| Autor: |
Shu-Jing, Chang, Ying-Chi, Chen, Chi-Hsun, Yang, Soon-Cen, Huang, Ho-Kai, Huang, Chun-Chun, Li, Hans I-Chen, Harn, Wen-Tai, Chiu |
| Rok vydání: |
2016 |
| Předmět: |
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| Zdroj: |
Biochimica et biophysica acta. General subjects. 1861(3) |
| ISSN: |
0304-4165 |
| Popis: |
Focal adhesions (FAs) are large, dynamic protein complexes located close to the plasma membrane, which serve as the mechanical linkages and a biochemical signaling hub of cells. The coordinated and dynamic regulation of focal adhesion is required for cell migration. Degradation, or turnover, of FAs is a major event at the trailing edge of a migratory cell, and is mediated by CaImages obtained with a total internal reflection fluorescence microscope (TIRFM) showed that CaVinculin was resistant to degradation and was not significantly affected by the presence of mutated calpain-resistant FA molecules. In contrast, talin was more sensitive to calpain-mediated turnover than the other molecules. Three-dimensional (3D) fluorescence imaging and immunoblotting demonstrated that outer FA molecules were more sensitive to calpain-mediated proteolysis than internal FA molecules. Furthermore, cell contraction is not involved in degradation of FA.These results suggest that CaThis study will help us to clearly understand the underlying mechanism of focal adhesion turnover by Ca |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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