Fig. 3. Control of the subcellular localization of migfilin. The figure shows a model for the mechanism that controls migfilin localization to cell-ECM adhesions, cell-cell junctions, actin filaments and nuclei. Migfilin is recruited to cell-ECM adhesions through its interaction with Mig-2, a component of cell-ECM adhesions. In epithelial and endothelial cells, migfilin is also recruited to adherens junctions in response to cadherin-mediated cell-cell adhesion through an interaction with a yet-to-be-identified protein, which is probably a component of the cadherin–ß-catenin complex. Migfilin associates with actin filaments through its interaction with filamin, although the associations of migfilin with cell-ECM and cell-cell adhesions appear to dominate. FBLP-1, a migfilin splicing variant lacking LIM3 and therefore the ability to localize to cell-ECM or cell-cell adhesions, predominantly associates with the actin filaments. Travel of migfilin to the nucleus is regulated both by intracellular Ca²⁺ signaling and a nuclear export signal located within the proline-rich domain that is subjected to alternative splicing.