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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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Schematic representation of the domain structure of full-length human δ-catenin compared with p120ctn. Amino acids 216–226  contain a proline rich motif that is absent in p120ctn. For δ-catenin, the amino acids 532–1013 are boxed and correspond to the 10 Armadillo repeats. Two Abl tyrosine phosphorylation consensus sites (Y292 and Y429) are indicated by arrows. The small arrowhead with an  asterisk indicates a 25–amino acid insertion site that was observed in murine δ-catenin but not in human clones. Amino acids 811–817  represent a lysine rich motif that is a potential nuclear localization signal (NLS) sequence. p120ctn has a similar, albeit somewhat weaker,  potential NLS at amino acids 622–628. A partial human δ-catenin cDNA sequence was previously published (Zhou et al., 1997) and the  full-length sequence is now updated (GenBank accession number U96136).
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Figure 1: Schematic representation of the domain structure of full-length human δ-catenin compared with p120ctn. Amino acids 216–226 contain a proline rich motif that is absent in p120ctn. For δ-catenin, the amino acids 532–1013 are boxed and correspond to the 10 Armadillo repeats. Two Abl tyrosine phosphorylation consensus sites (Y292 and Y429) are indicated by arrows. The small arrowhead with an asterisk indicates a 25–amino acid insertion site that was observed in murine δ-catenin but not in human clones. Amino acids 811–817 represent a lysine rich motif that is a potential nuclear localization signal (NLS) sequence. p120ctn has a similar, albeit somewhat weaker, potential NLS at amino acids 622–628. A partial human δ-catenin cDNA sequence was previously published (Zhou et al., 1997) and the full-length sequence is now updated (GenBank accession number U96136).

Mentions: We determined the complete sequence of human δ-catenin. It encodes a 1,225–amino acid protein with a predicted molecular weight of 132544.86 and a pI of 7.94 (Fig. 1). Mouse δ-catenin encodes a 1,247–amino acid protein that is highly related with 95% identity and 98% similarity (Paffenholz and Franke, 1997). Neither initiator methionine fits very well with the Kozak consensus sequence (Kozak, 1986) for the initiation of translation. Within the eighth Arm repeat of the human sequence, the mouse has a 25–amino acid insert at position 879 which may represent alternative splicing. A significant portion of the molecular mass lies NH2- and COOH-terminal to the Arm domain of δ-catenin. These regions contain several potentially important consensus sequences. An analysis of the complete sequence was conducted using the software CANSITE 1.0 (http://himiris.bidmc.harvard.edu), which tests putative proteins against the results of a combinatorial peptide library for selectivity of phosphorylation by signal transduction kinases (Zhou et al., 1995). The analysis revealed two potential Abl sites (Fig. 1) and several potential Abl binding motifs with the sequence XPXXPP. We found that δ-catenin showed a very high probability of being phosphorylated by Abl at tyrosine residues 292 and 429, with a specificity predicted to be within the top 1% of >2 million peptides tested. A polylysine stretch from amino acid 811 to 817 resembles a nuclear localization signal (Kalderon et al., 1984) and a polyproline tract, which is not present in p120ctn, could serve as a profilin binding site (Perelroizen et al., 1994).


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)

Schematic representation of the domain structure of full-length human δ-catenin compared with p120ctn. Amino acids 216–226  contain a proline rich motif that is absent in p120ctn. For δ-catenin, the amino acids 532–1013 are boxed and correspond to the 10 Armadillo repeats. Two Abl tyrosine phosphorylation consensus sites (Y292 and Y429) are indicated by arrows. The small arrowhead with an  asterisk indicates a 25–amino acid insertion site that was observed in murine δ-catenin but not in human clones. Amino acids 811–817  represent a lysine rich motif that is a potential nuclear localization signal (NLS) sequence. p120ctn has a similar, albeit somewhat weaker,  potential NLS at amino acids 622–628. A partial human δ-catenin cDNA sequence was previously published (Zhou et al., 1997) and the  full-length sequence is now updated (GenBank accession number U96136).
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2132907&req=5

Figure 1: Schematic representation of the domain structure of full-length human δ-catenin compared with p120ctn. Amino acids 216–226 contain a proline rich motif that is absent in p120ctn. For δ-catenin, the amino acids 532–1013 are boxed and correspond to the 10 Armadillo repeats. Two Abl tyrosine phosphorylation consensus sites (Y292 and Y429) are indicated by arrows. The small arrowhead with an asterisk indicates a 25–amino acid insertion site that was observed in murine δ-catenin but not in human clones. Amino acids 811–817 represent a lysine rich motif that is a potential nuclear localization signal (NLS) sequence. p120ctn has a similar, albeit somewhat weaker, potential NLS at amino acids 622–628. A partial human δ-catenin cDNA sequence was previously published (Zhou et al., 1997) and the full-length sequence is now updated (GenBank accession number U96136).
Mentions: We determined the complete sequence of human δ-catenin. It encodes a 1,225–amino acid protein with a predicted molecular weight of 132544.86 and a pI of 7.94 (Fig. 1). Mouse δ-catenin encodes a 1,247–amino acid protein that is highly related with 95% identity and 98% similarity (Paffenholz and Franke, 1997). Neither initiator methionine fits very well with the Kozak consensus sequence (Kozak, 1986) for the initiation of translation. Within the eighth Arm repeat of the human sequence, the mouse has a 25–amino acid insert at position 879 which may represent alternative splicing. A significant portion of the molecular mass lies NH2- and COOH-terminal to the Arm domain of δ-catenin. These regions contain several potentially important consensus sequences. An analysis of the complete sequence was conducted using the software CANSITE 1.0 (http://himiris.bidmc.harvard.edu), which tests putative proteins against the results of a combinatorial peptide library for selectivity of phosphorylation by signal transduction kinases (Zhou et al., 1995). The analysis revealed two potential Abl sites (Fig. 1) and several potential Abl binding motifs with the sequence XPXXPP. We found that δ-catenin showed a very high probability of being phosphorylated by Abl at tyrosine residues 292 and 429, with a specificity predicted to be within the top 1% of >2 million peptides tested. A polylysine stretch from amino acid 811 to 817 resembles a nuclear localization signal (Kalderon et al., 1984) and a polyproline tract, which is not present in p120ctn, could serve as a profilin binding site (Perelroizen et al., 1994).

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