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- Title
FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation.
- Authors
Thompson, Morgan E; Heimsath, Ernest G; Gauvin, Timothy J; Higgs, Henry N; Kull, F Jon
- Abstract
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-Å 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.
- Subjects
ACTIN; FORMINS; HOMOLOGY (Biology); NUCLEATION; ELONGATION factors (Biochemistry); CELL nuclei
- Publication
Nature Structural & Molecular Biology, 2013, Vol 20, Issue 1, p111
- ISSN
1545-9993
- Publication type
Article
- DOI
10.1038/nsmb.2462