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. 2018 Oct 15;37(22):e100005. doi: 10.15252/embj.2018100005

Figure 4. Contacts of SPIN90 with the long C‐terminal helix (αD) in ARPC4 are important for activation of Arp2/3 complex.

Figure 4

  1. Ribbon diagram of co‐complex structure with residues at the SPIN90‐Arp2/3 interface depicted as Cα atom spheres colored according to side chain chemistry (gray: hydrophobic, red: basic, blue: acidic). Only the ARPC4 subunit of Arp2/3 complex is shown in the zoomed in panel for clarity.
  2. Time courses of pyrene actin polymerization showing the influence of mutations on the ability of SPIN90 (269–722) to activate Arp2/3 complex. Reactions contained 3 μM 15% pyrene‐labeled actin, 50 nM Bos taurus Arp2/3 complex, and 20 μM wild‐type or mutant SPIN90 (269–722).
  3. Plot of maximum polymerization rate versus concentration of SPIN90 (269–722) for reactions as shown in panel (B).