Rap1 Spatially Controls ArhGAP29 To Inhibit Rho Signaling during Endothelial Barrier Regulation
| Autor: | Bas Ponsioen, Willem-Jan Pannekoek, Marjolein J. Vliem, Anneke Post, Johannes L. Bos |
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| Rok vydání: | 2015 |
| Předmět: |
rho GTP-Binding Proteins
endocrine system GTPase-activating protein GTPase Biology Human Umbilical Vein Endothelial Cells Guanine Nucleotide Exchange Factors Humans Small GTPase Molecular Biology Cells Cultured Microscopy Confocal GTPase-Activating Proteins Intracellular Signaling Peptides and Proteins rap1 GTP-Binding Proteins Articles Cell Biology Actin cytoskeleton Cell biology Luminescent Proteins Protein Transport enzymes and coenzymes (carbohydrates) HEK293 Cells Intercellular Junctions RNA Interference Rap1 MDia1 Guanine nucleotide exchange factor Signal transduction Carrier Proteins Protein Binding Signal Transduction |
| Zdroj: | Molecular and Cellular Biology, 35(14), 2495. American Society for Microbiology |
| ISSN: | 1098-5549 0270-7306 |
| Popis: | The small GTPase Rap1 controls the actin cytoskeleton by regulating Rho GTPase signaling. We recently established that the Rap1 effectors Radil and Rasip1, together with the Rho GTPase activating protein ArhGAP29, mediate Rap1-induced inhibition of Rho signaling in the processes of epithelial cell spreading and endothelial barrier function. Here, we show that Rap1 induces the independent translocations of Rasip1 and a Radil-ArhGAP29 complex to the plasma membrane. This results in the formation of a multimeric protein complex required for Rap1-induced inhibition of Rho signaling and increased endothelial barrier function. Together with the previously reported spatiotemporal control of the Rap guanine nucleotide exchange factor Epac1, these findings elucidate a signaling pathway for spatiotemporal control of Rho signaling that operates by successive protein translocations to and complex formation at the plasma membrane. |
| Databáze: | OpenAIRE |
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