srGAP2 Arginine Methylation Regulates Cell Migration and Cell Spreading through Promoting Dimerization |
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| Authors: | Shaoshi Guo Shilai Bao |
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| Institution: | From the ‡Key Laboratory of Molecular and Developmental Biology, Center for Molecular and Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China and ;the §Graduate University of the Chinese Academy of Sciences, Beijing 100039, China |
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| Abstract: | The Slit-Robo GTPase-activating proteins (srGAPs) are critical for neuronal migration through inactivation of Rho GTPases Cdc42, Rac1, and RhoA. Here we report that srGAP2 physically interacts with protein arginine methyltransferase 5 (PRMT5). srGAP2 localizes to the cytoplasm and plasma membrane protrusion. srGAP2 knockdown reduces cell adhesion spreading and increases cell migration, but has no effect on cell proliferation. PRMT5 binds to the N terminus of srGAP2 (225–538 aa) and methylates its C-terminal arginine residue Arg-927. The methylation mutant srGAP2-R927A fails to rescue the cell spreading rate, is unable to localize to the plasma membrane leading edge, and perturbs srGAP2 homodimer formation mediated by the F-BAR domain. These results suggest that srGAP2 arginine methylation plays important roles in cell spreading and cell migration through influencing membrane protrusion. |
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| Keywords: | Cell Migration Plasma Membrane Protein Domains Protein Methylation Protein-Protein Interactions Rho F-BAR Domain PRMT5 Cell Spreading srGAP2 |
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