Characterization of cadherin-24, a novel alternatively spliced type II cadherin.
Cadherins comprise a superfamily of calcium-dependent cell-cell adhesion molecules. Within the superfamily are six subfamilies including type I and type II cadherins. Both type I and type II cadherins are composed of five extracellular repeat domains with conserved calcium-binding motifs, a single pass transmembrane domain, and a highly conserved cytoplasmic domain that interacts with beta-catenin and p120 catenin. In this study, we describe a novel cadherin, cadherin-24. It is a type II cadherin with a 781-codon open reading frame, which encodes a type II cadherin protein complete with five extracellular repeats containing calcium-binding motifs, a transmembrane domain, and a conserved cytoplasmic domain. Cadherin-24 has the unusual feature of being alternatively spliced in extracellular repeat 4. This alternative exon encodes 38 in-frame amino acids, resulting in an 819-amino-acid protein. Sequence analysis suggests the presence of beta-catenin and p120 catenin-binding sequences, and immunoprecipitation experiments confirm the ability of both forms of the novel cadherin to associate with alpha-catenin, beta-catenin, and p120 catenin. In addition, aggregation assays show that both forms of cadherin-24 mediate strong cell-cell adhesion.
University of Nebraska Medical Center, Department of Oral Biology, College of Dentistry and Eppley Cancer Center, Omaha, Nebraska 68198, USA.
Bryan J
BJ
Katafiasz
Marvin T
MT
Nieman
Margaret J
MJ
Wheelock
Keith R
KR
Johnson
D017398:Alternative Splicing; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D001483:Base Sequence; D015820:Cadherins / Q000096:biosynthesis* / Q000737:chemistry / Q000502:physiology*; D051177:Catenins; D002448:Cell Adhesion; D015815:Cell Adhesion Molecules / Q000737:chemistry; D002460:Cell Line; D003001:Cloning, Molecular; D003593:Cytoplasm / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000378:metabolism; D018076:DNA, Complementary / Q000378:metabolism; D003902:Detergents / Q000494:pharmacology; D005091:Exons; D006801:Humans; D015151:Immunoblotting; D007438:Introns; D008957:Models, Genetic; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D010750:Phosphoproteins / Q000737:chemistry; D016133:Polymerase Chain Reaction; D011233:Precipitin Tests; D020033:Protein Isoforms; D017434:Protein Structure, Tertiary; D012333:RNA, Messenger / Q000378:metabolism; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D014018:Tissue Distribution; D015534:Trans-Activators / Q000378:metabolism; D014162:Transfection; D014407:Tumor Cells, Cultured; D051176:beta Catenin; D000095002:Delta Catenin
C476579:CDH24 protein, human; C495270:CTNNB1 protein, human; D015820:Cadherins; D051177:Catenins; D015815:Cell Adhesion Molecules; D003598:Cytoskeletal Proteins; D018076:DNA, Complementary; D003902:Detergents; D010750:Phosphoproteins; D020033:Protein Isoforms; D012333:RNA, Messenger; D015534:Trans-Activators; D051176:beta Catenin; D000095002:Delta Catenin; C000722347:CTNND1 protein, human