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Results: 141 to 144 of 144

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The novel catenin p120cas binds classical cadherins and induces an unusual morphological phenotype in NIH3T3 fibroblasts.
Reynolds AB, Daniel JM, Mo YY, Wu J, Zhang Z
(1996) Exp Cell Res 225: 328-37
MeSH Terms: 3T3 Cells, Animals, Cadherins, Catenins, Cell Adhesion Molecules, Cell Size, Cytoskeletal Proteins, DNA, Dendrites, Gene Expression, Mice, Mutation, Phenotype, Phosphoproteins, Protein Binding, Protein Structure, Tertiary, Repetitive Sequences, Nucleic Acid, Trans-Activators, beta Catenin
Show Abstract · Added March 5, 2014
p120cas (CAS) is a tyrosine kinase substrate whose phosphorylation has been implicated in cell transformation by Src and in ligand-induced signaling through the EGF, PDGF, and CSF-1 receptors. More recently, CAS has been shown to associate with E-cadherin and its cofactors (catenins), molecules that are involved in cell adhesion. Although both CAS and beta-catenin contain armadillo repeat domains (Arm domains), the amino acid identity between these proteins in this region is only 22%, and it is not yet clear whether CAS will emulate other catenins by associating with other members of the cadherin family. Here we report that in addition to binding E-cadherin, wild-type CAS associated with N-cadherin and P-cadherin. Transient transfection of cloned CAS isoforms into MDCK epithelial cells indicated that CAS1 and CAS2 isoforms are equally capable of binding to E-cadherin even though these cells preferentially express CAS2 isoforms. In addition, CAS colocalized with N-cadherin in NIH3T3 cells and analysis of CAS mutants in vivo indicated that the CAS-N-cadherin interaction requires an intact CAS Arm domain. The data suggest that CAS-cadherin interactions in general are dictated by the conserved armadillo repeats and are not heavily influenced by sequences added outside the Arm domain by alternative splicing. Interestingly, overexpression of CAS in NIH3T3 cells induced a striking morphological phenotype characterized by the presence of long dendrite-like processes. This branching phenotype was specific for CAS, since (i) overexpression of the structurally similar beta-catenin had little effect on cell morphology, and (ii) the branching was abolished by deletions in the CAS Arm domain. Our data indicate that, like other catenins, CAS is a cofactor for multiple members of the cadherin family. However, the dramatically distinct phenotype exhibited by fibroblasts overexpressing CAS, versus beta-catenin, support recent data suggesting that these catenins have fundamentally different and possibly opposing roles in cadherin complexes.
1 Communities
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19 MeSH Terms
A repeating amino acid motif shared by proteins with diverse cellular roles.
Peifer M, Berg S, Reynolds AB
(1994) Cell 76: 789-91
MeSH Terms: Amino Acid Sequence, Animals, Armadillo Domain Proteins, Consensus Sequence, Cytoskeletal Proteins, Desmoplakins, Drosophila Proteins, Drosophila melanogaster, Genes, Homeobox, Molecular Sequence Data, Proteins, Repetitive Sequences, Nucleic Acid, Sequence Alignment, Sequence Homology, Amino Acid, Trans-Activators, Transcription Factors, beta Catenin
Added March 5, 2014
1 Communities
1 Members
0 Resources
17 MeSH Terms
Identification of a new catenin: the tyrosine kinase substrate p120cas associates with E-cadherin complexes.
Reynolds AB, Daniel J, McCrea PD, Wheelock MJ, Wu J, Zhang Z
(1994) Mol Cell Biol 14: 8333-42
MeSH Terms: 3T3 Cells, Alternative Splicing, Amino Acid Sequence, Animals, Antibodies, Monoclonal, Cadherins, Catenins, Cattle, Cell Adhesion Molecules, Cell Line, Cell Transformation, Neoplastic, Cytoskeletal Proteins, Macromolecular Substances, Mice, Molecular Sequence Data, Phosphoproteins, Phosphotyrosine, Protein Binding, Protein-Tyrosine Kinases, Proto-Oncogene Proteins pp60(c-src), Trans-Activators, Tyrosine, beta Catenin
Show Abstract · Added March 5, 2014
p120cas is a tyrosine kinase substrate implicated in ligand-induced receptor signaling through the epidermal growth factor, platelet-derived growth factor, and colony-stimulating factor receptors and in cell transformation by Src. Here we report that p120 associates with a complex containing E-cadherin, alpha-catenin, beta-catenin, and plakoglobin. Furthermore, p120 precisely colocalizes with E-cadherin and catenins in vivo in both normal and Src-transformed MDCK cells. Unlike beta-catenin and plakoglobin, p120 has at least four isoforms which are differentially expressed in a variety of cell types, suggesting novel means of modulating cadherin activities in cells. In Src-transformed MDCK cells, p120, beta-catenin, and plakoglobin were heavily phosphorylated on tyrosine, but the physical associations between these proteins were not disrupted. Association of p120 with the cadherin machinery indicates that both Src and receptor tyrosine kinases cross talk with proteins important for cadherin-mediated cell adhesion. These results also strongly suggest a role for p120 in cell adhesion.
1 Communities
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23 MeSH Terms
p120, a novel substrate of protein tyrosine kinase receptors and of p60v-src, is related to cadherin-binding factors beta-catenin, plakoglobin and armadillo.
Reynolds AB, Herbert L, Cleveland JL, Berg ST, Gaut JR
(1992) Oncogene 7: 2439-45
MeSH Terms: 3T3 Cells, Amino Acid Sequence, Animals, Armadillo Domain Proteins, Base Sequence, Cadherins, Cell Adhesion Molecules, Cloning, Molecular, Cytoskeletal Proteins, DNA, DNA Probes, Desmoplakins, Drosophila, Drosophila Proteins, Gene Library, Humans, Insect Hormones, Mice, Molecular Sequence Data, Oncogene Protein pp60(v-src), Phosphoproteins, Polymerase Chain Reaction, Protein-Tyrosine Kinases, Proteins, Receptors, Cell Surface, Sequence Homology, Amino Acid, Sequence Homology, Nucleic Acid, Substrate Specificity, Trans-Activators, Transcription Factors, Xenopus, Xenopus Proteins, beta Catenin, gamma Catenin
Show Abstract · Added March 5, 2014
A novel protein tyrosine kinase (PTK) substrate, p120, has been previously implicated in ligand-induced signaling through the epidermal growth factor, platelet-derived growth factor and colony-stimulating factor 1 receptors, and in cell transformation by p60v-src. We have isolated a near full-length cDNA encoding murine p120. The encoded protein lacks significant homology with any reported protein, but it contains four copies of an imperfect 42 amino acid repeat that occurs 12.5 times in the protein encoded by Drosophila armadillo (arm), and its direct homologs, human plakoglobin (plak) and Xenopus laevis beta-catenin (beta-cat). The presence of this motif implies that p120 may share at least one aspect of its function with the arm protein and its homologs.
1 Communities
1 Members
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34 MeSH Terms