Table 2.
Properties of the C-terminal elements of different formins
Mm is M. musculus and Dm is D. melanogaster.
| Formin | Main actin interacting modulea | G-actin binding affinity | Nucleation activity in isolated form/contribution to FH2-mediated nucleation | Affecting G-actin interaction | Other effects in actin dynamics |
|---|---|---|---|---|---|
| Mm INF2 (12>) | WH2-like/DAD sequence | KD ∼0.06 μm | No/yes | Profilin interferes | Monomer sequestration, filament severing |
| 50 mm KCl | |||||
| Mm FMNL3 (14) | WH2-DAD-CT | KD ∼2–3 μm | Yes/yes | INF2 C terminus interferes | Inhibits elongation (∼ nm) |
| 50 mm KCl | mDia1 C terminus does not interfere | ||||
| Mm Dia1 (13) | DAD-CT | KD ∼100 μm | Yes/yes | Profilin does not interfere | Accelerates elongation (∼ μm) |
| 200 mm NaCl | |||||
| Dm Capu (15) | tail | KD ∼20 μm | No/yes | WH2, RPEL1 interfere | Inhibits elongation (>10 μm) |
| 50 mm NaCl | Profilin does not significantly interfere | ||||
| Dm DAAM (this study) | DAD-CT | KD = 44.4 ± 2.85 μm | No/yes | Profilin does not interfere | Inhibits elongation (>40–50 μm) |
| 50 mm NaCl | WH2 interferes |
a The main actin interacting elements of the C-terminal regions are highlighted in boldface.