Dl. Rimm et al., MOLECULAR-CLONING REVEALS ALTERNATIVE SPLICE FORMS OF HUMAN ALPHA(E)-CATENIN, Biochemical and biophysical research communications, 203(3), 1994, pp. 1691-1699
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 ident
ified two distinct transcripts, designated alpha(1)- and alpha(2)-. Th
e human alpha(1)(E)-catenin transcript predicts a 907 aa sequence 97%
identical to mouse alpha-catenin. The second transcript, alpha(2)(E)-c
atenin, displays a 24 amino acid insertion after codon 812, yielding a
931 amino acid protein (GenBank #L23805). analysis by RT-PCR and Nort
hern blotting detects one or both transcripts in epithelial and non-ep
ithelial tissues. Southern blotting indicates that both arise from a s
ingle gene. The alternative transcription site in alpha-catenin is ana
logous to the splice site in vinculin that creates meta-vinculin, exte
nding the homology between alpha-catenin and vinculin. These data with
the reported structure of other catenin genes suggest that vinculin a
nd alpha-catenin generate a superfamily of proteins mediating membrane
-cytoskeletal associations. (C) 1994 Academic Press, Inc.