PMID:10225955

Citation	Takahashi, K, Nakanishi, H, Miyahara, M, Mandai, K, Satoh, K, Satoh, A, Nishioka, H, Aoki, J, Nomoto, A, Mizoguchi, A and Takai, Y (1999) Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein. J. Cell Biol. 145:539-49
Abstract	We have isolated a novel actin filament-binding protein, named afadin, localized at cadherin-based cell-cell adherens junctions (AJs) in various tissues and cell lines. Afadin has one PDZ domain, three proline-rich regions, and one actin filament-binding domain. We found here that afadin directly interacted with a family of the immunoglobulin superfamily, which was isolated originally as the poliovirus receptor-related protein (PRR) family consisting of PRR1 and -2, and has been identified recently to be the alphaherpes virus receptor. PRR has a COOH-terminal consensus motif to which the PDZ domain of afadin binds. PRR and afadin were colocalized at cadherin-based cell-cell AJs in various tissues and cell lines. In E-cadherin-expressing EL cells, PRR was recruited to cadherin-based cell-cell AJs through interaction with afadin. PRR showed Ca2+-independent cell-cell adhesion activity. These results indicate that PRR is a cell-cell adhesion molecule of the immunoglobulin superfamily which is recruited to cadherin-based cell-cell AJs through interaction with afadin. We rename PRR as nectin (taken from the Latin word "necto" meaning "to connect").
Links	PubMed PMC2185068
Keywords	Alternative Splicing/genetics; Amino Acid Sequence; Animals; COS Cells/chemistry; COS Cells/metabolism; Cadherins/metabolism; Calcium/metabolism; Cell Adhesion Molecules/chemistry; Cell Adhesion Molecules/genetics; Cell Adhesion Molecules/metabolism; Cell Aggregation/physiology; Epithelial Cells/chemistry; Epithelial Cells/cytology; Epithelial Cells/metabolism; Intercellular Junctions/chemistry; Intercellular Junctions/metabolism; Intercellular Junctions/ultrastructure; Kinesin; Membrane Glycoproteins/chemistry; Membrane Glycoproteins/genetics; Membrane Glycoproteins/metabolism; Mice; Microfilament Proteins/chemistry; Microfilament Proteins/metabolism; Microscopy, Electron; Myocardium/chemistry; Myocardium/cytology; Myocardium/metabolism; Myosins; Protein Structure, Tertiary; Rabbits; Receptors, Tumor Necrosis Factor; Receptors, Tumor Necrosis Factor, Member 14; Receptors, Virus; Vinculin/metabolism
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