Focal Adhesion Kinase Stabilizes the Cytoskeleton

被引：81

作者：

Fabry, Ben ^{[1
]}

Klemm, Anna H. ^{[1
]}

Kienle, Sandra ^{[1
]}

Schaeffer, Tilman E. ^{[1
]}

Goldmann, Wolfgang H. ^{[1
]}

机构：

[1] Univ Erlangen Nurnberg, Dept Phys, Erlangen, Germany

来源：

BIOPHYSICAL JOURNAL | 2011年 / 101卷 / 09期

基金：

美国国家卫生研究院;

关键词：

RHO-ASSOCIATED KINASE; CELL LOCOMOTION; SMOOTH-MUSCLE; F9; CELLS; FAK; VINCULIN; ACTIN; PHOSPHORYLATION; TRANSDUCTION; ORGANIZATION;

D O I：

10.1016/j.bpj.2011.09.043

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

Focal adhesion kinase (FAK) is a central focal adhesion protein that promotes focal adhesion turnover, but the role of FAK for cell mechanical stability is unknown. We measured the mechanical properties of wild-type (FAKwt), FAK-deficient (FAK-/-), FAK-silenced (siFAK), and siControl mouse embryonic fibroblasts by magnetic tweezer, atomic force microscopy, traction microscopy, and nanoscale particle tracking microrheology. FAK-deficient cells showed lower cell stiffness, reduced adhesion strength, and increased cytoskeletal dynamics compared to wild-type cells. These observations imply a reduced stability of the cytoskeleton in FAK-deficient cells. We attribute the reduced cytoskeletal stability to rho-kinase activation in FAK-deficient cells that suppresses the formation of ordered stress fiber bundles, enhances cortical actin distribution, and reduces cell spreading. In agreement with this interpretation is that cell stiffness and cytoskeletal stability in FAK-/- cells is partially restored to wild-type level after rho-kinase inhibition with Y27632.

引用

页码：2131 / 2138

页数：8

共 53 条

[1] Identification of a putative target for Rho as the serine-threonine kinase protein kinase N [J].