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. Several mammalian formins, including mDia1, FRL, and formin homology domain protein 1 (FHOD1) are inhibited through an intramolecular interaction between the C-terminal Dia autoregulatory domain (DAD) and its recognition region at the N-terminus. In FHOD1, this autoinhibitory interaction is disrupted through phosphorylation of Ser-1131, Ser-1137, and Thr-1141 by ROCK. Subsequent FHOD1 activation leads to stress fiber formation. In endothelial cells, thrombin activates this ROCK pathway, leading to FHOD1-mediated stress fiber formation.
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*For more information, see UniProt Accession Q9Y613
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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:Boddy, KC et al. (2018) Cell Microbiol. Oct; 20(10): e12866. (WB: Hela cells)
Pandey, P. et al. (2018) Dev Cell. 45(5):661. (WB: rat cardiomyocytes)
Dwyer, J. wt al. (2014)Anat Rec (Hoboken). 297(9):1560 (WB: mouse heart, soleus, tibialis anterior)
Iskratsch, T. et al. (2013) Dev Cell. 27(5):545. (WB: mouse MEF, SYF, transfectants)
Truong, D. et al. (2013) Cell Microbiol. 15(12):2051. (WB, ICC: HeLa transfection)
Staus, D.P. et al. (2011) Arterioscler Thromb Vasc Biol. 31(2):360. (WB: mouse, smooth muscle, siRNA)
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