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Catenin (cadherin-associated protein), beta 1, 88kDa

PDB rendering based on 1dow.
Available structures
1dow, 1g3j, 1i7w, 1i7x, 1jdh, 1jpp, 1jpw, 1luj, 1m1e, 1qz7, 1t08, 1th1, 1v18, 2bct, 2gl7, 3bct
Symbols CTNNB1; CTNNB; FLJ25606
External IDs OMIM116806 MGI88276 HomoloGene1434 GeneCards: CTNNB1 Gene
RNA expression pattern
PBB GE CTNNB1 201533 at.png
More reference expression data
Species Human Mouse
Entrez 1499 12387
Ensembl ENSG00000168036 ENSMUSG00000006932
UniProt P35222 Q3UZT7
RefSeq (mRNA) XM_001133660 NM_007614
RefSeq (protein) XP_001133660 NP_031640
Location (UCSC) Chr 3:
41.22 - 41.26 Mb
Chr 9:
120.78 - 120.81 Mb
PubMed search [1] [2]
Figure 2. β-catenin (β) can interact with several different proteins inside cells. The interaction of β-catenin with other proteins is often regulated by the reversible attachment of phosphate (P).
Overview of signal transduction pathways involved in apoptosis.

Beta-catenin (or β-catenin) is a protein that in humans is encoded by the CTNNB1 gene.[1] In Drosophila, the homologous protein is called armadillo. β-catenin is a subunit of the cadherin protein complex and has been implicated as an integral component in the Wnt signaling pathway.



When β-catenin was sequenced it was found to be a member of the armadillo family of proteins. These proteins have multiple copies of the so-called armadillo repeat domain which is specialized for protein-protein binding. When β-catenin is not associated with cadherins and alpha-catenin, it can interact with other proteins such as ICAT and APC.


β-catenin is part of a complex of proteins that constitute adherens junctions (AJs). AJs are necessary for the creation and maintenance of epithelial cell layers by regulating cell growth and adhesion between cells. β-catenin also anchors the actin cytoskeleton and may be responsible for transmitting the contact inhibition signal that causes cells to stop dividing once the epithelial sheet is complete.[2]

Recent evidence suggests that β-catenin plays an important role in various aspects of liver biology including liver development (both embryonic and postnatal), liver regeneration following partial hepatectomy, HGF-induced hepatomegaly, liver zonation, and pathogenesis of liver cancer.[3]

Role in the Wnt signaling pathway

When Wnt is not present, GSK-3 (a kinase) constitutively phosphorylates the β-catenin protein. β-catenin is associated with axin (scaffolding protein) complexed with GSK3 and APC (adenomatosis polyposis coli). The creation of said complex acts to substantially increase the phosphorylation of β-catenin by facilitating the action of GSK3. When β-catenin is phosphorylated it is degraded and thus will not build up in the cell to a significant level. When Wnt binds to frizzled (Fz), its receptor, dishevelled (Dsh) is recruited to the membrane. GSK3 is inhibited by the activation of Dsh by Fz. Because of this, β-catenin is permitted to build up in the cytosol and can be subsequently translocated into the nucleus to perform a variety of functions. It can act in conjunction with TCF to activate specific genes as well as cause the export of TCF from the nucleus.

Clinical significance

β-catenin can function as an oncogene.[4] An increase in β-catenin production has been noted in those people who have basal cell carcinoma and leads to the increase in proliferation of related tumors.[5] Mutations in this gene are a cause of colorectal cancer (CRC), pilomatrixoma (PTR), medulloblastoma (MDB), and ovarian cancer. Finally, this protein binds to the product of the APC gene, which is mutated in adenomatous polyposis of the colon.

Interactions with other proteins

As mentioned above, β-catenin contains armadillo repeats and is able to bind to other proteins. Inside cells, β-catenin can be found in complexes with cadherins, transcription factors (TF in Figure 2) and other proteins such as axin, a component of the Wnt signalling pathway and galectin-3, beta-galactoside-binding protein. The ability of β-catenin to bind to other proteins is regulated by tyrosine kinases[6] and serine kinases such as GSK-3.[7]

When β-catenin is not assembled in complexes with cadherins, it can form a complex with axin. While bound to axin, β-catenin can be phosphorylated by GSK-3, which creates a signal for the rapid ubiquitin-dependent degradation of β-catenin by proteosomes. Various signals such as the Wnt signalling pathway can inhibit GSK-3-mediated phosphorylation of β-catenin,[8] allowing β-catenin to go to the cell nucleus, interact with transcription factors, and regulate gene transcription.

β-catenin can be phosphorylated by other kinases such as protein kinase A (PKA). Phosphorylation of β-catenin by PKA has been associated with reduced degradation of β-catenin, increased levels of β-catenin in the nucleus and interaction of β-catenin with TCF family transcription factors to regulate gene expression.[9]

In addition, β-catenin has been shown to interact with:

See also


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Further reading

  • Kikuchi A (2000). "Regulation of β-catenin signaling in the Wnt pathway.". Biochem. Biophys. Res. Commun. 268 (2): 243–8. doi:10.1006/bbrc.1999.1860. PMID 10679188.  
  • Wilson PD (2001). "Polycystin: new aspects of structure, function, and regulation.". J. Am. Soc. Nephrol. 12 (4): 834–45. PMID 11274246.  
  • Kalluri R, Neilson EG (2004). "Epithelial-mesenchymal transition and its implications for fibrosis.". J. Clin. Invest. 112 (12): 1776–84. doi:10.1172/JCI200320530. PMID 14679171.  
  • De Ferrari GV, Moon RT (2007). "The ups and downs of Wnt signaling in prevalent neurological disorders.". Oncogene 25 (57): 7545–53. doi:10.1038/sj.onc.1210064. PMID 17143299.  

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.



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