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    Biochem Biophys Res Commun. 1994 Sep 30;203(3):1691-9.

    Molecular cloning reveals alternative splice forms of human alpha(E)-catenin.

    Rimm DL, Kebriaei P, Morrow JS.

    Department of Pathology, Yale University School of Medicine, New Haven, CT 06510.

    At least three proteins (alpha, beta, and gamma catenin) comprise the cytoplasmic domain of the cadherin cell-cell adhesion complex. We have cloned and sequenced human epithelial alpha(E)-catenin and have identified two distinct transcripts, designated alpha 1- and alpha 2-. The human alpha 1(E)-catenin transcript predicts a 907 aa sequence 97% identical to mouse alpha-catenin. The second transcript, alpha 2(E)-catenin, displays a 24 amino acid insertion after codon 812, yielding a 931 amino acid protein (GenBank #L23805). Analysis by RT-PCR and Northern blotting detects one or both transcripts in epithelial and non-epithelial tissues. Southern blotting indicates that both arise from a single gene. The alternative transcription site in alpha-catenin is analogous to the splice site in vinculin that creates met alpha-vinculin, extending the homology between alpha-catenin and vinculin. These data with the reported structure of other catenin genes suggest that vinculin and alpha-catenin generate a superfamily of proteins mediating membrane-cytoskeletal associations.

    PMID: 7945318 [PubMed - indexed for MEDLINE]

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