Alpha catenin
Alpha-catenin was suggested to function as a linking protein between cadherins and actin-containing filaments of the cytoskeleton.[1] It has been reported that the actin binding proteins vinculin[2] and alpha-actinin[3] can bind to alpha-catenin. However, a protein complex including a cadherin, actin, beta-catenin and alpha-catenin has not been isolated. It has been suggested that alpha-catenin does not bind with high affinity to both actin filaments and the E-cadherin-beta-catenin complex at the same time.[4] It has been observed that when alpha-catenin is not in a molecular complex with beta-catenin, it dimerizes and functions to regulate actin filament assembly, possibly by competing with Arp2/3 protein.[5]
The amino acid sequence of alpha-catenin has sequence similarity to that of vinculin.[6]
Types
There are three human alpha-catenin genes:
- alpha-1-catenin (also called alpha-E-catenin)
- alpha-2-catenin (also called alpha-N-catenin)
- alpha-3-catenin (also called alpha-T-catenin)
See also
External links
References
- ↑ Cooper, Geoffrey M. (2000). "Figure 11.14: Model of attachment of actin filaments to catenin-cadherin complexes". The Cell: A Molecular Approach (2nd ed.). Sinauer Associates. ISBN 0-87893-219-4.
- ↑ Watabe-Uchida M, Uchida N, Imamura Y; et al. (August 1998). "alpha-Catenin-vinculin interaction functions to organize the apical junctional complex in epithelial cells". J. Cell Biol. 142 (3): 847–57. doi:10.1083/jcb.142.3.847. PMC 2148175. PMID 9700171.
- ↑ Knudsen KA, Soler AP, Johnson KR, Wheelock MJ (July 1995). "Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin". J. Cell Biol. 130 (1): 67–77. doi:10.1083/jcb.130.1.67. PMC 2120515. PMID 7790378.
- ↑ Yamada S, Pokutta S, Drees F, Weis WI, Nelson WJ (December 2005). "Deconstructing the cadherin-catenin-actin complex". Cell 123 (5): 889–901. doi:10.1016/j.cell.2005.09.020. PMC 3368712. PMID 16325582.
- ↑ Drees F, Pokutta S, Yamada S, Nelson WJ, Weis WI (December 2005). "Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly". Cell 123 (5): 903–15. doi:10.1016/j.cell.2005.09.021. PMC 3369825. PMID 16325583.
- ↑ Nagafuchi A, Takeichi M, Tsukita S (May 1991). "The 102 kd cadherin-associated protein: similarity to vinculin and posttranscriptional regulation of expression". Cell 65 (5): 849–57. doi:10.1016/0092-8674(91)90392-C. PMID 1904011.
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| See also: cytoskeletal defects |
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