Selected Publications

Ji, W. K., Hatch, A. L., Merrill, R. A., Strack, S. & Higgs, H. N. (2015) Actin filaments target the oligomeric maturation of the dynamin GTPase Drp1 to mitochondrial fission sites. eLife. PMID: 26609810.

Young, L. E., Heimsath, E. G. & Higgs, H. N. (2015) Cell type-dependent mechanisms for formin-mediated assembly of filopodia. Mol. Biol. Cell. 26(25): 4646-4659.

Gurel, P. S., Guo, B., Shu, R., Mirke, D. F. & Higgs, H. N. (2015) Assembly and turnover of short actin filaments by the formin INF2 and profilin. J. Biol. Chem. 11:290(37): 22494-22506.

Gauvin, T. J., Young, L. E. & Higgs, H. N. (2015) The formin FMNL3 assembles plasma membrane protrusions that participate in cell-cell adhesion. Mol. Biol. Cell. 26(3): 467-77.

Hatch, A. L., Gurel, P. S. & Higgs, H. N. (2014) Novel roles for actin in mitochondrial fission. J. Cell Sci. 127(21): 4549-4560.

Gurel, P. S., Hatch, A. L, & Higgs, H. N. (2014) Connecting the cytoskeleton to the endoplasmic reticulum and Golgi. Curr. Biol. 24(14): R660-72.

Korobova, F., Gauvin, T. J. & Higgs, H. N. (2014) A role for myosin II in mammalian mitochondrial fission. Curr. Biol. 24(4): 409-14.

Gurel, P. S., Ge, P., Grintsevich, E. E., Shu, R., Blanchoin, L., Zhou, Z. H., Reisler, E. & Higgs, H. N. (2014) INF2-mediated severing through actin filament encirclement and disruption. Curr. Biol. 24(2): 156-64.

Ramabhadran V., Hatch A. L., & Higgs H. N. (2013) Actin monomers activate inverted formin 2 by competing with its autoinhibitory interaction. J. Biol. Chem. 288(37): 26847-55.

Korobova, F., Ramabhadran, V. & Higgs, H. N. (2013) An actin-dependent step in mitochondrial fission mediated by the ER-associated formin INF2. Science 339(6118): 464-467.

Thompson, M. E., Heimsath, E. G., Gauvin, T. J., Higgs, H. N.* & Kull, F. J.* (2013) FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation. Nature Struct. Mol. Biol. 20(1): 111-118. *co-corresponding authors.

Ramabhadran, V., Gurel, P. G. & Higgs, H. N. (2012) Mutations to the formin homology 2 domain of INF2 have unexpected effects on actin polymerization and severing. J. Biol. Chem. 287(41): 34234-45.

Hager, M. H., Morley, S., Bielenberg, D. R., Gao, S., Morello, M., Holcomb, I. N., Liu, W., Mouneimne, G., Demichelis, F., Kim, J., Solomon, K. R., Adam, R. M., Isaacs, W. B., Higgs, H. N., Vessella, R., Di Visio, D. & Freeman, M. R. (2012) DIAPH3 governs the cellular transition to the amoeboid tumour phenotype. EMBO Mol. Med. 4(8): 743-760.

Hetheridge, C., Scott, A. N., Swain, R. K., Copeland, J. W., Higgs, H. N., Bicknell, R. & Mellor, H. (2012) The formin FMNL3 is a cytoskeletal regulator of angiogenesis. J. Cell Sci. 125(6): 1420-1426.

Heimsath, E. G. & Higgs, H. N. (2012). The C-terminus of the formin FMNL3 accelerates actin polymerization and contains a WH2-like sequence that binds both monomers and filament barbed ends. J. Biol. Chem. 287(5): 3087-3098.

Gaillard, J., Ramabhadran, V., Neumann, E., Gurel, P., Blanchoin, L., Vantard, M., & Higgs, H. N. (2011). Differential Interactions of the formins INF2, mDia1, and mDia2 with microtubules. Molec. Biol. Cell. 22(23): 4575-4587.

Ramabhadran, V., Korobova, F., Rahme, G., & Higgs, H. N. (2011). Splice variant-specific cellular function of the formin INF2 in the maintenance of Golgi architecture. Molec. Biol. Cell. 22(24): 4822-4833.

Sun, H., Schlondorff, J. S., Brown, E. J., Higgs, H. N. & Pollak, M. R. (2011) Rho activation of mDia formins is modulated by an interaction with inverted formin 2 (INF2). Proc. Natl. Acad. Sci. USA. 15; 108(7): 2933-2938.

Harris, E. S., Gauvin, T. J., Heimsath, E. G. & Higgs, H. N. (2010). Assembly of filopodia by the formin FRL2 (FMNL3). Cytoskeleton. 67(12): 755-772.

Brown, E. J., Schlondorff, J. S., Becker, D. J., Tsukaguchi, H., Uscinski, A. L., Higgs, H. N., Henderson, J. M., & Pollak M. R. (2010) Mutations in the formin gene INF2 cause focal segmental glomerulosclerosis. Nat. Genet. 42(1): 72-76.

Gauvin, T. J., Fukui, J., Peterson, J. R., & Higgs, H. N. (2009) Isoform-selective chemical inhibition of mDia-mediated actin assembly. Biochemistry 48(40): 9327-9329. PMCID: PMC2758331.

Chhabra, E. S., Ramabhadran, V., Gerber, S., & Higgs, H. N. (2009) INF2 is an endoplasmic reticulum-associated formin protein. J. Cell Sci. 122(9): 1430-1440. PMCID: PMC2721004.

Nicholson-Dykstra, S. M. & Higgs, H. N. (2008) Arp2 depletion inhibits sheet-like protrusions but not linear protrusions of fibroblasts and lymphocytes. Cell Motil. Cytoskeleton. 65(11): 904-922. PMCID: PMC2757053.

Chhabra, E. S. & Higgs, H. N. (2007) The many faces of actin: matching assembly factors with cellular structures. Nat. Cell Biol. 9(10): 1110-1121.

Chhabra, E. S. & Higgs, H. N. (2006) INF2 is a WH2 motif-containing formin that severs actin filaments and accelerates both polymerization and depolymerization. J. Biol. Chem. 281(36):26754-26767.

Harris, E. S., Rouiller, I., Hanein, D., & Higgs, H. N. (2006) Mechanistic differences in actin bundling activity of two mammalian formins, FRL1 and mDia2. J. Biol. Chem. 281 (20): 14383-14392.

Kovar, D. R., Harris, E. S., Mahaffy, R., Higgs, H. N., & Pollard, T. D. Control of the assembly of ATP- and ADP-actin by formins and profilin. (2006) Cell. 124: 423-435.

Li, F. & Higgs, H. N. Dissecting requirements for auto-inhibition of actin nucleation by the formin, mDia1. (2005) J. Biol. Chem. 280 (8): 6986-6992.

Higgs, H. N. & Peterson, K. J. Phylogenetic analysis of the Formin Homology 2 domain. (2005) Mol. Biol. Cell. 16(1): 1-13.

Majstoravich, S., Zhang, J., Nicholson-Dykstra, S., Linder, S., Friedrich, W., Siminovitch, K. A., & Higgs, H. N. Lymphocyte microvilli are dynamic, actin-dependent structures that do not require Wiskott-Aldrich syndrome protein (WASp) for their morphology. (2004) Blood. 104(5): 1396-1403.

Harris, E. S., Li, F., & Higgs, H. N. The mouse formin, FRLalpha, slows actin filament barbed end elongation, competes with capping protein, accelerates polymerization from monomers, and severs filaments. (2004) J. Biol. Chem. 279(19): 20076-20087.

Li, F., & Higgs, H. N. The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition. (2003) Curr. Biol. 13(15): 1335-1340.