The influence of Pyk2 on the mechanical properties in fibroblasts

被引：15
作者：
Klemm, Anna H. [1 ]
Kienle, Sandra [1 ]
Rheinlaender, Johannes [2 ]
Schaeffer, Tilman E. [2 ]
Goldmann, Wolfgang H. [1 ]
机构：
[1] Univ Erlangen Nurnberg, Ctr Med Phys & Technol, Biophys Grp, D-91052 Erlangen, Germany
[2] Univ Erlangen Nurnberg, Inst Appl Phys, D-91052 Erlangen, Germany
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2010年 / 393卷 / 04期
关键词：
Actin cytoskeleton; FAK; Pyk2; Focal adhesions; Western blotting; Magnetic tweezer; Immunofluorescence; Atomic force microscopy; FOCAL ADHESION KINASE; CELL-SHAPE; PROTEIN; FAK; AUTOPHOSPHORYLATION; ACTIVATION; VINCULIN; MATRIX; ACTIN;
D O I：
10.1016/j.bbrc.2010.02.059
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：
The cell surface receptor integrin is involved in signaling mechanical stresses via the focal adhesion complex (FAC) into the cell. Within FAC, the focal adhesion kinase (FAK) and Pyk2 are believed to act as important scaffolding proteins. Based on the knowledge that many signal transducing molecules are transiently immobilized within FAC connecting the cytoskeleton with integrins, we applied magnetic tweezer and atomic force microscopic measurements to determine the influence of FAK and Pyk2 in cells mechanically. Using mouse embryonic fibroblasts (MEF; FAK(+/+), FAK(-/-), and siRNA-Pyk2 treated FAK(-/-) cells) provided a unique opportunity to describe the function of FAK and Pyk2 in more detail and to define their influence on FAC and actin distribution. Published by Elsevier Inc.
引用
收藏
页码：694 / 697
页数：4
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