Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation.
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.
Mesh Terms:
Amino Acid Sequence, Animals, Base Sequence, CHO Cells, Caenorhabditis elegans Proteins, Cell Adhesion Molecules, Contractile Proteins, Cricetinae, Cytoskeletal Proteins, Cytoskeleton, DNA, Complementary, Eukaryotic Cells, Extracellular Matrix, Focal Adhesions, Humans, Mice, Microfilament Proteins, Microfilaments, Molecular Sequence Data, Rats, Tumor Cells, Cultured, rac GTP-Binding Proteins
Amino Acid Sequence, Animals, Base Sequence, CHO Cells, Caenorhabditis elegans Proteins, Cell Adhesion Molecules, Contractile Proteins, Cricetinae, Cytoskeletal Proteins, Cytoskeleton, DNA, Complementary, Eukaryotic Cells, Extracellular Matrix, Focal Adhesions, Humans, Mice, Microfilament Proteins, Microfilaments, Molecular Sequence Data, Rats, Tumor Cells, Cultured, rac GTP-Binding Proteins
Cell
Date: Apr. 04, 2003
PubMed ID: 12679033
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