Biomolecular condensates concentrate macromolecules into foci without a surrounding membrane. Many condensates appear to form through multivalent interactions that drive liquid-liquid phase separation (LLPS). LLPS increases the specific activity of actin regulatory proteins toward actin assembly by the Arp2/3 complex. We show that this increase occurs because LLPS of the Nephrin–Nck–N-WASP signaling pathway on lipid bilayers increases membrane dwell time of N-WASP and Arp2/3 complex, consequently increasing actin assembly. Dwell time varies with relative stoichiometry of the signaling proteins in the phase-separated clusters, rendering N-WASP and Arp2/3 activity stoichiometry dependent. This mechanism of controlling protein activity is enabled by the stoichiometrically undefined nature of biomolecular condensates. Such regulation should be a general feature of signaling systems that assemble through multivalent interactions and drive nonequilibrium outputs.
Figure1_b-c.tar
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Figure1_d.tar
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Figure1_e.tar
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Figure2_b.tar
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Figure2_c.tar
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Figure2_e.tar
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Figure2_f.tar
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Figure3_a.tar
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Figure3_c.tar
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Figure3_d.tar
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Figure3_e.tar
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Figure3_f.tar
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Figure3_g.tar
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Figure3_h-i.tar
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Figure3_j.tar
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Figure4_a.tar
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Figure4_b-c.tar
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Figure4_e.tar
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Figure4_f.tar
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Figure4_g.tar
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Supplemental_Figures_1-4.tar
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Supplemental_Figures_5-13.tar
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