Formins include several families of proteins that regulate actin cytoskeletal dynamics via two conserved formin homology domains, FH1 and FH2. The FH1 region contains poly-proline stretches that promote interactions with profilin. The FH2 domain, located C-terminally to the FH1 domain, is highly conserved in formin proteins and possesses actin nucleation and polymerization activities. Through cooperation of FH1 and FH2, formins construct actin-based structures comprising linear, unbranched filaments that are used in stress fibers, actin cables, microspikes, and contractile rings. A subgroup of the formins is the diaphanous (Dia) family, which includes mDia1 (Diap1), mDia2 (Diap3), and mDia3 (Diap2). The mDia2 protein has been implicated in cell migration and cytokinesis. This Dia protein can nucleate actin polymerization, as well as bind and stabilize microtubules. mDia2 may also have functions in the nucleus, since it is continually shuttled between the cytoplasm and nucleus.
Bartolini, F. et al. (2008) J Cell Biol. 181:523.
Alberts, A.S. (2001) J Biol Chem. 276:2824.
*For more information, see UniProt Accession Q9Z207
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
Product References:Egami, Y. et al. (2017). J Cell Sci. 130(24):4168. (WB: mouse macrophage cells)
Li X. et al. (2017) Haematologica. 102(6):984. (ICC: fetal liver cells)
Spence, EF et al. (2016) J Neurosci. 36(37):9696. (WB: mouse postnatal brain)
Monzo, P. et al. (2016) Mol Biol Cell. 27(8):1246. (WB: rat C6 glioma, shRNA knockdown)
Belin, BJ et al. (2015) Elife. Aug 19;4:e07735. (WB: human HeLa, shRNA knockdown)
Tabdanov, E. et al. (2015) Integrative Biology 7(10):1272 (ICC: human Jurkat T cells)
Sandbo, N. et al. (2013) J Biol Chem 288(22):15466. (WB : human lung fibroblasts)
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