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

被引：317

作者：

Tu, YZ ^{[1
]}

Wu, S ^{[1
]}

Shi, XH ^{[1
]}

Chen, K ^{[1
]}

Wu, CY ^{[1
]}

机构：

[1] Univ Pittsburgh, Dept Pathol, Pittsburgh, PA 15261 USA

来源：

CELL | 2003年 / 113卷 / 01期

关键词：

D O I：

10.1016/S0092-8674(03)00163-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：37 / 47

页数：11

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[1] The Rac1-and RhoG-specific GEF domain of Trio targets filamin to remodel cytoskeletal actin [J].