Reactome | Activated FMNL3 binds G-actin

Activated FMNL3 binds G-actin

Stable Identifier

R-HSA-5665767

Type

Reaction [binding]

Species

Homo sapiens

Compartment

cytosol, plasma membrane

ReviewStatus

5/5

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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
15507212	Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis Carlier, MF, Egile, C, Didry, D, Romero, S, Pantaloni, D, Le Clainche, C	Cell	2004
23222643	FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation Gauvin, TJ, Higgs, HN, Heimsath, EG, Thompson, ME, Kull, FJ	Nat. Struct. Mol. Biol.	2013
22275430	The formin FMNL3 is a cytoskeletal regulator of angiogenesis Swain, RK, Higgs, HN, Copeland, JW, Hetheridge, C, Mellor, H, Bicknell, R, Scott, AN	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 Ridley, AJ, Vega, FM, Fruhwirth, G, Ng, T	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 Higgs, HN, Heimsath, EG	J. Biol. Chem.	2012
16439214	Control of the assembly of ATP- and ADP-actin by formins and profilin Pollard, TD, Higgs, HN, Harris, ES, Mahaffy, R, Kovar, DR	Cell	2006