Activated FMNL3 binds G-actin

Stable Identifier
R-HSA-5665767
Type
Reaction [binding]
Species
Homo sapiens
Compartment
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Activated FMNL3 (presumably associated with RHOC:GTP) has the ability to directly bind G-actin through knob and coiled-coil subdomains of the FMNL3 FH2 domain. The proline-rich FH1 domain which precedes the FH2 domain presumably interacts with profilins bound to G-actin (Romero et al. 2004, Kovar et al. 2006, Kuhn and Geyer 2014). FMNL3 contributes to the elongation of actin filaments (Heimsath and Higgs 2012, Thompson et al. 2013). Activated FMNL3 may also trigger microtubule alignment during angiogenesis (Hetheridge et al. 2012).

Literature References
PubMed ID Title Journal Year
23222643 FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation

Thompson, ME, Heimsath, EG, Gauvin, TJ, Higgs, HN, Kull, FJ

Nat. Struct. Mol. Biol. 2013
15507212 Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis

Romero, S, Le Clainche, C, Didry, D, Egile, C, Pantaloni, D, Carlier, MF

Cell 2004
22275430 The formin FMNL3 is a cytoskeletal regulator of angiogenesis

Hetheridge, C, Scott, AN, Swain, RK, Copeland, JW, Higgs, HN, Bicknell, R, Mellor, H

J. Cell. Sci. 2012
24914801 Formins as effector proteins of Rho GTPases

Kühn, S, Geyer, M

Small GTPases 2014
21576392 RhoA and RhoC have distinct roles in migration and invasion by acting through different targets

Vega, FM, Fruhwirth, G, Ng, T, Ridley, AJ

J. Cell Biol. 2011
22094460 The C terminus of formin FMNL3 accelerates actin polymerization and contains a WH2 domain-like sequence that binds both monomers and filament barbed ends

Heimsath, EG, Higgs, HN

J. Biol. Chem. 2012
16439214 Control of the assembly of ATP- and ADP-actin by formins and profilin

Kovar, DR, Harris, ES, Mahaffy, R, Higgs, HN, Pollard, TD

Cell 2006
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