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delta-catenin, an adhesive junction-associated protein which promotes cell scattering.

Lu Q, Paredes M, Medina M, Zhou J, Cavallo R, Peifer M, Orecchio L, Kosik KS - J. Cell Biol. (1999)

Bottom Line: We found that delta-catenin can be immunoprecipitated as a complex with other components of the adherens junction, including cadherin and beta-catenin, from transfected cells and brain.In developing mouse brain, staining with delta-catenin antibodies is prominent towards the apical boundary of the neuroepithelial cells in the ventricular zone.The Arm domain alone was sufficient for achieving localization and coimmunoprecipitation with cadherin.

View Article: PubMed Central - PubMed

Affiliation: Center for Neurologic Diseases, Department of Neurology, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.

ABSTRACT
The classical adherens junction that holds epithelial cells together consists of a protein complex in which members of the cadherin family linked to various catenins are the principal components. delta-catenin is a mammalian brain protein in the Armadillo repeat superfamily with sequence similarity to the adherens junction protein p120(ctn). We found that delta-catenin can be immunoprecipitated as a complex with other components of the adherens junction, including cadherin and beta-catenin, from transfected cells and brain. The interaction with cadherin involves direct contact within the highly conserved juxtamembrane region of the COOH terminus, where p120(ctn) also binds. In developing mouse brain, staining with delta-catenin antibodies is prominent towards the apical boundary of the neuroepithelial cells in the ventricular zone. When transfected into Madin-Darby canine kidney (MDCK) epithelial cells delta-catenin colocalized with cadherin, p120(ctn), and beta-catenin. The Arm domain alone was sufficient for achieving localization and coimmunoprecipitation with cadherin. The ectopic expression of delta-catenin in MDCK cells altered their morphology, induced the elaboration of lamellipodia, interfered with monolayer formation, and increased scattering in response to hepatocyte growth factor treatment. We propose that delta-catenin can regulate adhesion molecules to implement the organization of large cellular arrays necessary for tissue morphogenesis.

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Ectopic expression of  δ-catenin does not lead to displacement of p120ctn from adhesive junction proteins. (A) Immunoblot showing p120ctn  coimmunoprecipitation with  E-cadherin in mock (1), and MF  cells (2). (3) MDCK cell lysate.  (B) Double immunofluorescent  microscopy showing redistribution of junctional proteins in  δ-catenin–transfected MDCK  cells after HGF stimulation. (a, c,  and e) Anti–δ-catenin. (b) Anti– β-catenin. (d) Anti-p120ctn. (f)  Anti-desmoplakin. Note the  colocalization of δ-catenin with  β-catenin and p120ctn, but not  desmoplakin, at the leading  edges of cells treated with HGF.  Arrows point to the lamellipodia  formation. Bar, 5 μm.
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Figure 11: Ectopic expression of δ-catenin does not lead to displacement of p120ctn from adhesive junction proteins. (A) Immunoblot showing p120ctn coimmunoprecipitation with E-cadherin in mock (1), and MF cells (2). (3) MDCK cell lysate. (B) Double immunofluorescent microscopy showing redistribution of junctional proteins in δ-catenin–transfected MDCK cells after HGF stimulation. (a, c, and e) Anti–δ-catenin. (b) Anti– β-catenin. (d) Anti-p120ctn. (f) Anti-desmoplakin. Note the colocalization of δ-catenin with β-catenin and p120ctn, but not desmoplakin, at the leading edges of cells treated with HGF. Arrows point to the lamellipodia formation. Bar, 5 μm.

Mentions: MDCK cells transfected with δ-catenin displayed an altered morphology. Transfected cells tended to lose their polygonal morphology and assumed either irregular shapes or an elongated fibroblastic appearance, sometimes with cell processes (Figs. 4 A and 5 A). Cells stably transfected with δ-catenin lost their organization as a regularly packed monolayer (compare Fig. 9 A, panels c and d). Immunolabeling of the δ-catenin–transfected cells showed that other major proteins of the adherens junction remained predominantly localized to cell–cell junctions (Fig. 9 A, c and d; B, a–d). Because δ-catenin and p120ctn both bind to the juxtamembrane region of cadherin, one might expect that their interaction with E-cadherin is competitive. However, in δ-catenin–expressing cells p120ctn retained its localization at the cell boundary (Reynolds et al., 1992; Fig. 9 B, c and d). Although a few cells showed increased cytoplasmic p120ctn staining after δ-catenin transfection, the differences from controls were insignificant, and there was no increase in the soluble pool of p120ctn (Fig. 2 C). Furthermore, after δ-catenin transfection there was no change in the amount of p120ctn coimmunoprecipitated with E-cadherin compared to mock-transfected cells (see Fig. 11 A, lanes 1 and 2).


delta-catenin, an adhesive junction-associated protein which promotes cell scattering.

Lu Q, Paredes M, Medina M, Zhou J, Cavallo R, Peifer M, Orecchio L, Kosik KS - J. Cell Biol. (1999)

Ectopic expression of  δ-catenin does not lead to displacement of p120ctn from adhesive junction proteins. (A) Immunoblot showing p120ctn  coimmunoprecipitation with  E-cadherin in mock (1), and MF  cells (2). (3) MDCK cell lysate.  (B) Double immunofluorescent  microscopy showing redistribution of junctional proteins in  δ-catenin–transfected MDCK  cells after HGF stimulation. (a, c,  and e) Anti–δ-catenin. (b) Anti– β-catenin. (d) Anti-p120ctn. (f)  Anti-desmoplakin. Note the  colocalization of δ-catenin with  β-catenin and p120ctn, but not  desmoplakin, at the leading  edges of cells treated with HGF.  Arrows point to the lamellipodia  formation. Bar, 5 μm.
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Figure 11: Ectopic expression of δ-catenin does not lead to displacement of p120ctn from adhesive junction proteins. (A) Immunoblot showing p120ctn coimmunoprecipitation with E-cadherin in mock (1), and MF cells (2). (3) MDCK cell lysate. (B) Double immunofluorescent microscopy showing redistribution of junctional proteins in δ-catenin–transfected MDCK cells after HGF stimulation. (a, c, and e) Anti–δ-catenin. (b) Anti– β-catenin. (d) Anti-p120ctn. (f) Anti-desmoplakin. Note the colocalization of δ-catenin with β-catenin and p120ctn, but not desmoplakin, at the leading edges of cells treated with HGF. Arrows point to the lamellipodia formation. Bar, 5 μm.
Mentions: MDCK cells transfected with δ-catenin displayed an altered morphology. Transfected cells tended to lose their polygonal morphology and assumed either irregular shapes or an elongated fibroblastic appearance, sometimes with cell processes (Figs. 4 A and 5 A). Cells stably transfected with δ-catenin lost their organization as a regularly packed monolayer (compare Fig. 9 A, panels c and d). Immunolabeling of the δ-catenin–transfected cells showed that other major proteins of the adherens junction remained predominantly localized to cell–cell junctions (Fig. 9 A, c and d; B, a–d). Because δ-catenin and p120ctn both bind to the juxtamembrane region of cadherin, one might expect that their interaction with E-cadherin is competitive. However, in δ-catenin–expressing cells p120ctn retained its localization at the cell boundary (Reynolds et al., 1992; Fig. 9 B, c and d). Although a few cells showed increased cytoplasmic p120ctn staining after δ-catenin transfection, the differences from controls were insignificant, and there was no increase in the soluble pool of p120ctn (Fig. 2 C). Furthermore, after δ-catenin transfection there was no change in the amount of p120ctn coimmunoprecipitated with E-cadherin compared to mock-transfected cells (see Fig. 11 A, lanes 1 and 2).

Bottom Line: We found that delta-catenin can be immunoprecipitated as a complex with other components of the adherens junction, including cadherin and beta-catenin, from transfected cells and brain.In developing mouse brain, staining with delta-catenin antibodies is prominent towards the apical boundary of the neuroepithelial cells in the ventricular zone.The Arm domain alone was sufficient for achieving localization and coimmunoprecipitation with cadherin.

View Article: PubMed Central - PubMed

Affiliation: Center for Neurologic Diseases, Department of Neurology, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.

ABSTRACT
The classical adherens junction that holds epithelial cells together consists of a protein complex in which members of the cadherin family linked to various catenins are the principal components. delta-catenin is a mammalian brain protein in the Armadillo repeat superfamily with sequence similarity to the adherens junction protein p120(ctn). We found that delta-catenin can be immunoprecipitated as a complex with other components of the adherens junction, including cadherin and beta-catenin, from transfected cells and brain. The interaction with cadherin involves direct contact within the highly conserved juxtamembrane region of the COOH terminus, where p120(ctn) also binds. In developing mouse brain, staining with delta-catenin antibodies is prominent towards the apical boundary of the neuroepithelial cells in the ventricular zone. When transfected into Madin-Darby canine kidney (MDCK) epithelial cells delta-catenin colocalized with cadherin, p120(ctn), and beta-catenin. The Arm domain alone was sufficient for achieving localization and coimmunoprecipitation with cadherin. The ectopic expression of delta-catenin in MDCK cells altered their morphology, induced the elaboration of lamellipodia, interfered with monolayer formation, and increased scattering in response to hepatocyte growth factor treatment. We propose that delta-catenin can regulate adhesion molecules to implement the organization of large cellular arrays necessary for tissue morphogenesis.

Show MeSH
Related in: MedlinePlus