Characterization of SynCAM surface trafficking using a SynCAM derived ligand with high homophilic binding affinity
- Resource Type
- Authors
- Daniel Choquet; Olivier Thoumine; Christelle Breillat
- Source
- Biochemical and Biophysical Research Communications. 359:655-659
- Subject
- Stereochemistry
Biophysics
Immunoglobulins
Plasma protein binding
Hippocampal formation
Ligands
Sensitivity and Specificity
Biochemistry
Rats, Sprague-Dawley
Extracellular
Animals
Humans
Receptors, Immunologic
Receptor
Molecular Biology
Cells, Cultured
Chemistry
Membrane Proteins
Cell Biology
Transfection
Ligand (biochemistry)
Fusion protein
Rats
Transport protein
Protein Transport
Solubility
Synapses
Protein Binding
- Language
- ISSN
- 0006-291X
In order to better probe SynCAM function in neurons, we produced a fusion protein between the extracellular domain of SynCAM1 and the constant fragment of human IgG (SynCAM-Fc). Whether in soluble form or immobilized on latex microspheres, the chimera bound specifically to the surface of hippocampal neurons and recruited endogenous SynCAM molecules. SynCAM-Fc was also used in combination with Quantum Dots to follow the mobility of transfected SynCAM receptors at the neuronal surface. Both immobile and highly mobile SynCAM were found. Thus, SynCAM-Fc behaves as a high affinity ligand that can be used to study the function of SynCAM at the neuronal membrane.