| First Author | Thompson ME | Year | 2013 |
| Journal | Nat Struct Mol Biol | Volume | 20 |
| Issue | 1 | Pages | 111-8 |
| PubMed ID | 23222643 | Mgi Jnum | J:245328 |
| Mgi Id | MGI:5917797 | Doi | 10.1038/nsmb.2462 |
| Citation | Thompson ME, et al. (2013) FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation. Nat Struct Mol Biol 20(1):111-8 |
| abstractText | Formins are actin-assembly factors that act in a variety of actin-based processes. The conserved formin homology 2 (FH2) domain promotes filament nucleation and influences elongation through interaction with the barbed end. FMNL3 is a formin that induces assembly of filopodia but whose FH2 domain is a poor nucleator. The 3.4-A structure of a mouse FMNL3 FH2 dimer in complex with tetramethylrhodamine-actin uncovers details of formin-regulated actin elongation. We observe distinct FH2 actin-binding regions; interactions in the knob and coiled-coil subdomains are necessary for actin binding, whereas those in the lasso-post interface are important for the stepping mechanism. Biochemical and cellular experiments test the importance of individual residues for function. This structure provides details for FH2-mediated filament elongation by processive capping and supports a model in which C-terminal non-FH2 residues of FMNL3 are required to stabilize the filament nucleus. |
