alphaT-catenin: a novel tissue-specific beta-catenin-binding protein mediating strong cell-cell adhesion

J Cell Sci. 2001 Sep;114(Pt 17):3177-88. doi: 10.1242/jcs.114.17.3177.

Abstract

Cadherins are major cell-cell adhesion proteins whose cytoplasmic domains bind to catenin proteins. Strong intercellular adhesion depends on linkage of the cadherin/catenin complex to the actin cytoskeleton via alpha-catenin. To date, it is not clear how different cell types achieve the variable strength of cell-cell adhesion clearly needed in a multicellular organism. Here, we report the cloning and molecular characterization of alphaT(testis)-catenin, a novel human cDNA encoding a protein with homology to both human alphaE(epithelial)-catenin and alphaN(neural)-catenin. Although originally discovered in testis, alphaT-catenin is expressed in other tissues, the highest levels being observed in heart. Immunohistochemical analysis showed human alphaT-catenin localization at intercalated discs of cardiomyocytes and in peritubular myoid cells of testis. In cells transfected with alphaT-catenin cDNA, interaction with beta-catenin was demonstrated by co-immunoprecipitation. Transfection of alpha-catenin-deficient colon carcinoma cells recruited E-cadherin and beta-catenin to cell-cell contacts and functional cadherin-mediated cell-cell adhesion was restored in this way. Moreover, compaction of these cells was at least as prominent as in the case of cells expressing endogenous alphaE-catenin. We propose that alphaT-catenin is necessary for the formation of stretch-resistant cell-cell adhesion complexes, in particular, muscle cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Blotting, Western
  • Cadherins / metabolism*
  • Cadherins / physiology*
  • Cell Adhesion
  • Cell Communication
  • Cell Line
  • Cells, Cultured
  • Cloning, Molecular
  • Cytoskeletal Proteins / chemistry*
  • Cytoskeletal Proteins / metabolism*
  • Cytoskeletal Proteins / physiology*
  • DNA, Complementary / metabolism
  • Electrophoresis, Polyacrylamide Gel
  • Green Fluorescent Proteins
  • Humans
  • Immunohistochemistry
  • Luminescent Proteins / metabolism
  • Male
  • Mice
  • Microscopy, Fluorescence
  • Molecular Sequence Data
  • Muscles / cytology
  • Myocardium / cytology
  • Myocardium / metabolism
  • Plasmids / metabolism
  • Precipitin Tests
  • Protein Binding
  • Protein Structure, Tertiary
  • Reverse Transcriptase Polymerase Chain Reaction
  • Sequence Homology, Amino Acid
  • Testis / cytology
  • Testis / metabolism
  • Tissue Distribution
  • Trans-Activators*
  • Transfection
  • Tumor Cells, Cultured
  • Vinculin / metabolism
  • alpha Catenin
  • beta Catenin

Substances

  • CTNNA1 protein, human
  • CTNNA3 protein, human
  • CTNNB1 protein, human
  • CTNNB1 protein, mouse
  • Cadherins
  • Ctnna1 protein, mouse
  • Cytoskeletal Proteins
  • DNA, Complementary
  • Luminescent Proteins
  • Trans-Activators
  • alpha Catenin
  • beta Catenin
  • Vinculin
  • Green Fluorescent Proteins

Associated data

  • GENBANK/AF091606