Alpha catenin
| catenin (cadherin-associated protein), alpha 1, 102kDa | |
|---|---|
|
| |
| Identifiers | |
| Symbol | CTNNA1 |
| Entrez | 1495 |
| HUGO | 2509 |
| OMIM | 116805 |
| RefSeq | NM_001903 |
| UniProt | P35221 |
| Other data | |
| Locus | Chr. 5 q31.2 |
| catenin (cadherin-associated protein), alpha 2 | |
|---|---|
| Identifiers | |
| Symbol | CTNNA2 |
| Entrez | 1496 |
| HUGO | 2510 |
| OMIM | 114025 |
| RefSeq | NM_004389 |
| UniProt | P26232 |
| Other data | |
| Locus | Chr. 2 p12-p11.1 |
| catenin (cadherin-associated protein), alpha 3 | |
|---|---|
| Identifiers | |
| Symbol | CTNNA3 |
| Entrez | 29119 |
| HUGO | 2511 |
| OMIM | 607667 |
| RefSeq | NM_013266 |
| UniProt | Q9UI47 |
| Other data | |
| Locus | Chr. 10 q21 |
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
- alpha Catenin at the US National Library of Medicine Medical Subject Headings (MeSH)
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.