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The Rho family GTPase Rif induces filopodia through mDia2.

Pellegrin S, Mellor H.

Curr Biol. 2005 Jan 26;15(2):129-33.


Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena complex.

Krugmann S, Jordens I, Gevaert K, Driessens M, Vandekerckhove J, Hall A.

Curr Biol. 2001 Oct 30;11(21):1645-55.


Rif-mDia1 interaction is involved in filopodium formation independent of Cdc42 and Rac effectors.

Goh WI, Sudhaharan T, Lim KB, Sem KP, Lau CL, Ahmed S.

J Biol Chem. 2011 Apr 15;286(15):13681-94. doi: 10.1074/jbc.M110.182683. Epub 2011 Feb 21.


The Cdc42 effector IRSp53 generates filopodia by coupling membrane protrusion with actin dynamics.

Lim KB, Bu W, Goh WI, Koh E, Ong SH, Pawson T, Sudhaharan T, Ahmed S.

J Biol Chem. 2008 Jul 18;283(29):20454-72. doi: 10.1074/jbc.M710185200. Epub 2008 Apr 29.


Regulation of cell shape by Cdc42 is mediated by the synergic actin-bundling activity of the Eps8-IRSp53 complex.

Disanza A, Mantoani S, Hertzog M, Gerboth S, Frittoli E, Steffen A, Berhoerster K, Kreienkamp HJ, Milanesi F, Di Fiore PP, Ciliberto A, Stradal TE, Scita G.

Nat Cell Biol. 2006 Dec;8(12):1337-47. Epub 2006 Nov 19.


WAVE and Arp2/3 jointly inhibit filopodium formation by entering into a complex with mDia2.

Beli P, Mascheroni D, Xu D, Innocenti M.

Nat Cell Biol. 2008 Jul;10(7):849-57. doi: 10.1038/ncb1745. Epub 2008 May 30.


Small GTPase Tc10 and its homologue RhoT induce N-WASP-mediated long process formation and neurite outgrowth.

Abe T, Kato M, Miki H, Takenawa T, Endo T.

J Cell Sci. 2003 Jan 1;116(Pt 1):155-68.


Disruption of the Diaphanous-related formin Drf1 gene encoding mDia1 reveals a role for Drf3 as an effector for Cdc42.

Peng J, Wallar BJ, Flanders A, Swiatek PJ, Alberts AS.

Curr Biol. 2003 Apr 1;13(7):534-45.


N-WASP, WAVE and Mena play different roles in the organization of actin cytoskeleton in lamellipodia.

Nakagawa H, Miki H, Ito M, Ohashi K, Takenawa T, Miyamoto S.

J Cell Sci. 2001 Apr;114(Pt 8):1555-65.


Atypical mechanism of regulation of the Wrch-1 Rho family small GTPase.

Shutes A, Berzat AC, Cox AD, Der CJ.

Curr Biol. 2004 Nov 23;14(22):2052-6.


The diaphanous-related formin DAAM1 collaborates with the Rho GTPases RhoA and Cdc42, CIP4 and Src in regulating cell morphogenesis and actin dynamics.

Aspenström P, Richnau N, Johansson AS.

Exp Cell Res. 2006 Jul 15;312(12):2180-94. Epub 2006 Apr 21.


The role of formins in filopodia formation.

Mellor H.

Biochim Biophys Acta. 2010 Feb;1803(2):191-200. doi: 10.1016/j.bbamcr.2008.12.018. Epub 2009 Jan 3. Review.


The mammalian verprolin, WIRE induces filopodia independent of N-WASP through IRSp53.

Misra A, Rajmohan R, Lim RP, Bhattacharyya S, Thanabalu T.

Exp Cell Res. 2010 Oct 15;316(17):2810-24. doi: 10.1016/j.yexcr.2010.07.015. Epub 2010 Aug 1.


mDia1 and WAVE2 proteins interact directly with IRSp53 in filopodia and are involved in filopodium formation.

Goh WI, Lim KB, Sudhaharan T, Sem KP, Bu W, Chou AM, Ahmed S.

J Biol Chem. 2012 Feb 10;287(7):4702-14. doi: 10.1074/jbc.M111.305102. Epub 2011 Dec 17.


Dia-interacting protein modulates formin-mediated actin assembly at the cell cortex.

Eisenmann KM, Harris ES, Kitchen SM, Holman HA, Higgs HN, Alberts AS.

Curr Biol. 2007 Apr 3;17(7):579-91.


A novel actin bundling/filopodium-forming domain conserved in insulin receptor tyrosine kinase substrate p53 and missing in metastasis protein.

Yamagishi A, Masuda M, Ohki T, Onishi H, Mochizuki N.

J Biol Chem. 2004 Apr 9;279(15):14929-36. Epub 2004 Jan 29.


Filopodia formation induced by active mDia2/Drf3.

Block J, Stradal TE, Hänisch J, Geffers R, Köstler SA, Urban E, Small JV, Rottner K, Faix J.

J Microsc. 2008 Sep;231(3):506-17. doi: 10.1111/j.1365-2818.2008.02063.x.


Wrch1 is a GTPase-deficient Cdc42-like protein with unusual binding characteristics and cellular effects.

Saras J, Wollberg P, Aspenström P.

Exp Cell Res. 2004 Oct 1;299(2):356-69.

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