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Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein.

Takahashi K, Nakanishi H, Miyahara M, Mandai K, Satoh K, Satoh A, Nishioka H, Aoki J, Nomoto A, Mizoguchi A, Takai Y - J. Cell Biol. (1999)

Bottom Line: 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").

View Article: PubMed Central - PubMed

Affiliation: Takai Biotimer Project, ERATO, Japan Science and Technology Corp., c/o JCR Pharmaceuticals Co., Ltd., Kobe 651-2241, Japan.

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").

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Localization of nectin and l-afadin in nonepithelial  cells. (A) Localization sites of nectin-2 and l-afadin in mouse  heart. The frozen sections of mouse heart were doubly stained  with the rat anti–nectin-2 mAb and the rabbit anti–l-afadin pAb.  They were visualized with rhodamine-conjugated anti–rat IgG  and FITC-conjugated anti–rabbit IgG Abs. (A1) Nectin-2; (A2)  l-afadin. Arrows, intercalated disc. Bar, 10 μm. (B) Localization  sites of nectin-2 and l-afadin in cultured EL cells. EL cells were  doubly stained with the rat anti–nectin-2 mAb and the mouse  anti–l-afadin mAb. They were visualized with FITC-conjugated  anti–rat IgG and rhodamine-conjugated anti–mouse IgG Abs.  There was nuclear staining with this anti–l-afadin mAb, but its  significance is not clear. (B1) Nectin-2; (B2) l-afadin. Bar, 10 μm.
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Figure 6: Localization of nectin and l-afadin in nonepithelial cells. (A) Localization sites of nectin-2 and l-afadin in mouse heart. The frozen sections of mouse heart were doubly stained with the rat anti–nectin-2 mAb and the rabbit anti–l-afadin pAb. They were visualized with rhodamine-conjugated anti–rat IgG and FITC-conjugated anti–rabbit IgG Abs. (A1) Nectin-2; (A2) l-afadin. Arrows, intercalated disc. Bar, 10 μm. (B) Localization sites of nectin-2 and l-afadin in cultured EL cells. EL cells were doubly stained with the rat anti–nectin-2 mAb and the mouse anti–l-afadin mAb. They were visualized with FITC-conjugated anti–rat IgG and rhodamine-conjugated anti–mouse IgG Abs. There was nuclear staining with this anti–l-afadin mAb, but its significance is not clear. (B1) Nectin-2; (B2) l-afadin. Bar, 10 μm.

Mentions: We next examined whether nectin and l-afadin are colocalized in nonepithelial cells. When the frozen sections of heart were doubly stained with the anti–nectin-2 mAb and the anti–l-afadin pAb, both of the proteins were colocalized at intercalated discs (cell–cell AJs) and not observed at costameres (cell–matrix AJs) (Fig. 6, A1 and A2). This result suggests that nectin and l-afadin are colocalized at cell–cell AJs in nonepithelial cells. To confirm this result, we examined their colocalization in EL cells expressing E-cadherin. EL cells were cloned by introduction of the exogenous E-cadherin cDNA to cadherin-deficient L cells (Nagafuchi et al., 1987). We have shown previously that l-afadin is colocalized with E-cadherin at cell–cell AJs in cultured EL cells (Mandai et al., 1997; Sakisaka et al., 1999). In this cell line, nectin-2 was also colocalized with l-afadin at cell–cell AJs (Fig. 6, B1 and B2). These results indicate that nectin is colocalized with l-afadin at cadherin-based cell–cell AJs in nonepithelial cells.


Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein.

Takahashi K, Nakanishi H, Miyahara M, Mandai K, Satoh K, Satoh A, Nishioka H, Aoki J, Nomoto A, Mizoguchi A, Takai Y - J. Cell Biol. (1999)

Localization of nectin and l-afadin in nonepithelial  cells. (A) Localization sites of nectin-2 and l-afadin in mouse  heart. The frozen sections of mouse heart were doubly stained  with the rat anti–nectin-2 mAb and the rabbit anti–l-afadin pAb.  They were visualized with rhodamine-conjugated anti–rat IgG  and FITC-conjugated anti–rabbit IgG Abs. (A1) Nectin-2; (A2)  l-afadin. Arrows, intercalated disc. Bar, 10 μm. (B) Localization  sites of nectin-2 and l-afadin in cultured EL cells. EL cells were  doubly stained with the rat anti–nectin-2 mAb and the mouse  anti–l-afadin mAb. They were visualized with FITC-conjugated  anti–rat IgG and rhodamine-conjugated anti–mouse IgG Abs.  There was nuclear staining with this anti–l-afadin mAb, but its  significance is not clear. (B1) Nectin-2; (B2) l-afadin. Bar, 10 μm.
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Figure 6: Localization of nectin and l-afadin in nonepithelial cells. (A) Localization sites of nectin-2 and l-afadin in mouse heart. The frozen sections of mouse heart were doubly stained with the rat anti–nectin-2 mAb and the rabbit anti–l-afadin pAb. They were visualized with rhodamine-conjugated anti–rat IgG and FITC-conjugated anti–rabbit IgG Abs. (A1) Nectin-2; (A2) l-afadin. Arrows, intercalated disc. Bar, 10 μm. (B) Localization sites of nectin-2 and l-afadin in cultured EL cells. EL cells were doubly stained with the rat anti–nectin-2 mAb and the mouse anti–l-afadin mAb. They were visualized with FITC-conjugated anti–rat IgG and rhodamine-conjugated anti–mouse IgG Abs. There was nuclear staining with this anti–l-afadin mAb, but its significance is not clear. (B1) Nectin-2; (B2) l-afadin. Bar, 10 μm.
Mentions: We next examined whether nectin and l-afadin are colocalized in nonepithelial cells. When the frozen sections of heart were doubly stained with the anti–nectin-2 mAb and the anti–l-afadin pAb, both of the proteins were colocalized at intercalated discs (cell–cell AJs) and not observed at costameres (cell–matrix AJs) (Fig. 6, A1 and A2). This result suggests that nectin and l-afadin are colocalized at cell–cell AJs in nonepithelial cells. To confirm this result, we examined their colocalization in EL cells expressing E-cadherin. EL cells were cloned by introduction of the exogenous E-cadherin cDNA to cadherin-deficient L cells (Nagafuchi et al., 1987). We have shown previously that l-afadin is colocalized with E-cadherin at cell–cell AJs in cultured EL cells (Mandai et al., 1997; Sakisaka et al., 1999). In this cell line, nectin-2 was also colocalized with l-afadin at cell–cell AJs (Fig. 6, B1 and B2). These results indicate that nectin is colocalized with l-afadin at cadherin-based cell–cell AJs in nonepithelial cells.

Bottom Line: 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").

View Article: PubMed Central - PubMed

Affiliation: Takai Biotimer Project, ERATO, Japan Science and Technology Corp., c/o JCR Pharmaceuticals Co., Ltd., Kobe 651-2241, Japan.

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").

Show MeSH
Related in: MedlinePlus