Alpha-catenin functions as the primary protein link between cadherins and the actincytoskeleton.[1] It has been reported that the actin binding proteins vinculin[2] and alpha-actinin[3] can bind to alpha-catenin. 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,[5] possibly by competing with Arp2/3 protein.[6] Alpha catenin exhibits significant protein dynamics.[7]
The amino acid sequence of alpha-catenin has sequence similarity to that of vinculin.[8]
^Farago B, Nicholl ID, Wang S, Cheng X, Callaway DJ, Bu Z (March 30, 2021). "Activated nanoscale actin-binding domain motion in the catenin-cadherin complex revealed by neutron spin echo spectroscopy". Proc Natl Acad Sci USA. 118 (13): e2025012118. Bibcode:2021PNAS..11825012F. doi:10.1073/pnas.2025012118. PMC 8020631. PMID33753508.
^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. S2CID38622586.