Actin cable distribution and dynamics arising from cross-linking, motor pulling, and filament turnover

Supplemental Materials

This article contains the following supporting material:

  • Supplemental Materials
  • Movie01 - Video 1. Myosin V density ρmyo (#/μm) affects actin cable structure (see Figure 3 and Figure S3). In simulations that lack of myosin pulling force, the cables are not able to span the entire cell, creating thick and curved cables. Increasing ρmyo stretches the cables, enabling them to connect with cables from the opposite end. At ρmyo = 10/μm, the pulling is strong and cables become straight and less bundled.
  • Movie02 - Video 2. Increasing γcrslnk bundles actin filaments (see Figure 4 and Figure S4). At γcrslnk = 0.07 μm, 15% of the total actin filaments are bundled, compared to 59% and 68% at γcrslnk = 0.08 μm and γcrslnk = 0.09 μm.
  • Movie03 - Video3. Increasing kcrslnk bundles actin filaments in a parallel fashion (see Figure 4 and Figure S4). At kcrslnk = 0.5 pN/μm, 9% of the total actin filaments are bundled, compared to 69% and 74% at kcrslnk = 2 pN/μm and kcrslnk = 5 pN/μm. Anti-parallel cables at kcrslnk = 5 pN/μm undergo buckling, bulging and breaking.
  • Movie04 - Video 4. Bundling mechanisms under different (γcrslnk, kcrslnk) parameter sets (corresponds to Figure 4D, Figure 5 and Figure S5). Simulation (γcrslnk, kcrslnk) at (0.07, 5), (0.1, 1), (0.1, 5) show features discussed as weak parallel bundling, strong anti-parallel bundling and strong parallel bundling. Units of (γcrslnk, kcrslnk): (μm, pN/μm).