Cadherins

Geiger, B; Ayalon, Oran

doi:10.1146/annurev.cb.08.110192.001515

Cited by 474 publications

(292 citation statements)

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“…The extracellular spaces are sealed by tight junctions, whose structural integrity is essential to the functional integrity of the tissue. A specific contributor to this structural integrity is E-cadherin, a transmembrane cell-cell adhesion protein located at the lateral junctions and usually concentrated in adhesion belts just below the tight junctions, which connect to the actin cytoskeleton of the cells (22). Our results demonstrate in CACO-2 cells that ErbB2 is localized to the lateral membrane, which is primarily co-localized with cadherin.…”

mentioning

confidence: 57%

Muc4/Sialomucin Complex, the Intramembrane ErbB2 Ligand, Translocates ErbB2 to the Apical Surface in Polarized Epithelial Cells

Palau

Carraway

Salas

et al. 2003

Journal of Biological Chemistry

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mentioning

confidence: 57%

Muc4/Sialomucin Complex, the Intramembrane ErbB2 Ligand, Translocates ErbB2 to the Apical Surface in Polarized Epithelial Cells

Palau

Carraway

Salas

et al. 2003

Journal of Biological Chemistry

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“…Thus, the complex formation with catenins and the anchorage to the actin cytoskeleton overcome the negative modulation imposed by serine/threonine phosphorylation of p120 ctn in the regulation of the activity. The amino acid residues of the p120 ctn -binding site of Ecadherin are relatively well conserved in other cadherins (2). Among these cadherins, E-cadherin (21)(22)(23)32, this study), Nand P-cadherin (41), VE-cadherin (33), and C-cadherin (31) have been shown to coprecipitate with p120 ctn .…”

Section: P120mentioning

confidence: 74%

“…Chemical cross-linking experiments revealed the presence of the E⌬C71 protein dimer in cells expressing the mutant p120 ctn proteins but not in cells expressing the fulllength p120 ctn protein. 2 It is therefore conceivable that these mutant p120 ctn proteins bound to the nonfunctional E-cadherin polypeptides could function as dominant-positive (activating) mutants through facilitating dimerization of the mutant E-2 M. Ozawa, unpublished results.…”

Section: Discussionmentioning

confidence: 99%

“…The cadherins are a family of transmembrane glycoproteins that play essential roles in the initiation and stabilization of cell-cell contacts (1)(2)(3)(4). The extracellular domain of cadherins is responsible for specific homophilic binding (5), whereas the carboxyl-terminal region of the cytoplasmic domain interacts with intracellular proteins termed catenins (6,7).…”

mentioning

confidence: 99%

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p120ctn Binds to the Membrane-proximal Region of the E-cadherin Cytoplasmic Domain and Is Involved in Modulation of Adhesion Activity

Ohkubo

Ozawa

1999

Journal of Biological Chemistry

158

143

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Cadherins are transmembrane glycoproteins involved in Ca2؉ -dependent cell-cell adhesion. Previously, we showed that the conserved membrane-proximal region of the E-cadherin cytoplasmic domain negatively regulates adhesion activity. In this report, we provide several lines of evidence that p120 ctn is involved in this negative regulation. p120 ctn binds to the membraneproximal region of the nonfunctional carboxyl-terminally deleted E-cadherin protein. An additional internal deletion in this region prevented the association with p120 ctn and activated the protein, as seen in an aggregation assay. Furthermore, the nonfunctional E-cadherin can be activated through coexpression of p120 ctn proteins with amino-terminal deletions, which eliminate several potential serine/threonine phosphorylation sites but do not affect the ability to bind to cadherins. Finally, we show that staurosporine, a kinase inhibitor, induces an increased electrophoretic mobility of p120 ctn bound to E-cadherin polypeptides, activates the nonfunctional E-cadherin protein, and converts the wildtype E-cadherin and an E-cadherin-␣-catenin chimeric protein from a cytochalasin D-sensitive to a cytochalasin D-insensitive state. Together, these results indicate that p120 ctn is a modulator of E-cadherin-mediated cell adhesion.

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“…14 Cadherins, the transmembrane components of adherens junctions, mediate via homotypic interactions and binding to the cytoplasmic catenin molecules the interaction with the actin cytoskeleton, and in this way they play an important role as morphoregulatory molecules. 2,4,39,40 In squamous epithelia, E-cadherin is one of the major cell adhesion molecules defining the architecture and differentiation of keratinocytes. 41,42 Evidence is accumulating that E-cadherin may perform as a tumor-suppressor and invasion-suppressor molecule 7,8 and is functionally disturbed during carcinogenesis of various epithelial tissues, including cervical lesions and carcinomas.…”

Section: Discussionmentioning

confidence: 99%

Changing Roles of Cadherins and Catenins during Progression of Squamous Intraepithelial Lesions in the Uterine Cervix

Boer

Dorst²,

Krieken

et al. 1999

The American Journal of Pathology

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Uterine cervix represents a convenient model for the study of the gradual transformation of normal squamous epithelium via low-to high-grade squamous intraepithelial lesions (SILs). Because SIL , on the basis of the cytokeratins expressed , are thought to originate from the reserve cells , we analyzed whether SILs also show a reserve cell phenotype with respect to intercellular interactions. The changes in expression and subcellular localization of the components of the adherens junction and desmosomal complexes were investigated in normal , metaplastic , and premalignant cervical epithelium , as well as in cell cultures derived from these tissues. The results suggest that 1) during progression of SILs , E-cadherin is suppressed, with its role in cell-cell connections diminishing; 2) P-cadherin , in contrast , becomes the predominant cadherin in high-grade SILs; 3) the level of cellular ␣-catenin is dramatically decreased in high-grade SILs; 4) the level of ␤-catenin is decreased during progression of SILs , with plakoglobin suggestively becoming the predominant catenin mediating connection of cadherins to the cytoskeleton; 5) the assembly of desmosomes is affected during progression of SILs and is accompanied by a dramatically decreased expression for desmogleins and desmoplakins (I , II); and 6) expression of differentiation markers (involucrin , CK13) in high-grade SILs seems to be controlled by P-cadherin as opposed to E-cadherin in the normal tissue counterpart. We conclude that during development of cervical lesions substantial (

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Cadherins

Cited by 474 publications

References 0 publications

Muc4/Sialomucin Complex, the Intramembrane ErbB2 Ligand, Translocates ErbB2 to the Apical Surface in Polarized Epithelial Cells

Muc4/Sialomucin Complex, the Intramembrane ErbB2 Ligand, Translocates ErbB2 to the Apical Surface in Polarized Epithelial Cells

p120ctn Binds to the Membrane-proximal Region of the E-cadherin Cytoplasmic Domain and Is Involved in Modulation of Adhesion Activity

Changing Roles of Cadherins and Catenins during Progression of Squamous Intraepithelial Lesions in the Uterine Cervix

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