Caldesmon, filamin 1, nebulin, villin, plastin, ADF, gelsolin, Dematin, and cofilin are differentially expressed actin binding proteins. Dematin is a bundling protein of the erythrocyte membrane skeleton. Dematin is localized to the spectrin-actin junctions, and its actin-bundling activity is abolished upon phosphorylation by cAMP-dependent protein kinase. It may also play a role in the regulation of cell shape, implying a role in tumorigenesis. Dematin is a trimeric protein containing two subunits of 48 kDa and one subunit of 52 kDa.