Computational modeling highlights disordered Formin Homology 1 domains role in profilin-actin transfer Institutional Repository Document uri icon


  • Formins accelerate actin polymerization, assumed to occur through flexible FH1 domain mediated transfer of profilin-actin to the barbed end. To study FH1 properties and address sequence effects including varying length/distribution of profilin-binding proline-rich motifs, we performed all-atom simulations of mouse mDia1, mDia2; budding yeast Bni1, Bnr1; fission yeast Cdc12, For3, and Fus1 FH1s. We find FH1 has flexible regions between high propensity polyproline helix regions. A coarse-grained model retaining sequence-specificity, assuming rigid polyproline segments, describes their size. Multiple profilins and profilin-actin complexes can simultaneously bind, expanding mDia1-FH1, which may be important in cells. Simulations of the barbed end bound to Bni1-FH1-FH2 dimer show the leading FH1 can better transfer profilin or profilin-actin, having decreasing probability with increasing distance from FH2.

altmetric score

  • 6.95

author list (cited authors)

  • Horan, B. G., Zerze, G. H., Kim, Y. C., Vavylonis, D., & Mittal, J.

citation count

  • 0

complete list of authors

  • Horan, Brandon G||Zerze, Gül H||Kim, Young C||Vavylonis, Dimitrios||Mittal, Jeetain

Book Title

  • bioRxiv

publication date

  • February 2018