The Neural Cell Adhesion Molecule NCAM. Molecular Mechanism of Homophilic Binding.:Molecular Mechanism of Homophilic Binding
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概要
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The neural cell adhesion molecule NCAM is a member of the immunoglobulin (Ig)-superfamily of recognition molecules. NCAM is a multidomain molecule which can interact with a variety of ligands. NCAM is also capable of homophilic binding, which plays a crucial role in cell-cell adhesion. Recent studies have led to the identification of the homophilic binding site to a decapeptide sequence (243-KYSFNYDGSE-252) in the third Ig-like domain of chick NCAM. This sequence corresponds to the C' β-strand and the subsequent turn structure in the predicted Ig fold. Mutational analysis indicates that the aromatic residues Tyr-244 and Phe-246, as well as the charged residues Lys-243 and Asp-249, are crucial to NCAM-NCAM binding. Further studies have shown that recombinant Ig-like domain 3 of NCAM can undergo homophilic binding, which isabolished when mutations are introduced into this decapeptide bi nding site. These results are consistent with the model that the NCAM homophilic binding site interacts isologously with the same sequence on apposing molecules. The integrity of its homophilic binding site is an absolute requirement for NCAM localization in intercellular contact regions. NCAM homophilic binding also triggers a signaling pathway that promotes neurite extension from a number of primary neurons. Thus, the NCAM homophilic binding site plays a key role not only in cell-cell contact formation but also in neurite outgrowth.
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