Beta-catenin mediates the interaction of the cadherin-catenin complex with epidermal growth factor receptor. 1994

H Hoschuetzky, and H Aberle, and R Kemler
Max-Planck-Institut für Immunobiologie, Freiburg, Germany.

Catenins mediate the linkage of classical cadherins with actin microfilaments and are part of a higher order protein structure by which cadherins are connected to other cytoplasmic and transmembrane proteins. The ratio of actin-bound to free cadherin-catenin complex, which varies depending on the type and growth rate of cells, is thought to be altered by cellular signals, such as those associated with mitosis, polarization of cells and growth factors during development. EGF induces an immediate tyrosine phosphorylation of beta-catenin and gamma-catenin (plakoglobin). We show here an association of the EGF-receptor with the cadherin-catenin complex. Using recombinant proteins we demonstrate the interaction of EGF-receptor and beta-catenin in in vitro kinase assays. This interaction is mediated by the evolutionarily conserved central "core" region of beta-catenin. These results suggest that catenins represent an important link between EGF-induced signal transduction and cadherin function.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010766 Phosphorylation The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety. Phosphorylations
D011993 Recombinant Fusion Proteins Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes. Fusion Proteins, Recombinant,Recombinant Chimeric Protein,Recombinant Fusion Protein,Recombinant Hybrid Protein,Chimeric Proteins, Recombinant,Hybrid Proteins, Recombinant,Recombinant Chimeric Proteins,Recombinant Hybrid Proteins,Chimeric Protein, Recombinant,Fusion Protein, Recombinant,Hybrid Protein, Recombinant,Protein, Recombinant Chimeric,Protein, Recombinant Fusion,Protein, Recombinant Hybrid,Proteins, Recombinant Chimeric,Proteins, Recombinant Fusion,Proteins, Recombinant Hybrid
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D002460 Cell Line Established cell cultures that have the potential to propagate indefinitely. Cell Lines,Line, Cell,Lines, Cell
D003598 Cytoskeletal Proteins Major constituent of the cytoskeleton found in the cytoplasm of eukaryotic cells. They form a flexible framework for the cell, provide attachment points for organelles and formed bodies, and make communication between parts of the cell possible. Proteins, Cytoskeletal
D004815 Epidermal Growth Factor A 6-kDa polypeptide growth factor initially discovered in mouse submaxillary glands. Human epidermal growth factor was originally isolated from urine based on its ability to inhibit gastric secretion and called urogastrone. Epidermal growth factor exerts a wide variety of biological effects including the promotion of proliferation and differentiation of mesenchymal and EPITHELIAL CELLS. It is synthesized as a transmembrane protein which can be cleaved to release a soluble active form. EGF,Epidermal Growth Factor-Urogastrone,Urogastrone,Human Urinary Gastric Inhibitor,beta-Urogastrone,Growth Factor, Epidermal,Growth Factor-Urogastrone, Epidermal,beta Urogastrone
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

Related Publications

H Hoschuetzky, and H Aberle, and R Kemler
July 2009, The Journal of biological chemistry,
H Hoschuetzky, and H Aberle, and R Kemler
July 2002, Lung cancer (Amsterdam, Netherlands),
H Hoschuetzky, and H Aberle, and R Kemler
April 1998, The Journal of biological chemistry,
H Hoschuetzky, and H Aberle, and R Kemler
December 1997, Laboratory investigation; a journal of technical methods and pathology,
H Hoschuetzky, and H Aberle, and R Kemler
September 2003, International journal of radiation oncology, biology, physics,
H Hoschuetzky, and H Aberle, and R Kemler
September 2002, Journal of oral pathology & medicine : official publication of the International Association of Oral Pathologists and the American Academy of Oral Pathology,
H Hoschuetzky, and H Aberle, and R Kemler
September 2001, The Journal of biological chemistry,
H Hoschuetzky, and H Aberle, and R Kemler
May 2008, Genes & development,
H Hoschuetzky, and H Aberle, and R Kemler
January 1994, Progress in nucleic acid research and molecular biology,
Copied contents to your clipboard!