Catenin

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Interactions of structural proteins at cadherin-based adherens junction. The exact means by which cadherins are linked to actin filaments is still under investigation.[1]

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]

Contents

[edit] Types

Figure 1. Beta-catenin at cell-to-cell contacts of P19 embryonal carcinoma cells.

All but alpha contain armadillo repeats.

[edit] 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-κB.[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]

Several types of catenins work with N-cadherins to play an important role in learning and memory. (For full article, see Cadherin-catenin complex in learning and memory)

[edit] References

  1. ^ Weis WI, Nelson WJ (November 2006). "Re-solving the cadherin-catenin-actin conundrum". J. Biol. Chem. 281 (47): 35593–7. doi:10.1074/jbc.R600027200. PMID 17005550. http://www.jbc.org/cgi/content/full/281/47/35593. 
  2. ^ Peyriéras N, Louvard D, Jacob F (December 1985). "Characterization of antigens recognized by monoclonal and polyclonal antibodies directed against uvomorulin". Proc. Natl. Acad. Sci. U.S.A. 82 (23): 8067–71. doi:10.1073/pnas.82.23.8067. PMC 391443. PMID 2415979. http://www.pnas.org/cgi/pmidlookup?view=long&pmid=2415979. 
  3. ^ Ozawa M, Baribault H, Kemler R (June 1989). "The cytoplasmic domain of the cell adhesion molecule uvomorulin associates with three independent proteins structurally related in different species". EMBO J. 8 (6): 1711–7. PMC 401013. PMID 2788574. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=401013. 
  4. ^ a b Fukunaga Y, Liu H, Shimizu M, Komiya S, Kawasuji M, Nagafuchi A (2005). "Defining the roles of beta-catenin and plakoglobin in cell-cell adhesion: isolation of beta-catenin/plakoglobin-deficient F9 cells". Cell Struct. Funct. 30 (2): 25–34. doi:10.1247/csf.30.25. PMID 16357441. http://joi.jlc.jst.go.jp/JST.JSTAGE/csf/30.25?from=PubMed. 
  5. ^ Cattelino A, Liebner S, Gallini R, et al. (September 2003). "The conditional inactivation of the beta-catenin gene in endothelial cells causes a defective vascular pattern and increased vascular fragility". J. Cell Biol. 162 (6): 1111–22. doi:10.1083/jcb.200212157. PMC 2172846. PMID 12975353. http://www.jcb.org/cgi/pmidlookup?view=long&pmid=12975353. 
  6. ^ Bierkamp C, Schwarz H, Huber O, Kemler R (January 1999). "Desmosomal localization of beta-catenin in the skin of plakoglobin null-mutant mice". Development 126 (2): 371–81. PMID 9847250. http://dev.biologists.org/cgi/reprint/126/2/371. 
  7. ^ a b Vasioukhin V, Bauer C, Degenstein L, Wise B, Fuchs E (February 2001). "Hyperproliferation and defects in epithelial polarity upon conditional ablation of alpha-catenin in skin". Cell 104 (4): 605–17. doi:10.1016/S0092-8674(01)00246-X. PMID 11239416. http://linkinghub.elsevier.com/retrieve/pii/S0092-8674(01)00246-X. 
  8. ^ Kobielak A, Fuchs E (February 2006). "Links between alpha-catenin, NF-kappaB, and squamous cell carcinoma in skin". Proc. Natl. Acad. Sci. U.S.A. 103 (7): 2322–7. doi:10.1073/pnas.0510422103. PMC 1413714. PMID 16452166. http://www.pnas.org/cgi/pmidlookup?view=long&pmid=16452166. 

[edit] External links
Human
A1, A2, B, C1, G1, G2
I (MYO1A, MYO1B, MYO1C, MYO1D, MYO1E, MYO1F, MYO1G, MYO1H) · II (MYH1, MYH2, MYH3, MYH4, MYH6, MYH7, MYH7B, MYH8, MYH9, MYH10, MYH11, MYH13, MYH14, MYH15, MYH16) · III (MYO3A, MYO3B) · V (MYO5A, MYO5B, MYO5C) · VI (MYO6) · VII (MYO7A, MYO7B) · IX (MYO9A, MYO9B) · X (MYO10) · XV (MYO15A) · XVIII (MYO18A, MYO18B) · LC (MYL1, MYL2, MYL3, MYL4, MYL5, MYL6, MYL6B, MYL7, MYL9, MYLIP, MYLK, MYLK2, MYLL1)
Other

Tropomodulin (1, 2, 3, 4) · Troponin (T 1 2 3, C 1 2, I 1 2 3) · Tropomyosin (1, 2, 3, 4)

Actinin (1, 2, 3, 4) · Arp2/3 complex · actin depolymerizing factors (Cofilin (1, 2) · Destrin) · Gelsolin · Profilin (1, 2) · Titin
Other
Type 1/2
(Keratin,
Cytokeratin)
Epithelial keratins
(soft alpha-keratins)

type I/chromosome 17 (10, 12, 13, 14, 15, 16, 17, 19, 20) · chromosome 12 (18) · none (21)

type II/chromosome 12 (1, 2A, 3, 4, 5, 6A, 6B, 7, 8, 9)
Hair keratins
(hard alpha-keratins)
Ungrouped alpha
Not alpha
Type 3
Type 4
Type 5
Other
Catenins
Other
Nonhuman
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