Semaphorin4F interacts with the synapse-associated protein SAP90/PSD-95.

Semaphorins are a family of secreted and membrane-associated proteins involved in growth cone guidance during development. Here, we describe the interaction of Semaphorin4F (Sema4F) with the post-synaptic density protein SAP90/PSD-95. Using the yeast two-hybrid system and coprecipitation assays we were able to show an interaction between the extreme C-terminus of ...
Sema4F and the PDZ domains of SAP90/PSD-95. Heterologous coexpression of a chimeric EphrinB1/Semaphorin4F protein with SAP90/PSD-95 in COS cells leads to translocation of SAP90/PSD-95 from the cytosol to the membrane. Deletion analysis shows that this translocation activity of Sema4F is completely dependent on the presence of the last three C-terminal amino acids. In addition, Sema4F immunoreactivity is present in synaptosome fractions and enriched in post-synaptic density fractions. Consistently, in cultured hippocampal neurons, we demonstrate punctate colocalization of Sema4F and SAP90/PSD-95 in dendrites, furthermore we found colocalization of Sema4F with synapsin1 suggesting a synaptic localization. Our data implicate a new functional context for semaphorins at glutamatergic synapses.
Mesh Terms:
Amino Acid Sequence, Animals, COS Cells, Carrier Proteins, Cell Fractionation, Cells, Cultured, Ephrin-B1, Hippocampus, Humans, Membrane Proteins, Microscopy, Fluorescence, Molecular Sequence Data, Nerve Growth Factors, Nerve Tissue Proteins, Neurons, Protein Structure, Tertiary, Rats, Rats, Wistar, Recombinant Fusion Proteins, Sequence Alignment, Transfection, Two-Hybrid System Techniques
J. Neurochem.
Date: Aug. 01, 2001
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