Direct association of presenilin‐1 with β‐catenin

Murayama, Miyuki; Tanaka, Shoji; Palacino, James; Murayama, Ohoshi; Honda, Toshiyuki; Sun, Xiaoyan; Yasutake, Kaori; Nihonmatsu, Naomi; Wolozin, Benjamin; Takashima, Akihiko

doi:10.1016/s0014-5793(98)00886-2

Cited by 154 publications

(119 citation statements)

References 31 publications

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“…PS1͞CTF sequence 340-375 binds E-cadherin sequence 604-615 and may tether the membrane-proximal cytoplasmic E-cadherin close to the plasma membrane. At a more distal site on E-cadherin are bound ␤-or ␥-catenin (16,17), which in turn may bind PS1 (19,20). These interactions could result in the formation of a stable three-member complex, each member of which binds directly to the other two.…”

Section: Discussionmentioning

confidence: 99%

“…1A). Because PS1 binds ␤-catenin (19,20), we attempted to determine whether PS1 binds E-cadherin independent of catenins. Triton X-100 extracted most of PS1͞ CTF from a ␤-catenin IP but failed to extract any PS1͞CTF from an E-cadherin IP, indicating that the PS1͞E-cadherin binding might be distinct from the PS1͞␤-catenin binding (Fig.…”

Section: Ps1͞e-cadherinmentioning

confidence: 99%

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Presenilin-1 binds cytoplasmic epithelial cadherin, inhibits cadherin/p120 association, and regulates stability and function of the cadherin/catenin adhesion complex

Baki

Marambaud

Efthimiopoulos

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

179

163

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Here we show that presenilin-1 (PS1), a protein involved in Alzheimer's disease, binds directly to epithelial cadherin (E-cadherin). This binding is mediated by the large cytoplasmic loop of PS1 and requires the membrane-proximal cytoplasmic sequence 604 -615 of mature E-cadherin. This sequence is also required for E-cadherin binding of protein p120, a known regulator of cadherin-mediated cell adhesion. Using wild-type and PS1 knockout cells, we found that increasing PS1 levels suppresses p120͞E-cadherin binding, and increasing p120 levels suppresses PS1͞E-cadherin binding. Thus PS1 and p120 bind to and mutually compete for cellular E-cadherin. Furthermore, PS1 stimulates E-cadherin binding to ␤-and ␥-catenin, promotes cytoskeletal association of the cadherin͞catenin complexes, and increases Ca 2؉ -dependent cell-cell aggregation. Remarkably, PS1 familial Alzheimer disease mutant ⌬E9 increased neither the levels of cadherin͞catenin complexes nor cell aggregation, suggesting that this familial Alzheimer disease mutation interferes with cadherin-based cell-cell adhesion. These data identify PS1 as an E-cadherin-binding protein and a regulator of E-cadherin function in vivo.

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Section: Discussionmentioning

confidence: 99%

Section: Ps1͞e-cadherinmentioning

confidence: 99%

Presenilin-1 binds cytoplasmic epithelial cadherin, inhibits cadherin/p120 association, and regulates stability and function of the cadherin/catenin adhesion complex

Baki

Marambaud

Efthimiopoulos

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

179

163

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“…< SYNTHÈSE REVUES PS-1 et la -caténine 1 interagissent sous forme de complexes, stabilisant ainsi le taux de forme libre de -caténine. Les mutations de PS-1 abolissent cet effet, favorisent la phosphorylation de la -caténine par la GSK-3 et bloquent ainsi la voie de signalisation dépendante de Wnt, provoquant alors la mort cellulaire [11]. Ainsi, par le biais des présénilines, la GSK-3 semble impliquée dans la production d'A , la régulation de la phosphorylation de Tau et la modulation des niveaux de -caténine (Figure 2).…”

Section: Dégénérescences Neurofibrillairesunclassified

GSK-3β : une kinase au cœur des maladies neuro-dégénératives ?

Petit-Paitel

2010

Med Sci (Paris)

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“…Presenilin also stimulates the interaction of E-cadherin with ␤-catenin and the cytoskeleton; the ultimate effect is to enhance adhesion (Baki et al, 2001;Georgakopoulos et al, 1999). The relationship between competition for binding of p120 ctn , enhanced binding of ␤-catenin to cadherin, and the interaction of presenilin with the cytosolic ␤-catenin complex (Murayama et al, 1998;Yu et al, 1998) remains to be clarified. This complex web of p120 ctn interactions and their ramifications, as well as its potential role in transcription (Daniel and Reynolds, 1999;Prokhortchouk et al, 2001), suggests that, like ␤-catenin, p120 ctn is a key regulatory molecule integrating cell adhesion and transcription during development.…”

Section: The Plot Regulatory Interactions At the Cytoplasmic Domain Omentioning

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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Direct association of presenilin‐1 with β‐catenin

Cited by 154 publications

References 31 publications

Presenilin-1 binds cytoplasmic epithelial cadherin, inhibits cadherin/p120 association, and regulates stability and function of the cadherin/catenin adhesion complex

Presenilin-1 binds cytoplasmic epithelial cadherin, inhibits cadherin/p120 association, and regulates stability and function of the cadherin/catenin adhesion complex

GSK-3β : une kinase au cœur des maladies neuro-dégénératives ?

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

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