Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein.
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").
Pubmed ID: 10225955 RIS Download
Alternative Splicing | Amino Acid Sequence | Animals | COS Cells | Cadherins | Calcium | Cell Adhesion Molecules | Cell Aggregation | Epithelial Cells | Intercellular Junctions | Kinesin | Membrane Glycoproteins | Mice | Microfilament Proteins | Microscopy, Electron | Myocardium | Myosins | Protein Structure, Tertiary | Rabbits | Receptors, Tumor Necrosis Factor | Receptors, Tumor Necrosis Factor, Member 14 | Receptors, Virus | Vinculin