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Actin monomers activate inverted formin 2 by competing with its autoinhibitory interaction.

Ramabhadran V, Hatch AL, Higgs HN.

J Biol Chem. 2013 Sep 13;288(37):26847-55. doi: 10.1074/jbc.M113.472415. Epub 2013 Aug 6.


How ATP hydrolysis controls filament assembly from profilin-actin: implication for formin processivity.

Romero S, Didry D, Larquet E, Boisset N, Pantaloni D, Carlier MF.

J Biol Chem. 2007 Mar 16;282(11):8435-45. Epub 2007 Jan 7.


INF2 is an endoplasmic reticulum-associated formin protein.

Chhabra ES, Ramabhadran V, Gerber SA, Higgs HN.

J Cell Sci. 2009 May 1;122(Pt 9):1430-40. doi: 10.1242/jcs.040691. Epub 2009 Apr 14.


Assembly and turnover of short actin filaments by the formin INF2 and profilin.

Gurel PS, A M, Guo B, Shu R, Mierke DF, Higgs HN.

J Biol Chem. 2015 Sep 11;290(37):22494-506. doi: 10.1074/jbc.M115.670166. Epub 2015 Jun 29.


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 Jr, Higgs HN.

J Biol Chem. 2012 Jan 27;287(5):3087-98. doi: 10.1074/jbc.M111.312207. Epub 2011 Nov 17.


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 Oct 29;119(3):419-29.


Mutations to the formin homology 2 domain of INF2 protein have unexpected effects on actin polymerization and severing.

Ramabhadran V, Gurel PS, Higgs HN.

J Biol Chem. 2012 Oct 5;287(41):34234-45. doi: 10.1074/jbc.M112.365122. Epub 2012 Aug 9.


Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain.

Otomo T, Tomchick DR, Otomo C, Panchal SC, Machius M, Rosen MK.

Nature. 2005 Feb 3;433(7025):488-94. Epub 2005 Jan 5.


Mechanism of formin-induced nucleation of actin filaments.

Pring M, Evangelista M, Boone C, Yang C, Zigmond SH.

Biochemistry. 2003 Jan 21;42(2):486-96.


Mouse MIM, a tissue-specific regulator of cytoskeletal dynamics, interacts with ATP-actin monomers through its C-terminal WH2 domain.

Mattila PK, Salminen M, Yamashiro T, Lappalainen P.

J Biol Chem. 2003 Mar 7;278(10):8452-9. Epub 2002 Dec 13.


Formin differentially utilizes profilin isoforms to rapidly assemble actin filaments.

Neidt EM, Scott BJ, Kovar DR.

J Biol Chem. 2009 Jan 2;284(1):673-84. doi: 10.1074/jbc.M804201200. Epub 2008 Oct 31.


Biochemical characterization of the diaphanous autoregulatory interaction in the formin homology protein FHOD1.

Schönichen A, Alexander M, Gasteier JE, Cuesta FE, Fackler OT, Geyer M.

J Biol Chem. 2006 Feb 24;281(8):5084-93. Epub 2005 Dec 16.


INF2-mediated severing through actin filament encirclement and disruption.

Gurel PS, Ge P, Grintsevich EE, Shu R, Blanchoin L, Zhou ZH, Reisler E, Higgs HN.

Curr Biol. 2014 Jan 20;24(2):156-64. doi: 10.1016/j.cub.2013.12.018. Epub 2014 Jan 9.


Formin proteins: a domain-based approach.

Higgs HN.

Trends Biochem Sci. 2005 Jun;30(6):342-53. Review.


The basic region of the diaphanous-autoregulatory domain (DAD) is required for autoregulatory interactions with the diaphanous-related formin inhibitory domain.

Wallar BJ, Stropich BN, Schoenherr JA, Holman HA, Kitchen SM, Alberts AS.

J Biol Chem. 2006 Feb 17;281(7):4300-7. Epub 2005 Dec 18.


Actin filament bundling and different nucleating effects of mouse Diaphanous-related formin FH2 domains on actin/ADF and actin/cofilin complexes.

Machaidze G, Sokoll A, Shimada A, Lustig A, Mazur A, Wittinghofer A, Aebi U, Mannherz HG.

J Mol Biol. 2010 Nov 5;403(4):529-45. doi: 10.1016/j.jmb.2010.09.017. Epub 2010 Oct 1.


Energetic requirements for processive elongation of actin filaments by FH1FH2-formins.

Paul AS, Pollard TD.

J Biol Chem. 2009 May 1;284(18):12533-40. doi: 10.1074/jbc.M808587200. Epub 2009 Feb 26.


Dissecting requirements for auto-inhibition of actin nucleation by the formin, mDia1.

Li F, Higgs HN.

J Biol Chem. 2005 Feb 25;280(8):6986-92. Epub 2004 Dec 9.

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