Alpha-catenin was proposed 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.[citation needed] 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] Alpha catenin exhibits significant protein dynamics.[6]
The amino acid sequence of alpha-catenin has sequence similarity to that of vinculin.[7]
Types
There are three human alpha-catenin genes:
CTNNA1, alpha-1-catenin (also called alpha-E-catenin)
CTNNA2, alpha-2-catenin (also called alpha-N-catenin)
CTNNA3, alpha-3-catenin (also called alpha-T-catenin)
^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. ISBN978-0-87893-219-1. {{cite book}}: External link in |chapterurl= (help); Unknown parameter |chapterurl= ignored (|chapter-url= suggested) (help)
^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. PMID1904011.
