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• W2952628315 abstract "RPEL proteins, which contain the G-actin-binding RPEL motif, coordinate cytoskeletal processes with actin dynamics. We show that the ArhGAP12- and ArhGAP32-family GTPase-activating proteins (GAPs) are RPEL proteins. We determine the structure of the ArhGAP12/G-actin complex, and show that G-actin contacts the RPEL motif and GAP domain sequences. G-actin inhibits ArhGAP12 GAP activity, and this requires the G-actin contacts identified in the structure. In B16 melanoma cells, ArhGAP12 suppresses basal Rac and Cdc42 activity, F-actin assembly, invadopodia formation and experimental metastasis. In this setting, ArhGAP12 mutants defective for G-actin binding exhibit more effective downregulation of Rac GTP loading following HGF stimulation and enhanced inhibition of Rac-dependent processes, including invadopodia formation. Potentiation or disruption of the G-actin/ArhGAP12 interaction, by treatment with the actin-binding drugs latrunculin B or cytochalasin D, has corresponding effects on Rac GTP loading. The interaction of G-actin with RPEL-family rhoGAPs thus provides a negative feedback loop that couples Rac activity to actin dynamics. Diring et al. identify ArhGAP12 and ArhGAP32 as RPEL proteins that bind G-actin. When bound to G-actin, ArhGAP12 cannot suppress Rac, thus coupling Rac activity to actin availability." @default.
• W2952628315 created "2019-06-27" @default.
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• W2952628315 date "2019-06-17" @default.
• W2952628315 modified "2023-10-18" @default.
• W2952628315 title "RPEL-family rhoGAPs link Rac/Cdc42 GTP loading to G-actin availability" @default.
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• W2952628315 doi "https://doi.org/10.1038/s41556-019-0337-y" @default.
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