Journal of Cell Science ot tet ata,M 25,USA 02454, MA Waltham, 415 Street, University, South Brandeis Biology, Center, of Research Department Sciences Medical Basic Rosenstiel Goode* L. Bruce and Breitsprecher Dennis glance a at Formins Glance a at Science Cell xadn oyo ieaueo this the on rapidly summarizing a literature family, organize protein of diverse to body aim expanding we microtubule accompanying been the poster, regulate on and recently directly Here, dynamics. have to actin shown and the of in cytoskeleton roles rearrangements instrumental controlling have that machines polymerization actin conserved are Formins 10.1242/jcs.107250 doi: 1–7 126, ß Science Cell of Journal ( correspondence for *Author 03 ulse yTeCmayo ilgssLtd Biologists of Company The by Published 2013. 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MTs stabilize to al., appear et (Thurston iceia tde aebgnto begun have studies Biochemical ossetwt oei stabilizing in role a with consistent , nvitro in ´ and -egd tal., et s-Delgado nvivo in (Bartolini in Journal of Cell Science omto yetrn noacmlxwt mDia2. with filopodium complex M. inhibit a Biol. Innocenti, into jointly Cell and entering Arp2/3 by D. and formation Xu, WAVE D., (2008). Mascheroni, P., Beli, tblt yatgnzn h ci ciiyo mDia1. of activity actin microtubule Cell the Biol. promotes Mol. antagonizing G. by protein G. stability Gundersen, Actin-capping and N. (2012). microtubules Ramalingam, activity. F., stabilizes nucleation Bartolini, J., actin G. mDia2 its Biol. Schmoranzer, G. formin of Gundersen, B., and independently The L. J. B. (2008). Goode, Moseley, L., Cassimeris, F., and of domains properties Bartolini, homology formin DAAM. biochemical the Drosophila of the function biological of Miha Characterization T., Matusek, Barko oiinn nmueoctsrle nadynamic a on relies H. oocytes filaments. M. P., actin Rassinier, mouse of Verlhac, meshwork V., in and Georget, positioning W., B. K. Leader, Lee, J., Azoury, eyoiae irtblsncsayfrcentrosome for cells. T necessary in reorientation microtubules detyrosinated A. M. Sa Andre membrane lymphocytes. plasma T the human to of Lck of A. transport M. MAL-mediated Alonso, and A. J. aeadtoa ciiis(..actin (e.g. and activities formins additional localization many have Furthermore, partners, regulation. their their do of as binding strength greatly, and directly vary the nucleation activities that species but filament elongation, different actin catalyze in formins emnldahnu-eae omnhmlg protein Andre homology domain. formin autoregulatory diaphanous-related S. terminal A. Alberts, References DC1 biologists.org/lookup/suppl/doi:10.1242/jcs.107250/-/ at online available material Supplementary months. 12 after release for B.G. PMC to in Deposited GM083137] number Institutes [grant National Health the of and D.B. Deutsche BR to the 4116/1-1] number by [grant supported Forschungsgemeinschaft was work This Funding reading. critical for Ydenberg C. and Rodal their WethankJ.Eskin,B.Graziano,R.Jaiswal,A. transform Acknowledgements ways. of can their variety a of consider in activities which context to roles. the ligands, important in cellular activities is formin its it is Moreover, about drawing of it before well conclusions properties individually reasons, the formin not these each characterize to attention For still crucial more Poster). and deserve are (see stabilization and that understood MT bundling) and and severing bundling, depolymerization, filament ez . ora,I,Gnesn .G n Alonso, and G. G. 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