Formins are a family of structurally conserved proteins that regulate the assembly of the fast-growing end of actin filaments. New work shows that the molecular mechanism of formin function is conserved but that the rates of the reactions vary within and between species to such a degree that the mechanisms of various formin family members may seem to differ qualitatively.
This is a preview of subscription content, access via your institution
Relevant articles
Open Access articles citing this article.
-
Cyclophosphamide treatment modifies the thermal stability of profilin bound monomeric and leiomodin2 bound filamentous actin
Journal of Thermal Analysis and Calorimetry Open Access 05 December 2022
-
A structural model of the profilin–formin pacemaker system for actin filament elongation
Scientific Reports Open Access 28 November 2022
-
F-actin architecture determines constraints on myosin thick filament motion
Nature Communications Open Access 16 November 2022
Access options
Subscribe to this journal
Receive 12 print issues and online access
$209.00 per year
only $17.42 per issue
Rent or buy this article
Prices vary by article type
from$1.95
to$39.95
Prices may be subject to local taxes which are calculated during checkout
References
Pollard, T. D. & Borisy, G. G. Cell 112, 453–465 (2003).
Kovar, D. R. J. Cell Biol. 161, 875–887 (2003).
Zigmond, S. H. et al. Curr. Biol. 13, 1820–1823 (2003).
Harris, E. S., Li, F. & Higgs, H. N. J. Biol. Chem. 279, 20076–20087 (2004).
Moseley, J. B. et al. Mol. Biol. Cell 15, 896–907 (2004).
Kovar, D. R. & Pollard, T. D. Proc. Natl Acad. Sci. USA 101, 14725–14730 (2004).
Higashida, C. et al. Science 303, 2007–2010 (2004).
Romero, S. et al. Cell 119, 419–429 (2004).
Dickinson, R. B., Caro, L. & Purich, D. L. Biophys. J. 87, 2838–2854 (2004).
Loisel, T. P., Boujemaa, R., Pantaloni, D. & Carlier, M. F. Nature 401, 613–616 (1999).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Kovar, D., Pollard, T. Progressing actin: Formin as a processive elongation machine. Nat Cell Biol 6, 1158–1159 (2004). https://doi.org/10.1038/ncb1204-1158
Issue Date:
DOI: https://doi.org/10.1038/ncb1204-1158
This article is cited by
-
Cyclophosphamide treatment modifies the thermal stability of profilin bound monomeric and leiomodin2 bound filamentous actin
Journal of Thermal Analysis and Calorimetry (2023)
-
A structural model of the profilin–formin pacemaker system for actin filament elongation
Scientific Reports (2022)
-
F-actin architecture determines constraints on myosin thick filament motion
Nature Communications (2022)
-
SPIN90 associates with mDia1 and the Arp2/3 complex to regulate cortical actin organization
Nature Cell Biology (2020)
-
Tropomodulin-3 is essential in asymmetric division during mouse oocyte maturation
Scientific Reports (2016)