Abstract
Formins are remarkable large multi-domain proteins that utilize a novel mechanism to rapidly assemble actin filaments for diverse cellular processes such as division, motility, polarity, stress fibers and focal adhesions. The formin homology 1 and 2 domains (FH1 and FH2) nucleate actin assembly and then remain processively associated with the elongating barbed end while directing the rapid addition of profilin-actin as much as 10-fold faster than the theoretical diffusion limit. Regulatory domains flank the FH1FH2 domains. Many formins are autoinhibited through association of their N- and C-terminal regulatory domains, and are partially activated by Rho GTPases. Most cells express multiple formin isoforms. We are beginning to understand that differences in both the regulatory and actin assembly properties tailor diverse formins for specific cellular processes.
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Acknowledgments
We thank Erin Neidt for helpful suggestions. Work on formins in the Kovar lab is funded by a National Institutes of Health grant RO1GM079265.
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Kovar, D.R., Bestul, A.J., Li, Y., Scott, B.J. (2010). Formin-Mediated Actin Assembly. In: Carlier, MF. (eds) Actin-based Motility. Springer, Dordrecht. https://doi.org/10.1007/978-90-481-9301-1_12
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