The influence of Pyk2 on the mechanical properties in fibroblasts

作者：Klemm Anna H; Kienle Sandra; Rheinlaender Johannes; Schaeffer Tilman E; Goldmann Wolfgang H^*

来源：Biochemical and Biophysical Research Communications, 2010, 393(4): 694-697.

DOI：10.1016/j.bbrc.2010.02.059

• Actin cytoskeleton
• FAK
• Pyk2
• Focal adhesions
• Western blotting
• Magnetic tweezer
• Immunofluorescence
• Atomic force microscopy

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.

• 出版日期2010-3-19