| First Author | Ma X | Year | 2014 |
| Journal | J Biol Chem | Volume | 289 |
| Issue | 19 | Pages | 13638-50 |
| PubMed ID | 24692549 | Mgi Jnum | J:315512 |
| Mgi Id | MGI:6829128 | Doi | 10.1074/jbc.M113.511360 |
| Citation | Ma X, et al. (2014) betaArrestin1 regulates the guanine nucleotide exchange factor RasGRF2 expression and the small GTPase Rac-mediated formation of membrane protrusion and cell motility. J Biol Chem 289(19):13638-50 |
| abstractText | betaArrestin proteins shuttle between the cytosol and nucleus and have been shown to regulate G protein-coupled receptor signaling, actin remodeling, and gene expression. Here, we tested the hypothesis that betaarrestin1 regulates actin remodeling and cell migration through the small GTPase Rac. Depletion of betaarrestin1 promotes Rac activation, leading to the formation of multipolar protrusions and increased cell circularity, and overexpression of a dominant negative form of Rac reverses these morphological changes. Small interfering RNA library screen identifies RasGRF2 as a target of betaarrestin1. RasGRF2 gene and protein expression levels are elevated following depletion of betaarrestin1, and the consequent activation of Rac results in dephosphorylation of cofilin that can promote actin polymerization and formation of multipolar protrusions, thereby retarding cell migration and invasion. Together, these results suggest that betaarrestin1 regulates rasgrf2 gene expression and Rac activation to affect membrane protrusion and cell migration and invasion. |
