Beta-catenin

From Wikipedia, the free encyclopedia
Jump to: navigation, search
Catenin (cadherin-associated protein), beta 1, 88kDa

PDB rendering based on 2bct.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols CTNNB1; CTNNB; MRD19; armadillo
External IDs OMIM: 116806 MGI: 88276 HomoloGene: 1434 ChEMBL: 5866 GeneCards: CTNNB1 Gene
RNA expression pattern
PBB GE CTNNB1 201533 at.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 1499 12387
Ensembl ENSG00000168036 ENSMUSG00000006932
UniProt P35222 Q02248
RefSeq (mRNA) NM_001098209 NM_001165902
RefSeq (protein) NP_001091679 NP_001159374
Location (UCSC) Chr 3:
41.24 – 41.3 Mb		 Chr 9:
120.93 – 120.96 Mb
PubMed search [1] [2]
This box:
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 dual function protein, regulating the coordination of cell–cell adhesion and gene transcription. In humans, β-catenin is encoded by the CTNNB1 gene.[1][2] In Drosophila, the homologous protein is called armadillo. β-catenin is a subunit of the cadherin protein complex and acts as an intracellular signal transducer in the Wnt signaling pathway.[3][4][5] Overexpression of β-catenin has been associated with many cancers, including endometrial cancer.[6]

Contents

Structure [edit]

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 composed of three alpha helices. The first armadillo (arm) repeat, near the N-terminus, is different from all the others in that it has an elongated helix with a kink, formed by the fusion of helices 1 and 2.[7]

Structural element HelixC caps the C-terminus end of the arm repeats, shielding hydrophobic residues. It has been shown that HelixC is not necessary for β-catenin to function in cell-cell adhesion, but rather is important in the Wnt signaling pathway. HelixC is speculated to be involved in the recruitment and binding of β-catenin coactivators. Collectively, the unique N and C-terminal tails are hypothesized to increase specificity in protein-protein interactions, since they flank the less specific, more conserved arm repeats.[8]

Role in Cell-Cell Adhesion [edit]

In complex tissues, cell–cell adhesion complexes are essential for organization and maintenance. β-catenin is part of a complex of proteins that constitute adherens junctions. β-catenin plays a role in cell-cell adhesion by controlling cadherin-mediated cell adhesion at the plasma membrane and by mediating the interplay of adherens junction molecules with the actin cytoskeleton.[9] At the plasma membrane, β-catenin functions by linking E-cadherins (E-cad) to α-catenin (α-cat). Weak cell-cell adhesion occurs when cadherins form trans-interactions on opposing cell surfaces, while stronger cell–cell adhesion occurs through the clustering of cadherin and through changes in the organization of the actin cytoskeleton.[10]

As a component of adherens junctions, β-catenin binds to the intracellular domain of the transmembrane protein cadherin, a Ca2+-dependent adhesion molecule, and links cadherin to the actin cytoskeleton through the adaptor protein, α-catenin.[11] Organization and function of the cadherin–catenin complex are additionally regulated through the processes of phosphorylation and endocytosis.

Adheren junctions 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.[12] The E-cadherin–β-catenin–α-catenin linked complex at the adherens junctions allows for the formation of a dynamic, rather than a stable, link to the actin cytoskeleton.[9]

Connection between cell adhesion and transcription [edit]

β-catenin also serves as a pivot between the roles of cell adhesion and gene transcription.[11] The switch between these two cellular functions is controlled by several factors, including conformation and stability of the protein, the presence of E-cadherin-mediated cell adhesion, the presence of the BCL9 family of proto-oncogenes and by the tyrosine phosphorylation/de-phosphorylation of β-catenin.[13] Activation of the transmembrane tyrosine kinases EGFR and c-Met and overexpression of the tyrosine kinases, Src and FER both serve to downregulate E-cadherin-mediated adhesion and play a role in enhancing tyrosine phosphorylation of β-catenin.[14] Increased tyrosine phosphorylation leads to both a loss of adhesion and to an increase in transcription.

The proper regulation of these two functions has been shown to be crucial for the stages of normal development, with loss of regulation being linked to many cancers and malignancies.[9] BCL9 plays a critical role in controlling the β-catenin pivot from cell adhesion to Wnt signaling during normal and malignant development.[11]

Embryo development [edit]

β-Catenin is an essential compound for developmental viability of embryos and experimentally modified embryos that do not express this protein will fail to develop mesoderm and initiate gastrulation.[15] β-Catenin is initially localized in all regions of the embryo, but it is targeted for ubiquitination and degradation through phosphorylation by the enzyme GSK-3. GSK3 is inhibited by the activation of Dsh by Fz which allows β-catenin to build up in the cytosol and subsequently be translocated into the nucleus to perform a variety of functions. Fertilization of the egg causes a rotation of the outer cortical layers, moving these factors closer to the equatorial region. β-Catenin can only exist when stabilized by the influence of these signaling pathways. β-Catenin can then enter the nucleus and cause transcription factor Tcf3 to activate several genes that induce dorsal cell characteristics.[16] This signaling results in a region of cells known as the grey crescent, which in turn was identified as the classical organizer of embryonic induction. Early experiments revealed that when this region was surgically removed from the embryo, gastrulation did not occur. In combination with signals from the VgT and Vg1 pathways, β-Catenin induces the organizer to become the blastopore lip, which in turn initiates gastrulation.[17] Inhibition of GSK-3 translation by injection of antisense mRNA can cause a second blastopore and a superfluous body axis to form. A similar effect results from the over expression of β-Catenin.[18]

Role in the Wnt signaling pathway [edit]

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 (adenomatous 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 and LEF to activate specific target genes involved in different processes.[19]

Clinical significance [edit]

CTNNB1, the gene for β-catenin, is associated with many cancers and is thus considered an oncogene.[20] Increased nuclear β-catenin levels has been noted in basal cell carcinoma (BCC), head and neck squamous cell carcinoma (HNSCC), prostate cancer (CaP), colorectal cancer (CRC), pilomatrixoma (PTR), medulloblastoma (MDB), and ovarian cancer. In the nucleus, β-catenin interacts with TCF/LEF family transcription factors which go on to activate various oncogenes associated with growth and proliferation. β-catenin inhibitors can aid in the treatment of these cancers.[21] Overexpression of β-catenin can be caused by mutation of the β-catenin gene itself, by excessive Wnt signalling, or by the dissociation of the APC-axin-GSK-3 complex.[22]

Tumor proliferation in basal cell carcinoma has been correlated with increased nuclear β-catenin levels. The cause of this increase is speculated to be overexpression of Wnt ligands due to the lack of evidence for a β-catenin gene mutation.[23]

Overexpression of β-catenin in colorectal cancer has been attributed to an APC gene mutation. Adenomas were found to have higher than normal levels of cytoplasmic β-catenin yet lacked overexpressed nuclear β-catenin, while intramucosal cancers did have overexpressed nuclear β-catenin. This suggests that nuclear translocation of β-catenin affects adenoma-carcinoma progression. The aid provided by nuclear translocation to the development of intramucosal cancer is independent of APC gene mutation.[24]

Pilomatricoma is a benign skin tumor that is associated with the hair matrix. β-catenin expression has been correlated with terminal hair shaft differentiation. After the differentiation is completed, β-catenin expression ceases. However in Pilomatricoma, expression of β-catenin in high levels is present at all times, not only during the differentiation process. The exact cause of this overexpression is undetermined, speculated to be either a mutation in the APC gene or the β-catenin gene.[25]

Medulloblastoma is a pediatric brain tumor, sometimes associated with a β-catenin gene mutation. Medulloblastoma's with high levels of nuclear β-catenin, resulting from a β-catenin gene mutation, are shown to have a more favorable outcome than medulloblastoma's without nuclear β-catenin accumulation.[26]

The overexpression of β-catenin in prostate cancer is thought to be caused by excessive Wnt signalling. The overexpressed β-catenin can associate with TCF/LEF transcription factors to activate specific genes or can bind to the androgen receptor, which regulates prostate growth.[27]

The transduction of 'stable' β-catenin, containing alanine in place of the four serine or threonine residues so therefore are not affected by the GSK-3 degradation pathway, have been found to increase survival rates of regulatory T cells and induce anergy in naive CD25- nonregulatory T cells,[28] making stable β-catenin a candidate for further studies on its application with transplanted regulatory T cells to combat inflammatory and autoimmune diseases.

Interactions with other proteins [edit]

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[14] and serine kinases such as GSK-3.[29]

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,[30] 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.[31]

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

See also [edit]

References [edit]

  1. ^ Kraus C, Liehr T, Hülsken J, Behrens J, Birchmeier W, Grzeschik KH, Ballhausen WG (September 1994). "Localization of the human β-catenin gene (CTNNB1) to 3p21: a region implicated in tumor development". Genomics 23 (1): 272–4. doi:10.1006/geno.1994.1493. PMID 7829088. 
  2. ^ MacDonald BT, Tamai K, He X (July 2009). "Wnt/beta-catenin signaling: components, mechanisms, and diseases". Developmental Cell 17 (1): 9–26. doi:10.1016/j.devcel.2009.06.016. PMC 2861485. PMID 19619488. 
  3. ^ Peifer M, Rauskolb C, Williams M, Riggleman B, Wieschaus E (Apr 1991). "The segment polarity gene armadillo interacts with the wingless signaling pathway in both embryonic and adult pattern formation". Development 111 (4): 1029–1043. PMID 1879348. 
  4. ^ Noordermeer J, Klingensmith, J, Perrimon, N, Nusse, R (Jan 1994). "dishevelled and armadillo act in the wingless signalling pathway in Drosophila". Nature 367 (6458): 80–83. PMID 7906389. 
  5. ^ Peifer M, Berg S, Reynolds AB (March 1994). "A repeating amino acid motif shared by proteins with diverse cellular roles". Cell 76 (5): 789–91. PMID 7907279. 
  6. ^ Morin PJ (1999). "beta-catenin signaling and cancer". Bioessays (12):1021-30. PMID 10580987.
  7. ^ Gottardi CJ, Peifer M (March 2008). "Terminal regions of beta-catenin come into view". Structure 16 (3): 336–8. doi:10.1016/j.str.2008.02.005. PMC 2329800. PMID 18334207. 
  8. ^ Xing Y, Takemaru K, Liu J, Berndt JD, Zheng JJ, Moon RT, Xu W (March 2008). "Crystal structure of a full-length beta-catenin". Structure 16 (3): 478–87. doi:10.1016/j.str.2007.12.021. PMID 18334222. 
  9. ^ a b c Brembeck FH, Rosário M, Birchmeier W (February 2006). "Balancing cell adhesion and Wnt signalin], the key role of β-catenin". Curr. Opin. Genet. Dev. 16 (1): 51–9. doi:10.1016/j.gde.2005.12.007. PMID 16377174. 
  10. ^ Nelson WJ (April 2008). "Regulation of cell-cell adhesion by the cadherin-catenin complex". Biochem. Soc. Trans. 36 (Pt 2): 149–55. doi:10.1042/BST0360149. PMC 3368607. PMID 18363555. 
  11. ^ a b c Bienz M (January 2005). "β-Catenin: a pivot between cell adhesion and Wnt signalling". Curr. Biol. 15 (2): R64–7. doi:10.1016/j.cub.2004.12.058. PMID 15668160. 
  12. ^ "Entrez Gene: catenin (cadherin-associated protein)". 
  13. ^ Harris TJ, Peifer M (May 2005). "Decisions, decisions: β-catenin chooses between adhesion and transcription". Trends Cell Biol. 15 (5): 234–7. doi:10.1016/j.tcb.2005.03.002. PMID 15866026. 
  14. ^ a b Lilien J, Balsamo J (October 2005). "The regulation of cadherin-mediated adhesion by tyrosine phosphorylation/dephosphorylation of β-catenin". Curr. Opin. Cell Biol. 17 (5): 459–65. doi:10.1016/j.ceb.2005.08.009. PMID 16099633. 
  15. ^ Haegel H, Larue L, Ohsugi M, Fedorov L, Herrenknecht K, Kemler R (November 1995). "Lack of beta-catenin affects mouse development at gastrulation". Development 121 (11): 3529–37. PMID 8582267. 
  16. ^ Schneider S, Steinbeisser H, Warga RM, Hausen P (July 1996). "Beta-catenin translocation into nuclei demarcates the dorsalizing centers in frog and fish embryos". Mech. Dev. 57 (2): 191–8. PMID 8843396. 
  17. ^ Larabell CA, Torres M, Rowning BA, Yost C, Miller JR, Wu M, Kimelman D, Moon RT (March 1997). "Establishment of the dorso-ventral axis in Xenopus embryos is presaged by early asymmetries in beta-catenin that are modulated by the Wnt signaling pathway". J. Cell Biol. 136 (5): 1123–36. PMC 2132470. PMID 9060476. 
  18. ^ Kelly GM, Erezyilmaz DF, Moon RT (October 1995). "Induction of a secondary embryonic axis in zebrafish occurs following the overexpression of beta-catenin". Mech. Dev. 53 (2): 261–73. PMID 8562427. 
  19. ^ "Wnt / β-Catenin Signaling". Cell Signalling Technology. 
  20. ^ Wang X, Goode EL, Fredericksen ZS, Vierkant RA, Pankratz VS, Liu-Mares W, Rider DN, Vachon CM, Cerhan JR, Olson JE, Couch FJ (August 2008). "Association of genetic variation in genes implicated in the beta-catenin destruction complex with risk of breast cancer". Cancer Epidemiol. Biomarkers Prev. 17 (8): 2101–8. doi:10.1158/1055-9965.EPI-08-0134. PMC 2771409. PMID 18708403. 
  21. ^ Maher S Saifo, Donald R Rempinski, Youcef M Rustum, Rami G Azrak (2010). "Targeting the oncogenic protein beta-catenin to enhance chemotherapy outcome against solid human cancers". Molecular Cancer 9:310. doi:10.1186/1476-4598-9-310. PMID 21126356.
  22. ^ Polakis P (Feb. 1999). "The oncogenic activation of beta-catenin". Curr Opin Genet Dev (1):15-21. PMID 10072352
  23. ^ Saldanha G, Ghura V, Potter L, Fletcher A (July 2004). "Nuclear β-catenin in basal cell carcinoma correlates with increased proliferation". Br. J. Dermatol. 151 (1): 157–64. doi:10.1111/j.1365-2133.2004.06048.x. PMID 15270885. 
  24. ^ M Kobayashi, T Honma, Y Matsuda, Y Suzuki, R Narisawa, Y Ajioka, H Asakura (May 2000). "Nuclear translocation of beta-catenin in colorectal cancer". Br J Cancer (10): 1689–1693. doi: 10.1054/bjoc.1999.1112. PMID 10817505.
  25. ^ Ashraf M. Hassanein, Steven M. Glanz, Harvey P. Kessler, Thomas A. Eskin, Chen Liu (2003). "β-Catenin Is Expressed Aberrantly in Tumors Expressing Shadow Cells". Anatomic Pathology (5):732-6. doi: 10.1309/EALEG7LD6W7167PX. PMID 14608900.
  26. ^ Ellison DW, Onilude OE, Lindsey JC, Lusher ME, Weston CL, Taylor RE, Pearson AD, Clifford SC; United Kingdom Children's Cancer Study Group Brain Tumour Committee (Nov. 2005). "beta-Catenin status predicts a favorable outcome in childhood medulloblastoma: the United Kingdom Children's Cancer Study Group Brain Tumour Committee". J Clin Oncol (31):7951-7. PMID 16258095.
  27. ^ Kypta RM, Waxman J (Jun. 2012). "Wnt/β-catenin signalling in prostate cancer". Nat Rev Urol. doi: 10.1038/nrurol.2012.116. PMID 22710668
  28. ^ Yi Ding, Shiqian Shen, Andreia C Lino, Maria A Curotto de Lafaille, Juan J Lafaille (2008). "Beta-catenin stabilization extends regulatory T cell survival and induces anergy in nonregulatory T cells". Nature Medicine 14 (2): 162. 
  29. ^ Castellone MD, Teramoto H, Williams BO, Druey KM, Gutkind JS (December 2005). "Prostaglandin E2 promotes colon cancer cell growth through a Gs-axin-beta-catenin signaling axis". Science 310 (5753): 1504–10. doi:10.1126/science.1116221. PMID 16293724. 
  30. ^ Liu X, Rubin JS, Kimmel AR (November 2005). "Rapid, Wnt-induced changes in GSK3beta associations that regulate beta-catenin stabilization are mediated by Galpha proteins". Curr. Biol. 15 (22): 1989–97. doi:10.1016/j.cub.2005.10.050. PMID 16303557. 
  31. ^ Hino S, Tanji C, Nakayama KI, Kikuchi A (October 2005). "Phosphorylation of β-Catenin by Cyclic AMP-Dependent Protein Kinase Stabilizes β-Catenin through Inhibition of Its Ubiquitination". Mol. Cell. Biol. 25 (20): 9063–72. doi:10.1128/MCB.25.20.9063-9072.2005. PMC 1265785. PMID 16199882. 
  32. ^ Yang, Fajun; Li Xiaoyu, Sharma Manju, Sasaki Carl Y, Longo Dan L, Lim Bing, Sun Zijie (Mar. 2002). "Linking β-catenin to androgen-signaling pathway". J. Biol. Chem. 277 (13): 11336–44. doi:10.1074/jbc.M111962200. PMID 11792709. 
  33. ^ Masiello, David; Chen Shao-Yong, Xu Youyuan, Verhoeven Manon C, Choi Eunis, Hollenberg Anthony N, Balk Steven P (Oct. 2004). "Recruitment of β-catenin by wild-type or mutant androgen receptors correlates with ligand-stimulated growth of prostate cancer cells". Mol. Endocrinol. 18 (10): 2388–401. doi:10.1210/me.2003-0436. PMID 15256534. 
  34. ^ Song, Liang-Nian; Coghlan Meghan, Gelmann Edward P (Jan. 2004). "Antiandrogen effects of mifepristone on coactivator and corepressor interactions with the androgen receptor". Mol. Endocrinol. 18 (1): 70–85. doi:10.1210/me.2003-0189. PMID 14593076. 
  35. ^ Amir, Avital L; Barua Moumita, McKnight Nicole C, Cheng Shinta, Yuan Xin, Balk Steven P (Aug. 2003). "A direct β-catenin-independent interaction between androgen receptor and T cell factor 4". J. Biol. Chem. 278 (33): 30828–34. doi:10.1074/jbc.M301208200. PMID 12799378. 
  36. ^ a b Mulholland, David J; Read Jason T, Rennie Paul S, Cox Michael E, Nelson Colleen C (Aug. 2003). "Functional localization and competition between the androgen receptor and T-cell factor for nuclear β-catenin: a means for inhibition of the Tcf signaling axis". Oncogene 22 (36): 5602–13. doi:10.1038/sj.onc.1206802. PMID 12944908. 
  37. ^ Pawlowski, John E; Ertel Jessica R, Allen Melissa P, Xu Mei, Butler Cheryl, Wilson Elizabeth M, Wierman Margaret E (Jun. 2002). "Liganded androgen receptor interaction with β-catenin: nuclear co-localization and modulation of transcriptional activity in neuronal cells". J. Biol. Chem. 277 (23): 20702–10. doi:10.1074/jbc.M200545200. PMID 11916967. 
  38. ^ Su, L K; Vogelstein B, Kinzler K W (Dec. 1993). "Association of the APC tumor suppressor protein with catenins". Science 262 (5140): 1734–7. doi:10.1126/science.8259519. PMID 8259519. 
  39. ^ a b c d Kucerová, D; Sloncová E, Tuhácková Z, Vojtechová M, Sovová V (Dec. 2001). "Expression and interaction of different catenins in colorectal carcinoma cells". Int. J. Mol. Med. (Greece) 8 (6): 695–8. PMID 11712088. 
  40. ^ Tickenbrock, Lara; Kössmeier Katja, Rehmann Holger, Herrmann Christian, Müller Oliver (Mar. 2003). "Differences between the interaction of β-catenin with non-phosphorylated and single-mimicked phosphorylated 20-amino acid residue repeats of the APC protein". J. Mol. Biol. 327 (2): 359–67. doi:10.1016/S0022-2836(03)00144-X. PMID 12628243. 
  41. ^ a b Davies, G; Jiang W G, Mason M D (Apr. 2001). "The interaction between β-catenin, GSK3β and APC after motogen induced cell-cell dissociation, and their involvement in signal transduction pathways in prostate cancer". Int. J. Oncol. (Greece) 18 (4): 843–7. PMID 11251183. 
  42. ^ Ryo, A; Nakamura M, Wulf G, Liou Y C, Lu K P (Sep. 2001). "Pin1 regulates turnover and subcellular localization of β-catenin by inhibiting its interaction with APC". Nat. Cell Biol. 3 (9): 793–801. doi:10.1038/ncb0901-793. PMID 11533658. 
  43. ^ Homma, Miwako Kato; Li Dongxia, Krebs Edwin G, Yuasa Yasuhito, Homma Yoshimi (Apr. 2002). "Association and regulation of casein kinase 2 activity by adenomatous polyposis coli protein". Proc. Natl. Acad. Sci. U.S.A. 99 (9): 5959–64. doi:10.1073/pnas.092143199. PMC 122884. PMID 11972058. 
  44. ^ Satoh, K; Yanai H, Senda T, Kohu K, Nakamura T, Okumura N, Matsumine A, Kobayashi S, Toyoshima K, Akiyama T (Jun. 1997). "DAP-1, a novel protein that interacts with the guanylate kinase-like domains of hDLG and PSD-95". Genes Cells 2 (6): 415–24. doi:10.1046/j.1365-2443.1997.1310329.x. PMID 9286858. 
  45. ^ Eklof Spink, K; Fridman S G, Weis W I (Nov. 2001). "Molecular mechanisms of β-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC–β-catenin complex". EMBO J. 20 (22): 6203–12. doi:10.1093/emboj/20.22.6203. PMC 125720. PMID 11707392. 
  46. ^ Nakamura, T; Hamada F, Ishidate T, Anai K, Kawahara K, Toyoshima K, Akiyama T (Jun. 1998). "Axin, an inhibitor of the Wnt signalling pathway, interacts with β-catenin, GSK-3β and APC and reduces the β-catenin level". Genes Cells 3 (6): 395–403. doi:10.1046/j.1365-2443.1998.00198.x. PMID 9734785. 
  47. ^ Hocevar, B A; Mou F, Rennolds J L, Morris S M, Cooper J A, Howe P H (Jun. 2003). "Regulation of the Wnt signaling pathway by disabled-2 (Dab2)". EMBO J. 22 (12): 3084–94. doi:10.1093/emboj/cdg286. PMC 162138. PMID 12805222. 
  48. ^ Takemaru, Ken-Ichi; Yamaguchi Shinji, Lee Young Sik, Zhang Yang, Carthew Richard W, Moon Randall T (Apr. 2003). "Chibby, a nuclear β-catenin-associated antagonist of the Wnt/Wingless pathway". Nature 422 (6934): 905–9. doi:10.1038/nature01570. PMID 12712206. 
  49. ^ Davies, G; Jiang W G, Mason M D (Apr. 2001). "HGF/SF modifies the interaction between its receptor c-Met, and the E-cadherin/catenin complex in prostate cancer cells". Int. J. Mol. Med. (Greece) 7 (4): 385–8. PMID 11254878. 
  50. ^ a b Oyama, T; Kanai Y, Ochiai A, Akimoto S, Oda T, Yanagihara K, Nagafuchi A, Tsukita S, Shibamoto S, Ito F (Dec. 1994). "A truncated β-catenin disrupts the interaction between E-cadherin and alpha-catenin: a cause of loss of intercellular adhesiveness in human cancer cell lines". Cancer Res. 54 (23): 6282–7. PMID 7954478. 
  51. ^ Hazan, R B; Kang L, Roe S, Borgen P I, Rimm D L (Dec. 1997). "Vinculin is associated with the E-cadherin adhesion complex". J. Biol. Chem. 272 (51): 32448–53. doi:10.1074/jbc.272.51.32448. PMID 9405455. 
  52. ^ Kinch, M S; Clark G J, Der C J, Burridge K (Jul. 1995). "Tyrosine phosphorylation regulates the adhesions of ras-transformed breast epithelia". J. Cell Biol. 130 (2): 461–71. doi:10.1083/jcb.130.2.461. PMC 2199929. PMID 7542250. 
  53. ^ Jiang, Ming-Chung; Liao Ching-Fong, Tai Chia-Chen (Jun. 2002). "CAS/CSE 1 stimulates E-cadhrin-dependent cell polarity in HT-29 human colon epithelial cells". Biochem. Biophys. Res. Commun. 294 (4): 900–5. doi:10.1016/S0006-291X(02)00551-X. ISSN 0006-291X. PMID 12061792. 
  54. ^ a b c d Hazan, R B; Norton L (Apr. 1998). "The epidermal growth factor receptor modulates the interaction of E-cadherin with the actin cytoskeleton". J. Biol. Chem. 273 (15): 9078–84. doi:10.1074/jbc.273.15.9078. PMID 9535896. 
  55. ^ a b c Bonvini, P; An W G, Rosolen A, Nguyen P, Trepel J, Garcia de Herreros A, Dunach M, Neckers L M (Feb. 2001). "Geldanamycin abrogates ErbB2 association with proteasome-resistant β-catenin in melanoma cells, increases β-catenin-E-cadherin association, and decreases β-catenin-sensitive transcription". Cancer Res. 61 (4): 1671–7. PMID 11245482. 
  56. ^ a b Li, Y; Bharti A, Chen D, Gong J, Kufe D (Dec. 1998). "Interaction of Glycogen Synthase Kinase 3β with the DF3/MUC1 Carcinoma-Associated Antigen and β-Catenin". Mol. Cell. Biol. 18 (12): 7216–24. PMC 109303. PMID 9819408. 
  57. ^ Wendeler, M W; Praus M, Jung R, Hecking M, Metzig C, Gessner R (Apr. 2004). "Ksp-cadherin is a functional cell-cell adhesion molecule related to LI-cadherin". Exp. Cell Res. 294 (2): 345–55. doi:10.1016/j.yexcr.2003.11.022. PMID 15023525. 
  58. ^ a b Shibata, Tatsuhiro; Chuma Makoto, Kokubu Akiko, Sakamoto Michiie, Hirohashi Setsuo (Jul. 2003). "EBP50, a β-catenin-associating protein, enhances Wnt signaling and is over-expressed in hepatocellular carcinoma". Hepatology 38 (1): 178–86. doi:10.1053/jhep.2003.50270. PMID 12830000. 
  59. ^ a b Piedra, Jose; Miravet Susana, Castaño Julio, Pálmer Héctor G, Heisterkamp Nora, García de Herreros Antonio, Duñach Mireia (Apr. 2003). "p120 Catenin-Associated Fer and Fyn Tyrosine Kinases Regulate β-Catenin Tyr-142 Phosphorylation and β-Catenin-α-Catenin Interaction". Mol. Cell. Biol. 23 (7): 2287–97. doi:10.1128/MCB.23.7.2287-2297.2003. PMC 150740. PMID 12640114. 
  60. ^ Kang, Jong-Sun; Feinleib Jessica L, Knox Sarah, Ketteringham Michael A, Krauss Robert S (Apr. 2003). "Promyogenic members of the Ig and cadherin families associate to positively regulate differentiation". Proc. Natl. Acad. Sci. U.S.A. 100 (7): 3989–94. doi:10.1073/pnas.0736565100. PMC 153035. PMID 12634428. 
  61. ^ Oneyama, Chitose; Nakano Hirofumi, Sharma Sreenath V (Mar. 2002). "UCS15A, a novel small molecule, SH3 domain-mediated protein-protein interaction blocking drug". Oncogene 21 (13): 2037–50. doi:10.1038/sj.onc.1205271. PMID 11960376. 
  62. ^ Navarro, P; Lozano E, Cano A (Aug. 1993). "Expression of E- or P-cadherin is not sufficient to modify the morphology and the tumorigenic behavior of murine spindle carcinoma cells. Possible involvement of plakoglobin". J. Cell. Sci. 105 (4): 923–34. PMID 8227214. 
  63. ^ a b Takahashi, K; Suzuki K, Tsukatani Y (Jul. 1997). "Induction of tyrosine phosphorylation and association of β-catenin with EGF receptor upon tryptic digestion of quiescent cells at confluence". Oncogene 15 (1): 71–8. doi:10.1038/sj.onc.1201160. PMID 9233779. 
  64. ^ a b Dobrosotskaya, I Y; James G L (Apr. 2000). "MAGI-1 interacts with β-catenin and is associated with cell-cell adhesion structures". Biochem. Biophys. Res. Commun. 270 (3): 903–9. doi:10.1006/bbrc.2000.2471. ISSN 0006-291X. PMID 10772923. 
  65. ^ Geng, L; Burrow C R, Li H P, Wilson P D (Dec. 2000). "Modification of the composition of polycystin-1 multiprotein complexes by calcium and tyrosine phosphorylation". Biochim. Biophys. Acta (NETHERLANDS) 1535 (1): 21–35. doi:10.1016/S0925-4439(00)00079-X. PMID 11113628. 
  66. ^ Shibamoto, S; Hayakawa M, Takeuchi K, Hori T, Miyazawa K, Kitamura N, Johnson K R, Wheelock M J, Matsuyoshi N, Takeichi M (Mar. 1995). "Association of p120, a tyrosine kinase substrate, with E- cadherin/catenin complexes". J. Cell Biol. 128 (5): 949–57. doi:10.1083/jcb.128.5.949. PMC 2120395. PMID 7876318. 
  67. ^ Rao, Radhakrishna K; Basuroy Shyamali, Rao Vijay U, Karnaky Jr Karl J, Gupta Akshay (Dec. 2002). "Tyrosine phosphorylation and dissociation of occludin-ZO-1 and E-cadherin-beta-catenin complexes from the cytoskeleton by oxidative stress". Biochem. J. 368 (Pt 2): 471–81. doi:10.1042/BJ20011804. PMC 1222996. PMID 12169098. 
  68. ^ Huber, A H; Weis W I (May. 2001). "The structure of the β-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by β-catenin". Cell 105 (3): 391–402. doi:10.1016/S0092-8674(01)00330-0. PMID 11348595. 
  69. ^ a b Schmeiser, K; Grand R J (Apr. 1999). "The fate of E- and P-cadherin during the early stages of apoptosis". Cell Death Differ. 6 (4): 377–86. doi:10.1038/sj.cdd.4400504. PMID 10381631. 
  70. ^ Pai, Rama; Dunlap Debra, Qing Jing, Mohtashemi Iman, Hotzel Kathy, French Dorothy M (Jul. 2008). "Inhibition of fibroblast growth factor 19 reduces tumor growth by modulating β-catenin signaling". Cancer Res. 68 (13): 5086–95. doi:10.1158/0008-5472.CAN-07-2325. PMID 18593907. 
  71. ^ Straub, Beate K; Boda Judit, Kuhn Caecilia, Schnoelzer Martina, Korf Ulrike, Kempf Tore, Spring Herbert, Hatzfeld Mechthild, Franke Werner W (Dec. 2003). "A novel cell-cell junction system: the cortex adhaerens mosaic of lens fiber cells". J. Cell. Sci. 116 (Pt 24): 4985–95. doi:10.1242/jcs.00815. PMID 14625392. 
  72. ^ Wahl, James K; Kim Young J, Cullen Janet M, Johnson Keith R, Wheelock Margaret J (May. 2003). "N-cadherin-catenin complexes form prior to cleavage of the proregion and transport to the plasma membrane". J. Biol. Chem. 278 (19): 17269–76. doi:10.1074/jbc.M211452200. PMID 12604612. 
  73. ^ Klingelhöfer, J; Troyanovsky R B, Laur O Y, Troyanovsky S (Aug. 2000). "Amino-terminal domain of classic cadherins determines the specificity of the adhesive interactions". J. Cell. Sci. 113 (16): 2829–36. PMID 10910767. 
  74. ^ Kesavapany, S; Lau K F, McLoughlin D M, Brownlees J, Ackerley S, Leigh P N, Shaw C E, Miller C C (Jan. 2001). "p35/cdk5 binds and phosphorylates β-catenin and regulates β-catenin/presenilin-1 interaction". Eur. J. Neurosci. (France) 13 (2): 241–7. doi:10.1046/j.1460-9568.2001.01376.x. ISSN 0953-816X. PMID 11168528. 
  75. ^ a b Lamberti, C; Lin K M, Yamamoto Y, Verma U, Verma I M, Byers S, Gaynor R B (Nov. 2001). "Regulation of β-catenin function by the IkappaB kinases". J. Biol. Chem. 276 (45): 42276–86. doi:10.1074/jbc.M104227200. PMID 11527961. 
  76. ^ Roe, S; Koslov E R, Rimm D L (Jun. 1998). "A mutation in alpha-catenin disrupts adhesion in clone A cells without perturbing its actin and β-catenin binding activity". Cell Adhes. Commun. (SWITZERLAND) 5 (4): 283–96. doi:10.3109/15419069809040298. PMID 9762469. 
  77. ^ Aberle, H; Butz S, Stappert J, Weissig H, Kemler R, Hoschuetzky H (Dec. 1994). "Assembly of the cadherin-catenin complex in vitro with recombinant proteins". J. Cell. Sci. 107 (12): 3655–63. PMID 7706414. 
  78. ^ Reuver, S M; Garner C C (Apr. 1998). "E-cadherin mediated cell adhesion recruits SAP97 into the cortical cytoskeleton". J. Cell. Sci. 111 (8): 1071–80. PMID 9512503. 
  79. ^ a b Schroeder, Joyce A; Adriance Melissa C, McConnell Elizabeth J, Thompson Melissa C, Pockaj Barbara, Gendler Sandra J (Jun. 2002). "ErbB-β-catenin complexes are associated with human infiltrating ductal breast and murine mammary tumor virus (MMTV)-Wnt-1 and MMTV-c-Neu transgenic carcinomas". J. Biol. Chem. 277 (25): 22692–8. doi:10.1074/jbc.M201975200. PMID 11950845. 
  80. ^ Wei, Yu; Renard Claire-Angélique, Labalette Charlotte, Wu Yuanfei, Lévy Laurence, Neuveut Christine, Prieur Xavier, Flajolet Marc, Prigent Sylvie, Buendia Marie-Annick (Feb. 2003). "Identification of the LIM protein FHL2 as a coactivator of β-catenin". J. Biol. Chem. 278 (7): 5188–94. doi:10.1074/jbc.M207216200. PMID 12466281. 
  81. ^ Kishida, S; Yamamoto H, Hino S, Ikeda S, Kishida M, Kikuchi A (Jun. 1999). "DIX Domains of Dvl and Axin Are Necessary for Protein Interactions and Their Ability To Regulate β-Catenin Stability". Mol. Cell. Biol. 19 (6): 4414–22. PMC 104400. PMID 10330181. 
  82. ^ Kanai, Y; Ochiai A, Shibata T, Oyama T, Ushijima S, Akimoto S, Hirohashi S (Mar. 1995). "c-erbB-2 gene product directly associates with β-catenin and plakoglobin". Biochem. Biophys. Res. Commun. 208 (3): 1067–72. doi:10.1006/bbrc.1995.1443. ISSN 0006-291X. PMID 7702605. 
  83. ^ a b Edlund, Sofia; Lee So Young, Grimsby Susanne, Zhang Shouthing, Aspenström Pontus, Heldin Carl-Henrik, Landström Maréne (Feb. 2005). "Interaction between Smad7 and β-Catenin: Importance for Transforming Growth Factor β-Induced Apoptosis". Mol. Cell. Biol. 25 (4): 1475–88. doi:10.1128/MCB.25.4.1475-1488.2005. PMC 548008. PMID 15684397. 
  84. ^ Grueneberg, Dorre A; Pablo Lourdes, Hu Kang-Quan, August Paul, Weng Zhigang, Papkoff Jacqueline (Jun. 2003). "A Functional Screen in Human Cells Identifies UBF2 as an RNA Polymerase II Transcription Factor That Enhances the β-Catenin Signaling Pathway". Mol. Cell. Biol. 23 (11): 3936–50. doi:10.1128/MCB.23.11.3936-3950.2003. PMC 155208. PMID 12748295. 
  85. ^ Behrens, J; von Kries J P, Kühl M, Bruhn L, Wedlich D, Grosschedl R, Birchmeier W (Aug. 1996). "Functional interaction of β-catenin with the transcription factor LEF-1". Nature 382 (6592): 638–42. doi:10.1038/382638a0. PMID 8757136. 
  86. ^ Labbé, E; Letamendia A, Attisano L (Jul. 2000). "Association of Smads with lymphoid enhancer binding factor 1/T cell-specific factor mediates cooperative signaling by the transforming growth factor-β and Wnt pathways". Proc. Natl. Acad. Sci. U.S.A. 97 (15): 8358–63. doi:10.1073/pnas.150152697. PMC 26952. PMID 10890911. 
  87. ^ Yamamoto, M; Bharti A, Li Y, Kufe D (May. 1997). "Interaction of the DF3/MUC1 breast carcinoma-associated antigen and β-catenin in cell adhesion". J. Biol. Chem. 272 (19): 12492–4. doi:10.1074/jbc.272.19.12492. PMID 9139698. 
  88. ^ Li, Yongqing; Chen Wen, Ren Jian, Yu Wei-Hsuan, Li Quan, Yoshida Kiyotsugu, Kufe Donald (2003). "DF3/MUC1 signaling in multiple myeloma cells is regulated by interleukin-7". Cancer Biol. Ther. 2 (2): 187–93. PMID 12750561. 
  89. ^ Schroeder, Joyce A; Adriance Melissa C, Thompson Melissa C, Camenisch Todd D, Gendler Sandra J (Mar. 2003). "MUC1 alters β-catenin-dependent tumor formation and promotes cellular invasion". Oncogene 22 (9): 1324–32. doi:10.1038/sj.onc.1206291. PMID 12618757. 
  90. ^ Li, Y; Kuwahara H, Ren J, Wen G, Kufe D (Mar. 2001). "The c-Src tyrosine kinase regulates signaling of the human DF3/MUC1 carcinoma-associated antigen with GSK3 β and β-catenin". J. Biol. Chem. 276 (9): 6061–4. doi:10.1074/jbc.C000754200. PMID 11152665. 
  91. ^ Ren, Jian; Li Yongqing, Kufe Donald (May. 2002). "Protein kinase C delta regulates function of the DF3/MUC1 carcinoma antigen in β-catenin signaling". J. Biol. Chem. 277 (20): 17616–22. doi:10.1074/jbc.M200436200. PMID 11877440. 
  92. ^ Li, Y; Ren J, Yu W, Li Q, Kuwahara H, Yin L, Carraway K L, Kufe D (Sep. 2001). "The epidermal growth factor receptor regulates interaction of the human DF3/MUC1 carcinoma antigen with c-Src and β-catenin". J. Biol. Chem. 276 (38): 35239–42. doi:10.1074/jbc.C100359200. PMID 11483589. 
  93. ^ Kennell, Jennifer A; O'Leary Erin E, Gummow Brian M, Hammer Gary D, MacDougald Ormond A (Aug. 2003). "T-Cell Factor 4N (TCF-4N), a Novel Isoform of Mouse TCF-4, Synergizes with β-Catenin To Coactivate C/EBPα and Steroidogenic Factor 1 Transcription Factors". Mol. Cell. Biol. 23 (15): 5366–75. doi:10.1128/MCB.23.15.5366-5375.2003. PMC 165725. PMID 12861022. 
  94. ^ Mizusaki, Hirofumi; Kawabe Ken, Mukai Tokuo, Ariyoshi Etsuko, Kasahara Megumi, Yoshioka Hidefumi, Swain Amanda, Morohashi Ken-Ichirou (Apr. 2003). "Dax-1 (dosage-sensitive sex reversal-adrenal hypoplasia congenita critical region on the X chromosome, gene 1) gene transcription is regulated by wnt4 in the female developing gonad". Mol. Endocrinol. 17 (4): 507–19. doi:10.1210/me.2002-0362. PMID 12554773. 
  95. ^ Ge, Xinjian; Jin Qihuang, Zhang Fang, Yan Tingting, Zhai Qiwei (Jan. 2009). "PCAF acetylates {β}-catenin and improves its stability". Mol. Biol. Cell 20 (1): 419–27. doi:10.1091/mbc.E08-08-0792. PMID 18987336. 
  96. ^ Chitalia, Vipul C; Foy Rebecca L, Bachschmid Markus M, Zeng Liling, Panchenko Maria V, Zhou Mina I, Bharti Ajit, Seldin David C, Lecker Stewart H, Dominguez Isabel, Cohen Herbert T (Oct. 2008). "Jade-1 inhibits Wnt signaling by ubiquitinating β-catenin and mediates Wnt pathway inhibition by pVHL". Nat. Cell Biol. 10 (10): 1208–16. doi:10.1038/ncb1781. PMC 2830866. PMID 18806787. 
  97. ^ Wadham, Carol; Gamble Jennifer R, Vadas Mathew A, Khew-Goodall Yeesim (Jun. 2003). "The Protein Tyrosine Phosphatase Pez Is a Major Phosphatase of Adherens Junctions and Dephosphorylates β-Catenin". Mol. Biol. Cell 14 (6): 2520–9. doi:10.1091/mbc.E02-09-0577. PMC 194899. PMID 12808048. 
  98. ^ Aicher, B; Lerch M M, Müller T, Schilling J, Ullrich A (Aug. 1997). "Cellular Redistribution of Protein Tyrosine Phosphatases LAR and PTPσ by Inducible Proteolytic Processing". J. Cell Biol. 138 (3): 681–96. doi:10.1083/jcb.138.3.681. PMC 2141638. PMID 9245795. 
  99. ^ Fuchs, M; Müller T, Lerch M M, Ullrich A (Jul. 1996). "Association of human protein-tyrosine phosphatase kappa with members of the armadillo family". J. Biol. Chem. 271 (28): 16712–9. doi:10.1074/jbc.271.28.16712. PMID 8663237. 
  100. ^ Besco JA, Hooft van Huijsduijnen R, Frostholm A, Rotter A (2006). "Intracellular substrates of brain-enriched receptor protein tyrosine phosphatase rho (RPTPrho/PTPRT).". Brain Res 1116 (1): 50–7. doi:10.1016/j.brainres.2006.07.122. PMID 16973135. 
  101. ^ Wang B, Kishihara K, Zhang D, Hara H, Nomoto K (February 1997). "Molecular cloning and characterization of a novel human receptor protein tyrosine phosphatase gene, hPTP-J: down-regulation of gene expression by PMA and calcium ionophore in Jurkat T lymphoma cells". Biochem. Biophys. Res. Commun. 231 (1): 77–81. doi:10.1006/bbrc.1997.6004. PMID 9070223. 
  102. ^ Yan HX, He YQ, Dong H, Zhang P, Zeng JZ, Cao HF, Wu MC, Wang HY (December 2002). "Physical and functional interaction between receptor-like protein tyrosine phosphatase PCP-2 and beta-catenin". Biochemistry 41 (52): 15854–60. PMID 12501215. 
  103. ^ He Y, Yan H, Dong H, Zhang P, Tang L, Qiu X, Wu M, Wang H (April 2005). "Structural basis of interaction between protein tyrosine phosphatase PCP-2 and beta-catenin". Sci. China, C, Life Sci. 48 (2): 163–7. PMID 15986889. 
  104. ^ Tesco, G; Kim T W, Diehlmann A, Beyreuther K, Tanzi R E (Dec. 1998). "Abrogation of the presenilin 1/β-catenin interaction and preservation of the heterodimeric presenilin 1 complex following caspase activation". J. Biol. Chem. 273 (51): 33909–14. doi:10.1074/jbc.273.51.33909. PMID 9852041. 
  105. ^ Kang, D E; Soriano S, Frosch M P, Collins T, Naruse S, Sisodia S S, Leibowitz G, Levine F, Koo E H (Jun. 1999). "Presenilin 1 facilitates the constitutive turnover of β-catenin: differential activity of Alzheimer's disease-linked PS1 mutants in the β-catenin-signaling pathway". J. Neurosci. 19 (11): 4229–37. PMID 10341227. 
  106. ^ Murayama, M; Tanaka S, Palacino J, Murayama O, Honda T, Sun X, Yasutake K, Nihonmatsu N, Wolozin B, Takashima A (Aug. 1998). "Direct association of presenilin-1 with β-catenin". FEBS Lett. (NETHERLANDS) 433 (1–2): 73–7. doi:10.1016/S0014-5793(98)00886-2. PMID 9738936. 
  107. ^ Bauer, A; Huber O, Kemler R (Dec. 1998). "Pontin52, an interaction partner of β-catenin, binds to the TATA box binding protein". Proc. Natl. Acad. Sci. U.S.A. 95 (25): 14787–92. doi:10.1073/pnas.95.25.14787. PMC 24527. PMID 9843967. 
  108. ^ Barker, N; Hurlstone A, Musisi H, Miles A, Bienz M, Clevers H (Sep. 2001). "The chromatin remodelling factor Brg-1 interacts with β-catenin to promote target gene activation". EMBO J. 20 (17): 4935–43. doi:10.1093/emboj/20.17.4935. PMC 125268. PMID 11532957. 
  109. ^ Taya, S; Yamamoto T, Kanai-Azuma M, Wood S A, Kaibuchi K (Dec. 1999). "The deubiquitinating enzyme Fam interacts with and stabilizes β-catenin". Genes Cells 4 (12): 757–67. doi:10.1046/j.1365-2443.1999.00297.x. PMID 10620020. 
  110. ^ Lewalle, J M; Bajou K, Desreux J, Mareel M, Dejana E, Noël A, Foidart J M (Dec. 1997). "Alteration of interendothelial adherens junctions following tumor cell-endothelial cell interaction in vitro". Exp. Cell Res. 237 (2): 347–56. doi:10.1006/excr.1997.3799. PMID 9434630. 
  111. ^ Shasby, D Michael; Ries Dana R, Shasby Sandra S, Winter Michael C (Jun. 2002). "Histamine stimulates phosphorylation of adherens junction proteins and alters their link to vimentin". Am. J. Physiol. Lung Cell Mol. Physiol. 282 (6): L1330–8. doi:10.1152/ajplung.00329.2001 (inactive 2010-03-12). PMID 12003790. 
  112. ^ Puppo, F; Thomé V, Lhoumeau AC, Cibois M, Gangar A, Lembo F, Belotti E, Marchetto S, Lécine P, Prébet T, Sebbagh M, Shin WS, Lee ST, Kodjabachian L, Borg JP (Dec. 2010). "Protein tyrosine kinase 7 has a conserved role in Wnt/β-catenin canonical signalling". EMBO Rep. Epub ahead of print (1): 43–9. doi:10.1038/embor.2010.185. PMC 3024124. PMID 21132015. 

Further reading [edit]

External links [edit]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.
Human
Microfilaments
(ABPs)
Myofilament
Actins
Myosins
Other
Other
IFs
Type 1/2
(Keratin,
Cytokeratin)
Epithelial keratins
(soft alpha-keratins)
Hair keratins
(hard alpha-keratins)
Ungrouped alpha
Not alpha
Type 3
Type 4
Type 5
Microtubules/
MAPs
Kinesins
Dyneins
Other
Catenins
Membrane
Other
Nonhuman
Ligand
Receptor
Second messenger
Ligand
Receptor
Intracellular signaling P+Ps
  • ONCO: Beta-catenin
  • TSP: APC
Other/unknown
Nucleus
Mitochondria
Other/ungrouped
Retrieved from "http://en.wikipedia.org/w/index.php?title=Beta-catenin&oldid=554611214"