Two Cell Adhesion Molecules, Nectin and Cadherin, Interact through Their Cytoplasmic Domain–Associated Proteins

Tachibana, Kunihide; Nakanishi, Hiroyuki; Mandai, Kenji; Ozaki, Kumi; Ikeda, Wataru; Yamamoto, Yasunori; Nagafuchi, Akira; Tsukita, Shöichiro; Takai, Yoshimi

doi:10.1083/jcb.150.5.1161

Cited by 249 publications

(255 citation statements)

References 67 publications

(157 reference statements)

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“…Given the reduced affinity of tyrosine-phosphorylated ␤-catenin for cadherin, it is difficult to explain other exceptions to the general rule (e.g., Calautti et al, 1998) other than through technical differences in measurement of adhesion and/or differences in the complexity of protein-protein interactions at de novo formed cadherin-mediated adhesions versus fully formed adherens junctions. Fully formed adherens junctions are indeed a complex web of many interacting components and may contain more than one system of cell-cell adhesion (Tachibana et al, 2000).…”

Section: Another Layer Of Action: Regulating the Phosphorylation Of ␤mentioning

confidence: 99%

Turn‐off, drop‐out: Functional state switching of cadherins

Lilien

Balsamo

Arregui

et al. 2002

Developmental Dynamics

149

116

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The classic cadherins are a group of calcium dependent, homophilic cell-cell adhesion molecules that drive morphogenetic rearrangements and maintain the integrity of cell groups through the formation of adherens junctions. The formation and maintenance of cadherin-mediated adhesions is a multistep process and mechanisms have evolved to regulate each step. This suggests that functional state switching plays an important role in development. Among the many challenges ahead is to determine the developmental role that functional state switching plays in tissue morphogenesis and to define the roles of each of the several regulatory interactions that participate in switching. One correlate of the loss of cadherinmediated adhesion, the "turn-off" of cadherin function, is the exit, or "drop-out" of cells from neural and epithelial layers and their conversion to a motile phenotype. We suggest that epithelial mesenchymal conversions may be initiated by signaling pathways that result in the loss of cadherin function. Tyrosine phosphorylation of ␤-catenin is one such mechanism. Enhanced phosphorylation of tyrosine residues on ␤-catenin is almost invariably associated with loss of the cadherin-actin connection concomitant with loss of adhesive function. There are several tyrosine kinases and phosphatases that have been shown to have the potential to alter the phosphorylation state of ␤-catenin and thus the function of cadherins. Our laboratory has focused on the role of the nonreceptor tyrosine phosphatase PTP1B in regulating the phosphorylation of ␤-catenin on tyrosine residues. Our data suggest that PTP1B is crucial for maintenance of N-cadherin-mediated adhesions in embryonic neural retina cells. By using an L-cell model system constitutively expressing N-cadherin, we have worked out many of the molecular interactions essential for this regulatory interaction. Extracellular cues that bias this critical regulatory interaction toward increased phosphorylation of ␤-catenin may be a critical component of many developmental events.

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Section: Another Layer Of Action: Regulating the Phosphorylation Of ␤mentioning

confidence: 99%

Turn‐off, drop‐out: Functional state switching of cadherins

Lilien

Balsamo

Arregui

et al. 2002

Developmental Dynamics

149

116

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“…The cytoplasmic domain of nectins associates with AF6/afadin via the carboxyterminal PDZ-binding motif of the former. Afadin, on the other hand, was shown to interact with a-catenin, suggesting that a physical association might occur between the cadherin -catenin and nectin -afadin complexes (Tachibana et al 2000). Because afadin is an actin-binding protein (Mandai et al 1997;Takahashi et al 1999), this system may also play a role in the linking of AJ to actin filaments.…”

Section: Cooperation Between Cadherin and Nectinmentioning

confidence: 99%

Adherens Junction: Molecular Architecture and Regulation

Meng¹,

Takeichi²

2009

Cold Spring Harbor Perspectives in Biology

509

449

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“…Afadin and the small amounts of nectin-1 and -2 were expressed in L cells (29). ␣-Catenin and ␤-catenin were down-regulated because of the lack of cadherin in this cell line (13). When L cells stably expressing exogenous nectin-3␣ (nectin-3-L cells) were cultured, the nectin-3␣-based cell-cell adhesion was formed as described ( Fig.…”

Section: Requirement Of Afadin For the Recruitment Of Plekha7 To The mentioning

confidence: 99%

Binding between the Junctional Proteins Afadin and PLEKHA7 and Implication in the Formation of Adherens Junction in Epithelial Cells

Kurita

Yamada

Rikitsu

et al. 2013

Journal of Biological Chemistry

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Background:Afadin is an important regulator of cell-cell adhesion. Results: PLEKHA7 binds to afadin and this binding is required for the proper formation of adherens junction (AJ). Conclusion: PLEKHA7 plays a cooperative role with nectin and afadin in the proper formation of AJ in epithelial cells. Significance: The result indicates a novel regulatory mechanism for the formation of cell-cell adhesion.

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Two Cell Adhesion Molecules, Nectin and Cadherin, Interact through Their Cytoplasmic Domain–Associated Proteins

Cited by 249 publications

References 67 publications

Turn‐off, drop‐out: Functional state switching of cadherins

Turn‐off, drop‐out: Functional state switching of cadherins

Adherens Junction: Molecular Architecture and Regulation

Binding between the Junctional Proteins Afadin and PLEKHA7 and Implication in the Formation of Adherens Junction in Epithelial Cells

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