| Autor: |
Dagliyan, O., Karginov, A. V., Elston, T. C., Chu, P.-H., Tsygankov, D., Gomez, S. M., Hahn, K. M., Berginski, M. E. |
| Jazyk: |
angličtina |
| Rok vydání: |
2014 |
| DOI: |
10.17615/zvc6-gk15 |
| Popis: |
Src family kinases (SFKs), critical in many aspects of homeostasis and disease, occur as multiple isoforms. It has been difficult to dissect the unique function of each isoform because their structures are so similar. Here we specifically activated each SFK isoform through insertion of an engineered domain. The domain caused the kinases to be catalytically inactive until they were reactivated by the small molecule rapamycin. Computational methods for quantifying dynamic changes in cell shape revealed that activation of each isoform produced dramatically different cell behaviors. Quantitative analysis showed that these behaviors correlated with specific patterns of subcellular trafficking, and depended on isoform acylation. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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