Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis.
By Stéphane Romero, Christophe Le Clainche, D. Didry, C. Egile, D. Pantaloni, M. Carlier. Cell, 2004
597 citations recorded by the source corpus.
Motile and morphogenetic cellular processes are driven by site-directed assembly of actin filaments. Formins, proteins characterized by formin homology domains FH1 and FH2, are initiators of actin assembly. How formins simply bind to filament barbed ends in rapid equilibrium or find free energy to become a processive motor of filament assembly remains enigmatic. Here we demonstrate that the FH1-FH2 domain accelerates hydrolysis of ATP coupled to profilin-actin polymerization and uses the derived free energy for processive polymerization, increasing 15-fold the rate constant for profilin-actin association to barbed ends. Profilin is required for and takes part in the processive function. Single filaments grow at least 10 microm long from formin bound beads without detaching. Transitory formin-associated processes are generated by poisoning of the processive cycle by barbed-end capping proteins. We successfully reconstitute formin-induced motility in vitro, demonstrating that this mechanism accounts for the puzzlingly rapid formin-induced actin processes observed in vivo.
Subfields: Biomedical Engineering, Cardiology and Cardiovascular Medicine, Cell Biology
View Paper: https://www.semanticscholar.org/paper/689b13b73e04a9b61494cf00dbc063e9361a5b9d
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Biomedical Engineering
In Cell Biology
Citations in the corpus
- Actin dynamics, architecture, and mechanics in cell motility. (2014, background): “Similar to a branched actin network, elongating actin bundles can exert enough force to move an object (200, 264).”
- Regulation of actin assembly associated with protrusion and adhesion in cell migration. (2008, background): “However, the total depletion of mDia1 does not abolish the formation of stress fibers but only decreases their elongation rate (82), suggesting that the major function of mDia1 is probably not to nucleate the filaments but to link their processive growth to focal adhesions (187).”
- 'Life is motion': multiscale motility of molecular motors (2005, background): “More recently, surface-anchored formin proteins has been shown to initiate the growth of unbranched actin bundles [71].”
- A Nucleator Arms Race: Cellular Control of Actin Assembly (2010, background): “As a result, they prevent other capping proteins from terminating elongatio”