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© The Rockefeller University Press, 0021-9525/1999//539 $5.00
The Journal of Cell Biology, Volume 145, Number 3, , 1999 539-549

Nectin/PRR: An Immunoglobulin-like Cell Adhesion Molecule Recruited to Cadherin-based Adherens Junctions through Interaction with Afadin, a PDZ Domain–containing Protein

Kenichi Takahashi^*, Hiroyuki Nakanishi^*, Masako Miyahara^*, Kenji Mandai^*, Keiko Satoh^*, Ayako Satoh^*, Hideo Nishioka^*, Junken Aoki, Akio Nomoto, Akira Mizoguchi, and Yoshimi Takai^*,||

^* Takai Biotimer Project, ERATO, Japan Science and Technology Corp., c/o JCR Pharmaceuticals Co., Ltd., Kobe 651-2241, Japan; Department of Microbiology, Tokyo Metropolitan Institute of Medical Science, Tokyo 113-0033, Japan; Department of Anatomy and Neurobiology, Faculty of Medicine, Kyoto University, Kyoto 606-8501, Japan; and ^|| Department of Molecular Biology and Biochemistry, Osaka University Medical School, Suita 565-0871, Japan

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").

Key Words: afadin • cadherin • poliovirus receptor– related protein • immunoglobulin superfamily • zonula adherens

Abbreviations used in this paper: AJs, adherens junctions; CAM, cell adhesion molecule; F-actin, actin filament; GST, glutathione S-transferase; PRR, poliovirus receptor–related protein; ZA, zonula adherens; ZO, zonula occludens.

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• Lui, W.-Y., Mruk, D. D., Lee, W. M., Cheng, C. Y. (2003). Adherens Junction Dynamics in the Testis and Spermatogenesis. J Androl 24: 1-14 [Full Text]  
• Takai, Y., Nakanishi, H. (2003). Nectin and afadin: novel organizers of intercellular junctions. J. Cell Sci. 116: 17-27 [Abstract] [Full Text]  
• Kawakatsu, T., Shimizu, K., Honda, T., Fukuhara, T., Hoshino, T., Takai, Y. (2002). trans-Interactions of Nectins Induce Formation of Filopodia and Lamellipodia through the Respective Activation of Cdc42 and Rac Small G Proteins. J. Biol. Chem. 277: 50749-50755 [Abstract] [Full Text]  
• Kim, D. Y., Ingano, L. A. M., Kovacs, D. M. (2002). Nectin-1alpha , an Immunoglobulin-like Receptor Involved in the Formation of Synapses, Is a Substrate for Presenilin/gamma -Secretase-like Cleavage. J. Biol. Chem. 277: 49976-49981 [Abstract] [Full Text]  
• Gosselin, A.-S., Simonin, Y., Guivel-Benhassine, F., Rincheval, V., Vayssiere, J.-L., Mignotte, B., Colbere-Garapin, F., Couderc, T., Blondel, B. (2002). Poliovirus-Induced Apoptosis Is Reduced in Cells Expressing a Mutant CD155 Selected during Persistent Poliovirus Infection in Neuroblastoma Cells. J. Virol. 77: 790-798 [Abstract] [Full Text]  
• Struyf, F., Martinez, W. M., Spear, P. G. (2002). Mutations in the N-Terminal Domains of Nectin-1 and Nectin-2 Reveal Differences in Requirements for Entry of Various Alphaherpesviruses and for Nectin-Nectin Interactions. J. Virol. 76: 12940-12950 [Abstract] [Full Text]  
• Cheng, C. Y., Mruk, D. D. (2002). Cell Junction Dynamics in the Testis: Sertoli-Germ Cell Interactions and Male Contraceptive Development. Physiol. Rev. 82: 825-874 [Abstract] [Full Text]  
• Suzuki, A., Ishiyama, C., Hashiba, K., Shimizu, M., Ebnet, K., Ohno, S. (2002). aPKC kinase activity is required for the asymmetric differentiation of the premature junctional complex during epithelial cell polarization. J. Cell Sci. 115: 3565-3573 [Abstract] [Full Text]  
• Masuda, M., Yageta, M., Fukuhara, H., Kuramochi, M., Maruyama, T., Nomoto, A., Murakami, Y. (2002). The Tumor Suppressor Protein TSLC1 Is Involved in Cell-Cell Adhesion. J. Biol. Chem. 277: 31014-31019 [Abstract] [Full Text]  
• Fabre, S., Reymond, N., Cocchi, F., Menotti, L., Dubreuil, P., Campadelli-Fiume, G., Lopez, M. (2002). Prominent Role of the Ig-like V Domain in trans-Interactions of Nectins. NECTIN3 AND NECTIN4 BIND TO THE PREDICTED C-C'-C"-D beta -STRANDS OF THE NECTIN1 V DOMAIN. J. Biol. Chem. 277: 27006-27013 [Abstract] [Full Text]  
• Solecki, D. J., Gromeier, M., Mueller, S., Bernhardt, G., Wimmer, E. (2002). Expression of the Human Poliovirus Receptor/CD155 Gene Is Activated by Sonic Hedgehog. J. Biol. Chem. 277: 25697-25702 [Abstract] [Full Text]  
• Yoon, M., Spear, P. G. (2002). Disruption of Adherens Junctions Liberates Nectin-1 To Serve as Receptor for Herpes Simplex Virus and Pseudorabies Virus Entry. J. Virol. 76: 7203-7208 [Abstract] [Full Text]  
• Martinez, W. M., Spear, P. G. (2002). Amino Acid Substitutions in the V Domain of Nectin-1 (HveC) That Impair Entry Activity for Herpes Simplex Virus Types 1 and 2 but Not for Pseudorabies Virus or Bovine Herpesvirus 1. J. Virol. 76: 7255-7262 [Abstract] [Full Text]  
• Pokutta, S., Drees, F., Takai, Y., Nelson, W. J., Weis, W. I. (2002). Biochemical and Structural Definition of the l-Afadin- and Actin-binding Sites of alpha -Catenin. J. Biol. Chem. 277: 18868-18874 [Abstract] [Full Text]  
• Zhou, G., Roizman, B. (2002). Cation-Independent Mannose 6-Phosphate Receptor Blocks Apoptosis Induced by Herpes Simplex Virus 1 Mutants Lacking Glycoprotein D and Is Likely the Target of Antiapoptotic Activity of the Glycoprotein. J. Virol. 76: 6197-6204 [Abstract] [Full Text]  
• Krummenacher, C., Baribaud, I., Sanzo, J. F., Cohen, G. H., Eisenberg, R. J. (2002). Effects of Herpes Simplex Virus on Structure and Function of Nectin-1/HveC. J. Virol. 76: 2424-2433 [Abstract] [Full Text]  
• Nishimura, M., Kakizaki, M., Ono, Y., Morimoto, K., Takeuchi, M., Inoue, Y., Imai, T., Takai, Y. (2002). JEAP, a Novel Component of Tight Junctions in Exocrine Cells. J. Biol. Chem. 277: 5583-5587 [Abstract] [Full Text]  
• Mizoguchi, A., Nakanishi, H., Kimura, K., Matsubara, K., Ozaki-Kuroda, K., Katata, T., Honda, T., Kiyohara, Y., Heo, K., Higashi, M., Tsutsumi, T., Sonoda, S., Ide, C., Takai, Y. (2002). Nectin: an adhesion molecule involved in formation of synapses. JCB 156: 555-565 [Abstract] [Full Text]  

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