Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation

Cell. 2003 Apr 4;113(1):37-47. doi: 10.1016/s0092-8674(03)00163-6.

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Actin Cytoskeleton / metabolism*
  • Amino Acid Sequence / genetics
  • Animals
  • Base Sequence / genetics
  • CHO Cells
  • Caenorhabditis elegans Proteins / genetics
  • Caenorhabditis elegans Proteins / metabolism*
  • Cell Adhesion Molecules / genetics
  • Cell Adhesion Molecules / isolation & purification*
  • Contractile Proteins / metabolism*
  • Cricetinae
  • Cytoskeletal Proteins
  • Cytoskeleton / metabolism
  • DNA, Complementary / analysis
  • DNA, Complementary / genetics
  • Eukaryotic Cells / metabolism*
  • Extracellular Matrix / metabolism*
  • Filamins
  • Focal Adhesions / genetics
  • Focal Adhesions / metabolism*
  • Humans
  • Mice
  • Microfilament Proteins / metabolism*
  • Molecular Sequence Data
  • Rats
  • Tumor Cells, Cultured
  • rac GTP-Binding Proteins / genetics
  • rac GTP-Binding Proteins / metabolism*

Substances

  • Caenorhabditis elegans Proteins
  • Cell Adhesion Molecules
  • Contractile Proteins
  • Cytoskeletal Proteins
  • DNA, Complementary
  • FBLIM1 protein, human
  • Filamins
  • Microfilament Proteins
  • Mig-2 protein, C elegans
  • rac GTP-Binding Proteins

Associated data

  • GENBANK/AY180161