Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 20, Issue 1, Pages 111-U143Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2462
Keywords
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Funding
- US National Institutes of Health [R01 GM069818, F31 GM089149]
- Howard Hughes Medical Institute [52006921]
- National Science Foundation [0947790]
- US federal funds from the National Cancer Institute [Y1-CO-1020]
- National Institute of General Medical Sciences [Y1-GM-1104]
- US Department of Energy, Basic Energy Sciences, Office of Science [DE-AC02-06CH11357]
- Direct For Education and Human Resources
- Division Of Graduate Education [0947790] Funding Source: National Science Foundation
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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-angstrom 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.
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