Rap1 controls cell adhesion and cell motility through the regulation of myosin II
| Autor: | Richard A. Firtel, Taeck J. Jeon, Gerald Weeks, Dai-Jen Lee, Sylvain Merlot |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2007 |
| Předmět: |
endocrine system
Myosin light-chain kinase Cell Surface Extension macromolecular substances Biology Dictyostelium discoideum Article 03 medical and health sciences Cell Movement Myosin Cell Adhesion Animals Dictyostelium Phosphorylation Cell adhesion Research Articles 030304 developmental biology Myosin Type II 0303 health sciences 030302 biochemistry & molecular biology Phosphotransferases Membrane Proteins rap1 GTP-Binding Proteins Chemotaxis Cell Biology biology.organism_classification Actin cytoskeleton Cell biology enzymes and coenzymes (carbohydrates) Actin Cytoskeleton Rap1 Cell Surface Extensions |
| Zdroj: | The Journal of Cell Biology |
| ISSN: | 1540-8140 0021-9525 |
| Popis: | We have investigated the role of Rap1 in controlling chemotaxis and cell adhesion in Dictyostelium discoideum. Rap1 is activated rapidly in response to chemoattractant stimulation, and activated Rap1 is preferentially found at the leading edge of chemotaxing cells. Cells expressing constitutively active Rap1 are highly adhesive and exhibit strong chemotaxis defects, which are partially caused by an inability to spatially and temporally regulate myosin assembly and disassembly. We demonstrate that the kinase Phg2, a putative Rap1 effector, colocalizes with Rap1–guanosine triphosphate at the leading edge and is required in an in vitro assay for myosin II phosphorylation, which disassembles myosin II and facilitates filamentous actin–mediated leading edge protrusion. We suggest that Rap1/Phg2 plays a role in controlling leading edge myosin II disassembly while passively allowing myosin II assembly along the lateral sides and posterior of the cell. |
| Databáze: | OpenAIRE |
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