PMID: 23105102 RLIMS-P 2 Check other iTextMine results Issue Report
Title
| 1. | Dynamic phosphorylation of tyrosine 665 in pseudopodium-enriched atypical kinase 1 (PEAK1) is essential for the regulation of cell migration and focal adhesion turnover. |
Abstract
| 2. | Pseudopodium-enriched atypical kinase 1 (PEAK1) is a recently described tyrosine kinase that associates with the actin cytoskeleton and focal adhesion (FA) in migrating cells. |
| 3. | PEAK1 is known to promote cell migration, but the responsible mechanisms remain unclear. |
| 4. | Here, we show that PEAK1 controls FA assembly and disassembly in a dynamic pathway controlled by PEAK1 phosphorylation at Tyr-665. |
| 5. | Knockdown of endogenous PEAK1 inhibits random cell migration. |
| 6. | In PEAK1-deficient cells, FA lifetimes are decreased, FA assembly times are shortened, and FA disassembly times are extended. |
| 7. | Phosphorylation of Tyr-665 in PEAK1 is essential for normal PEAK1 localization and its function in the regulation of FAs; however, constitutive phosphorylation of PEAK1 Tyr-665 is also disruptive of its function, indicating a requirement for precise spatiotemporal regulation of PEAK1. |
| 8. | Src family kinases are required for normal PEAK1 localization and function. |
| 9. | Finally, we provide evidence that PEAK1 promotes cancer cell invasion through Matrigel by a mechanism that requires dynamic regulation of Tyr-665 phosphorylation. |
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