Migfilin is a LIM-domain protein recruited to junctions that link cells with the extracellular matrix. It has multiple binding partners and appears to function as a scaffold that connects matrix-bound integrin-Mig-2 complexes with the actin-associated protein filamin. In a Research Article on , Chanyue Wu and co-workers reveal that migfilin also resides at cell-cell junctions. They find that it colocalizes with cadherin adhesion molecules and β-catenin at these sites. Moreover, they demonstrate it has a role there, since RNAi directed against migfilin disrupts the organization of these junctions and weakens endothelial cell-cell association. In a Commentary on , Wu goes on to discuss the broader roles of migfilin in cells. The protein represents a critical link between adhesion sites and the actin cytoskeleton. Consequently, it controls actin remodelling, cell morphology and motility. Furthermore, it can also translocate to the nucleus, where it interacts with transcription factors such as CSX/NKX2-5 to regulate gene expression and cell differentiation. Mutations in several migfilin binding partners are associated with severe human diseases (e.g. periventricular heterotopia and Kindler syndrome), underlining the importance of this protein for normal physiology.
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