Structural highlights
Function
[ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Publication Abstract from PubMed
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.
FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation.,Thompson ME, Heimsath EG, Gauvin TJ, Higgs HN, Kull FJ Nat Struct Mol Biol. 2012 Dec 9. doi: 10.1038/nsmb.2462. PMID:23222643[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Thompson ME, Heimsath EG, Gauvin TJ, Higgs HN, Kull FJ. FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation. Nat Struct Mol Biol. 2012 Dec 9. doi: 10.1038/nsmb.2462. PMID:23222643 doi:http://dx.doi.org/10.1038/nsmb.2462
