Stoichiometry controls activity of phase-separated clusters of actin signaling proteins
Marine Biological Laboratory · Howard Hughes Medical Institute · +2 more institutions
Abstract
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…
Citation impact
- FWCI
- 24.35
- Percentile
- 100%
- References
- 27
Authors
4- LBLindsay B. Case
Marine Biological Laboratory, Howard Hughes Medical Institute, Southwestern Medical Center, The University of Texas Southwestern Medical Center
- XZXu Zhang
Howard Hughes Medical Institute, Southwestern Medical Center, The University of Texas Southwestern Medical Center
- JAJonathon A. Ditlev
Marine Biological Laboratory, Howard Hughes Medical Institute, Southwestern Medical Center, The University of Texas Southwestern Medical Center
- MKMichael K. RosenCorresponding
Marine Biological Laboratory, Howard Hughes Medical Institute, Southwestern Medical Center, The University of Texas Southwestern Medical Center
Topics & keywords
- Actin
- Biophysics
- Stoichiometry
- Macromolecule
- Cell biology
- Membrane
- Cytoskeleton
- Chemistry