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Catenins are proteins found in complexes with cadherin cell adhesion molecules of animal cells. The first two catenins that were identified[2] became known as alpha-catenin and beta-catenin. Alpha-catenin can bind to beta-catenin and can also bind actin. Beta-catenin binds the cytoplasmic domain of some cadherins. Additional catenins such as gamma-catenin and delta-catenin have been identified. The name "catenin" was originally selected ('catena' means 'chain' in Latin) because it was suspected that catenins might link cadherins to the cytoskeleton.[3]



  • alpha catenin
  • beta catenin
  • delta catenin
  • gamma catenin

All but alpha contain armadillo repeats.

Catenins and cadherin function

F9 embryonal carcinoma cells are similar to the P19 cells shown in Figure 1 and normally have cell-to-cell adhesion mediated by E-cadherin with beta-catenin bound to the cytoplasmic domain of E-cadherin. F9 cells were genetically engineered to lack beta-catenin, resulting in increased association of plakoglobin with E-cadherin.[4] In F9 cells lacking both beta-catenin and plakoglobin, very little E-cadherin and alpha-catenin accumulated at the cell surface.[4] Mice lacking beta-catenin have defective embryos. Mice engineered to specifically have vascular endothelium cells deficient in beta-catenin showed disrupted adhesion between vascular endothelial cells.[5] Mice lacking plakoglobin have cell adhesion defects in many tissues, although beta-catenin substitutes for plakoglobin at many cellular junctions.[6] Keratinocytes engineered to not express alpha-catenin have disrupted cell adhesion[7] and activated NF-kB.[8] A tumor cell line with defective delta-catenin, low levels of E-cadherin and poor cell-to-cell adhesion could be reverted to normal epithelial morphology and increased E-cadherin levels by expression of normal levels of functional delta-catenin.[7]


  1. ^ Re-solving the Cadherin-Catenin-Actin Conundrum by William I. Weis and W. James Nelson in Journal of Biological Chemistry (2006) Volume 281, pages 35593-35597.
  2. ^ N. Peyrieras, D. Louvard and F. Jacob. "Characterization of antigens recognized by monoclonal and polyclonal antibodies directed against uvomorulin" in Proceedings of the National Academy of Sciences of the United States of America (1985) Volume 82, pages 8067-8071. Full text at PMC: 2415979
  3. ^ M. Ozawa, H. Baribault and R. Kemler. "The cytoplasmic domain of the cell adhesion molecule uvomorulin associates with three independent proteins structurally related in different species" in The EMBO Journal (1989) Volume 8, pages 1711-1717. Full text at PMC: 2788574
  4. ^ a b Y. Fukunaga, H. Liu, M. Shimizu, S. Komiya, M. Kawasuji, A. Nagafuchi. "Defining the roles of beta-catenin and plakoglobin in cell-cell adhesion: isolation of beta-catenin/plakoglobin-deficient F9 cells" in Cell Structure and Function (2005) Volume 30, pages 25-34. Entrez PubMed 16357441
  5. ^ Anna Cattelino, Stefan Liebner, Radiosa Gallini, Adriana Zanetti, Giovanna Balconi, Alessandro Corsi, Paolo Bianco, Hartwig Wolburg, Robert Moore, Boussadia Oreda, Rolf Kemler and Elisabetta Dejana "The conditional inactivation of the beta-catenin gene in endothelial cells causes a defective vascular pattern and increased vascular fragility" in Journal of Cell Biology (2003) Volume 162, pages 1111-1122. doi:10.1083/jcb.200212157
  6. ^ Christiane Bierkamp, Heinz Schwarz, Otmar Huber and Rolf Kemler. Full text online: Desmosomal localization of beta-catenin in the skin of plakoglobin null-mutant mice in Development (1999) Volume 126, pages 371-381.
  7. ^ a b V. Vasioukhin, c. Bauer, L. Degenstein, B. Wise and E. Fuchs. "Hyperproliferation and defects in epithelial polarity upon conditional ablation of alpha-catenin in skin" in Cell (2001) Volume 104, pages 605-617. Entrez PubMed 11239416
  8. ^ A. Kobielak and E. Fuchs "Links between alpha-catenin, NF-kappaB, and squamous cell carcinoma in skin" in Proceedings of the National Academy of Sciences of the United States of America (2006) Volume 103, pages 2322-2327. Entrez PubMed 16452166
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Catenin". A list of authors is available in Wikipedia.
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