DOI: 10.5061/dryad.hh37793
title: Data from: Stoichiometry controls activity of phase-separated clusters of actin signaling proteins

description: 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.
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