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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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Ultrastructural localization sites of nectin-2 in mouse  small intestine absorptive epithelial cells. Intestine absorptive epithelial cells were labeled with the anti–nectin-2 mAb using the  silver-enhancement technique. Open arrow, ZO; closed arrow,  ZA; asterisk, desmosome. Bars, 0.2 μm.
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Figure 5: Ultrastructural localization sites of nectin-2 in mouse small intestine absorptive epithelial cells. Intestine absorptive epithelial cells were labeled with the anti–nectin-2 mAb using the silver-enhancement technique. Open arrow, ZO; closed arrow, ZA; asterisk, desmosome. Bars, 0.2 μm.

Mentions: To examine the precise localization sites of nectin-2 at the junctional complex region of intestine absorptive epithelia, immunoelectron microscopy was performed. Nectin-2 was localized at ZA, but not at ZO or desmosome (Fig. 5). This result is consistent with our previous observation that l-afadin is localized at ZA (Mandai et al., 1997), and indicates that nectin is colocalized with l-afadin at ZA in epithelial 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)

Ultrastructural localization sites of nectin-2 in mouse  small intestine absorptive epithelial cells. Intestine absorptive epithelial cells were labeled with the anti–nectin-2 mAb using the  silver-enhancement technique. Open arrow, ZO; closed arrow,  ZA; asterisk, desmosome. Bars, 0.2 μm.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2185068&req=5

Figure 5: Ultrastructural localization sites of nectin-2 in mouse small intestine absorptive epithelial cells. Intestine absorptive epithelial cells were labeled with the anti–nectin-2 mAb using the silver-enhancement technique. Open arrow, ZO; closed arrow, ZA; asterisk, desmosome. Bars, 0.2 μm.
Mentions: To examine the precise localization sites of nectin-2 at the junctional complex region of intestine absorptive epithelia, immunoelectron microscopy was performed. Nectin-2 was localized at ZA, but not at ZO or desmosome (Fig. 5). This result is consistent with our previous observation that l-afadin is localized at ZA (Mandai et al., 1997), and indicates that nectin is colocalized with l-afadin at ZA in epithelial 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