.

Abstract

The semaphorins are a large family of proteins that act as guidance signals for axons and dendrites. The class 4 semaphorins are integral membrane proteins that are widely expressed throughout the nervous system. Here, we show that a subclass of these semaphorins is characterized by a PDZ-binding motif at their carboxy-terminus. This sequence mediates the interaction with the post-synaptic density protein PSD-95/SAP90. Co-expression of Sema4B with PSD-95 in COS 7 cells results in the clustering of Sema4B. Sema4B co-localizes with PSD-95 at synaptic contacts between cultured hippocampal neurons. This synaptic localization depends on the presence of the PDZ-binding motif.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Animals
  • COS Cells
  • Chlorocebus aethiops
  • Disks Large Homolog 4 Protein
  • Guanylate Kinases
  • Hippocampus / cytology
  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins
  • Mice
  • Nerve Tissue Proteins / analysis
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / metabolism*
  • Neurons / metabolism
  • Protein Structure, Tertiary
  • SAP90-PSD95 Associated Proteins
  • Semaphorins / analysis
  • Semaphorins / chemistry*
  • Semaphorins / metabolism*
  • Synapses / chemistry
  • Synapses / metabolism*

Substances

  • Disks Large Homolog 4 Protein
  • Dlg4 protein, mouse
  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins
  • Nerve Tissue Proteins
  • SAP90-PSD95 Associated Proteins
  • Semaphorins
  • postsynaptic density proteins
  • Guanylate Kinases