 thumb|350px|principal interactions of structural proteins at cadherin-based adherens junction. actin filaments are linked to Î±-actinin and to membrane through vinculin. the head domain of vinculin associates to e-cadherin via Î±-, Î²-, and Î³-catenins. the tail domain of vinculin binds to membrane lipids and to actin filaments. cadherins (named for "calcium-dependent adhesion") are a class of type-1 transmembrane proteins. they play important roles in cell adhesion, forming adherens junctions to bind cells within tissues together. they are dependent on calcium (ca2+) ions to function, hence their name. the cadherin superfamily includes cadherins, protocadherins, desmogleins, and desmocollins, and more. in structure, they share cadherin repeats, which are the extracellular ca2+-binding domains. there are multiple classes of cadherin molecule, each designated with a prefix (in general, noting the type of tissue with which it is associated). it has been observed that cells containing a specific cadherin subtype tend to cluster together to the exclusion of other types, both in cell culture and during development.bello s.m., millo h., rajebhosale m., price s.r. (2012) catenin-dependent cadherin function drives divisional segregation of spinal chord motor neurons. j. neuroscience 32(2):490-505 for example, cells containing n-cadherin tend to cluster with other n-cadherin-expressing cells. however, it has been noted that the mixing speed in the cell culture experiments can have an effect on the extent of homotypic specificity. in addition, several groups have observed heterotypic binding affinity (i.e., binding of different types of cadherin together) in various assays.{{cite journal | last1 = niessen | first1 = carien m. | last2 = gumbiner | first2 = barry m. | year = 2002 | title = cadherin-mediated cell sorting not determined by binding or adhesion specificity | journal = the journal of cell biology | volume = 156 | issue = 2 | doi = 10.1083/jcb.200108040 | pmid =
Cell_adhesion_proteins Transmembrane_proteins