10.5061/DRYAD.HH37793
Case, Lindsay B.
Marine Biological Laboratory
Zhang, Xu
Howard Hughes Medical Institute
Ditlev, Jonathon A.
Marine Biological Laboratory
Rosen, Michael K.
Marine Biological Laboratory
Data from: Stoichiometry controls activity of phase-separated clusters of
actin signaling proteins
Dryad
dataset
2019
2019-03-08T12:13:21Z
2019-03-08T12:13:21Z
en
https://doi.org/10.1126/science.aau6313
74866902570 bytes
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CC0 1.0 Universal (CC0 1.0) Public Domain Dedication
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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