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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Substitution
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Animals
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Arginine / genetics
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Arginine / metabolism
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CHO Cells
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Cell Membrane / genetics
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Cell Membrane / metabolism
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Cell Movement / physiology*
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Cell Proliferation
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Cricetinae
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Cricetulus
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Cytoplasm / genetics
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Cytoplasm / metabolism
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GTPase-Activating Proteins / genetics
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GTPase-Activating Proteins / metabolism*
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HEK293 Cells
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HeLa Cells
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Humans
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Methylation
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Mutation, Missense
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Protein Methyltransferases / genetics
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Protein Methyltransferases / metabolism
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Protein Multimerization / physiology*
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Protein-Arginine N-Methyltransferases
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cdc42 GTP-Binding Protein / genetics
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cdc42 GTP-Binding Protein / metabolism
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rac1 GTP-Binding Protein / genetics
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rac1 GTP-Binding Protein / metabolism
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rhoA GTP-Binding Protein / genetics
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rhoA GTP-Binding Protein / metabolism
Substances
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GTPase-Activating Proteins
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RAC1 protein, human
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SRGAP2 protein, human
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RHOA protein, human
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Arginine
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Protein Methyltransferases
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PRMT5 protein, human
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Protein-Arginine N-Methyltransferases
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cdc42 GTP-Binding Protein
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rac1 GTP-Binding Protein
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rhoA GTP-Binding Protein