Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation |
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Authors: | Tu Yizeng Wu Shan Shi Xiaohua Chen Ka Wu Chuanyue |
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Institution: | Department of Pathology, University of Pittsburgh, Pittsburgh, PA 15261, USA. |
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Abstract: | Cell-extracellular matrix adhesion is an important determinant of cell morphology. We show here that migfilin, a LIM-containing protein, localizes to cell-matrix adhesions, associates with actin filaments, and is essential for cell shape modulation. Migfilin interacts with the cell-matrix adhesion protein Mig-2 (mitogen inducible gene-2), a mammalian homolog of UNC-112, and the actin binding protein filamin through its C- and N-terminal domains, respectively. Loss of Mig-2 or migfilin impairs cell shape modulation. Mig-2 recruits migfilin to cell-matrix adhesions, while the interaction with filamin mediates the association of migfilin with actin filaments. Migfilin therefore functions as an important scaffold at cell-matrix adhesions. Together, Mig-2, migfilin and filamin define a connection between cell matrix adhesions and the actin cytoskeleton and participate in the orchestration of actin assembly and cell shape modulation. |
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