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Xinxin Wang1, Brian J Galletta2, John A Cooper3

  • 1Department of Physics, Washington University, St. Louis, Missouri.

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Cellular endocytosis relies on pulsed actin assembly, regulated by protein interactions. This study models yeast endocytosis, revealing how actin regulators control polymerization dynamics and response to mutations and drugs.

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Area of Science:

  • Cell Biology
  • Biophysics
  • Computational Biology

Background:

  • Clathrin-mediated endocytosis is crucial for cell signaling and receptor regulation.
  • Actin polymerization dynamics are essential for endocytosis, particularly in yeast.
  • The Arp2/3 complex and its regulators play a key role in actin nucleation and branching during endocytosis.

Purpose of the Study:

  • To identify protein-protein interactions driving pulsed actin assembly during yeast endocytosis.
  • To investigate the impact of mutations and drug treatments on actin and regulator dynamics.
  • To model the complex interplay between actin, its regulators, and the Arp2/3 complex.

Main Methods:

  • Development of a stochastic 3D actin network model and a Fitzhugh-Nagumo type model.
  • Incorporation of negative feedback from F-actin onto Arp2/3 regulators in both models.
  • Experimental validation using quantitative fluorescence microscopy in Saccharomyces cerevisiae.

Main Results:

  • Models successfully explain pulsed actin polymerization and responses to interventions.
  • Observed a surprising increase in F-actin with reduced regulator branching activity.
  • Confirmed prediction that decreased branching activity increases regulator accumulation.

Conclusions:

  • Pulsed actin dynamics in endocytosis are governed by specific protein-protein interactions and feedback mechanisms.
  • Actin regulators exhibit quasi-independent accumulation, primarily affected by their own mutations.
  • The study provides insights into the regulation of actin dynamics crucial for cellular processes like endocytosis.