Charras, G. & Paluch, E. Blebs lead the way: how to migrate without lamellipodia. Nature Rev. Mol. Cell Biol. 9, 730–736 (2008).
Daubon, T., Rochelle, T., Bourmeyster, N. & Genot, E. Invadopodia and rolling-type motility are specific features of highly invasive p190bcr-abl leukemic cells. Eur. J. Cell Biol. 91, 978–987 (2012).
Bear, J. E. & Gertler, F. B. Ena/VASP: towards resolving a pointed controversy at the barbed end. J. Cell Sci. 122, 1947–1953 (2009).
Nurnberg, A., Kitzing, T. & Grosse, R. Nucleating actin for invasion. Nature Rev. Cancer 11, 177–187 (2011).
Ridley, A. J. Life at the leading edge. Cell 145, 1012–1022 (2011).
Rotty, J. D., Wu, C. & Bear, J. E. New insights into the regulation and cellular functions of the ARP2/3 complex. Nature Rev. Mol. Cell Biol. 14, 7–12 (2012).
Webb, D. J., Parsons, J. T. & Horwitz, A. F. Adhesion assembly, disassembly and turnover in migrating cells — over and over and over again. Nature Cell Biol. 4, e97–e100 (2002).
Roussos, E. T., Condeelis, J. S. & Patsialou, A. Chemotaxis in cancer. Nature Rev. Cancer 11, 573–587 (2011).
Chen, Q. & Pollard, T. D. Actin filament severing by cofilin is more important for assembly than constriction of the cytokinetic contractile ring. J. Cell Biol. 195, 485–498 (2011).
Demonstrates that cofilin severing activity is crucial for the assembly and contractility of the contractile ring during cytokinesis.
Zhang, L. et al. Regulation of cofilin phosphorylation and asymmetry in collective cell migration during morphogenesis. Development 138, 455–464 (2011).
Gu, J. et al. ADF/cofilin-mediated actin dynamics regulate AMPA receptor trafficking during synaptic plasticity. Nature Neurosci. 13, 1208–1215 (2010).
Bamburg, J. R. & Wiggan, O. P. ADF/cofilin and actin dynamics in disease. Trends Cell Biol. 12, 598–605 (2002).
Bernstein, B. W. & Bamburg, J. R. ADF/cofilin: a functional node in cell biology. Trends Cell Biol. 20, 187–195 (2010).
Poukkula, M., Kremneva, E., Serlachius, M. & Lappalainen, P. Actin-depolymerizing factor homology domain: a conserved fold performing diverse roles in cytoskeletal dynamics. Cytoskeleton (Hoboken) 68, 471–490 (2011).
Reviews the different proteins that contain ADF homology domains.
Andrianantoandro, E. & Pollard, T. D. Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin. Mol. Cell 24, 13–23 (2006).
Ichetovkin, I., Han, J., Pang, K. M., Knecht, D. A. & Condeelis, J. S. Actin filaments are severed by both native and recombinant dictyostelium cofilin but to different extents. Cell Motil. Cytoskeleton 45, 293–306 (2000).
Pavlov, D., Muhlrad, A., Cooper, J., Wear, M. & Reisler, E. Actin filament severing by cofilin. J. Mol. Biol. 365, 1350–1358 (2007).
Carlier, M. F. et al. Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility. J. Cell Biol. 136, 1307–1322 (1997).
Carlier, M. F. & Pantaloni, D. Control of actin dynamics in cell motility. J. Mol. Biol. 269, 459–467 (1997).
Ichetovkin, I., Grant, W. & Condeelis, J. Cofilin produces newly polymerized actin filaments that are preferred for dendritic nucleation by the Arp2/3 complex. Curr. Biol. 12, 79–84 (2002).
Mahaffy, R. E. & Pollard, T. D. Kinetics of the formation and dissociation of actin filament branches mediated by Arp2/3 complex. Biophys. J. 91, 3519–3528 (2006).
Chan, C., Beltzner, C. C. & Pollard, T. D. Cofilin dissociates Arp2/3 complex and branches from actin filaments. Curr. Biol. 19, 537–545 (2009).
Mseka, T. & Cramer, L. P. Actin depolymerization-based force retracts the cell rear in polarizing and migrating cells. Curr. Biol. 21, 2085–2091 (2011).
Wiggan, O., Shaw, A. E., DeLuca, J. G. & Bamburg, J. R. ADF/cofilin regulates actomyosin assembly through competitive inhibition of myosin II binding to F-actin. Dev. Cell 22, 530–543 (2012).
Galkin, V. E. et al. Remodeling of actin filaments by ADF/cofilin proteins. Proc. Natl Acad. Sci. USA 108, 20568–20572 (2011).
Describes the mechanism of actin filament severing by cofilin.
Prochniewicz, E., Janson, N., Thomas, D. D. & De La Cruz, E. M. Cofilin increases the torsional flexibility and dynamics of actin filaments. J. Mol. Biol. 353, 990–1000 (2005).
Suarez, C. et al. Cofilin tunes the nucleotide state of actin filaments and severs at bare and decorated segment boundaries. Curr. Biol. 21, 862–868 (2011).
McCullough, B. R., Blanchoin, L., Martiel, J. L. & De La Cruz, E. M. Cofilin increases the bending flexibility of actin filaments: implications for severing and cell mechanics. J. Mol. Biol. 381, 550–558 (2008).
Bobkov, A. A. et al. Cooperative effects of cofilin (ADF) on actin structure suggest allosteric mechanism of cofilin function. J. Mol. Biol. 356, 325–334 (2006).
Mehta, S. & Sibley, L. D. Toxoplasma gondii actin depolymerizing factor acts primarily to sequester G-actin. J. Biol. Chem. 285, 6835–6847 (2010).
Kuhn, J. R. & Pollard, T. D. Real-time measurements of actin filament polymerization by total internal reflection fluorescence microscopy. Biophys. J. 88, 1387–1402 (2005).
Moriyama, K. & Yahara, I. Human CAP1 is a key factor in the recycling of cofilin and actin for rapid actin turnover. J. Cell Sci. 115, 1591–1601 (2002).
Jockusch, B. M., Murk, K. & Rothkegel, M. The profile of profilins. Rev. Physiol. Biochem. Pharmacol. 159, 131–149 (2007).
Normoyle, K. P. & Brieher, W. M. Cyclase-associated protein (CAP) acts directly on F-actin to accelerate cofilin-mediated actin severing across the range of physiological pH. J. Biol. Chem. 287, 35722–35732 (2012).
DesMarais, V., Ghosh, M., Eddy, R. & Condeelis, J. Cofilin takes the lead. J. Cell Sci. 118, 19–26 (2005).
Hotulainen, P., Paunola, E., Vartiainen, M. K. & Lappalainen, P. Actin-depolymerizing factor and cofilin-1 play overlapping roles in promoting rapid F-actin depolymerization in mammalian nonmuscle cells. Mol. Biol. Cell 16, 649–664 (2005).
Kiuchi, T., Ohashi, K., Kurita, S. & Mizuno, K. Cofilin promotes stimulus-induced lamellipodium formation by generating an abundant supply of actin monomers. J. Cell Biol. 177, 465–476 (2007).
Bravo-Cordero, J. J., Hodgson, L. & Condeelis, J. Directed cell invasion and migration during metastasis. Curr. Opin. Cell Biol. 24, 277–283 (2012).
Brieher, W. M., Kueh, H. Y., Ballif, B. A. & Mitchison, T. J. Rapid actin monomer-insensitive depolymerization of Listeria actin comet tails by cofilin, coronin, and Aip1. J. Cell Biol. 175, 315–324 (2006).
Lin, M. C., Galletta, B. J., Sept, D. & Cooper, J. A. Overlapping and distinct functions for cofilin, coronin and Aip1 in actin dynamics in vivo. J. Cell Sci. 123, 1329–1342 (2010).
Mohri, K., Ono, K., Yu, R., Yamashiro, S. & Ono, S. Enhancement of actin-depolymerizing factor/cofilin-dependent actin disassembly by actin-interacting protein 1 is required for organized actin filament assembly in the Caenorhabditis elegans body wall muscle. Mol. Biol. Cell 17, 2190–2199 (2006).
Okada, K. et al. Xenopus actin-interacting protein 1 (XAip1) enhances cofilin fragmentation of filaments by capping filament ends. J. Biol. Chem. 277, 43011–43016 (2002).
Ono, S., Mohri, K. & Ono, K. Microscopic evidence that actin-interacting protein 1 actively disassembles actin-depolymerizing factor/Cofilin-bound actin filaments. J. Biol. Chem. 279, 14207–14212 (2004).
Philippar, U. et al. A Mena invasion isoform potentiates EGF-induced carcinoma cell invasion and metastasis. Dev. Cell 15, 813–828 (2008).
Bravo-Cordero, J. J. et al. A novel spatiotemporal RhoC activation pathway locally regulates cofilin activity at invadopodia. Curr. Biol. 21, 635–644 (2011).
Shows that confinement of cofilin activity at the invadopodium core involves RHOC-mediated cofilin phosphorylation outside the invadopodium, concentrating activated cofilin inside the invadopodium core.
Bravo-Cordero, J. J. et al. Spatial regulation of RhoC activity defines protrusion formation in migrating cells. J. Cell Sci. 23 May 2013 (doi:10.1242/jcs.123547).
Demonstrates how RHOC spatially restricts cofilin activity at the leading edge to drive polarized protrusions and chemotaxis.
Han, L. et al. Direct stimulation of receptor-controlled phospholipase D1 by phospho-cofilin. EMBO J. 26, 4189–4202 (2007).
DesMarais, V., Macaluso, F., Condeelis, J. & Bailly, M. Synergistic interaction between the Arp2/3 complex and cofilin drives stimulated lamellipod extension. J. Cell Sci. 117, 3499–3510 (2004).
van Rheenen, J. et al. EGF-induced PIP2 hydrolysis releases and activates cofilin locally in carcinoma cells. J. Cell Biol. 179, 1247–1259 (2007).
Shows how PLC releases the inhibitory interaction of cofilin with PtdIns(4,5)P2 at the plasma membrane, resulting in the local activation of cofilin severing activity.
Kim, J. S., Huang, T. Y. & Bokoch, G. M. Reactive oxygen species regulate a Slingshot–cofilin activation pathway. Mol. Biol. Cell 20, 2650–2660 (2009).
Song, X. et al. Initiation of cofilin activity in response to EGF is uncoupled from cofilin phosphorylation and dephosphorylation in carcinoma cells. J. Cell Sci. 119, 2871–2881 (2006).
Sakuma, M. et al. Novel PKCα-mediated phosphorylation site(s) on cofilin and their potential role in terminating histamine release. Mol. Biol. Cell 23, 3707–3721 (2012).
Yoo, Y., Ho, H. J., Wang, C. & Guan, J. L. Tyrosine phosphorylation of cofilin at Y68 by v-Src leads to its degradation through ubiquitin–proteasome pathway. Oncogene 29, 263–272 (2010).
Delorme, V. et al. Cofilin activity downstream of Pak1 regulates cell protrusion efficiency by organizing lamellipodium and lamella actin networks. Dev. Cell 13, 646–662 (2007).
Mouneimne, G. et al. Spatial and temporal control of cofilin activity is required for directional sensing during chemotaxis. Curr. Biol. 16, 2193–2205 (2006).
Sidani, M. et al. Cofilin determines the migration behavior and turning frequency of metastatic cancer cells. J. Cell Biol. 179, 777–791 (2007).
Cao, W., Goodarzi, J. P. & De La Cruz, E. M. Energetics and kinetics of cooperative cofilin–actin filament interactions. J. Mol. Biol. 361, 257–267 (2006).
Ressad, F., Didry, D., Egile, C., Pantaloni, D. & Carlier, M. F. Control of actin filament length and turnover by actin depolymerizing factor (ADF/cofilin) in the presence of capping proteins and ARP2/3 complex. J. Biol. Chem. 274, 20970–20976 (1999).
Tania, N., Prosk, E., Condeelis, J. & Edelstein-Keshet, L. A temporal model of cofilin regulation and the early peak of actin barbed ends in invasive tumor cells. Biophys. J. 100, 1883–1892 (2011).
DesMarais, V., Ichetovkin, I., Condeelis, J. & Hitchcock-DeGregori, S. E. Spatial regulation of actin dynamics: a tropomyosin-free, actin-rich compartment at the leading edge. J. Cell Sci. 115, 4649–4660 (2002).
Munsie, L. N., Desmond, C. R. & Truant, R. Cofilin nuclear–cytoplasmic shuttling affects cofilin–actin rod formation during stress. J. Cell Sci. 125, 3977–3988 (2012).
Obrdlik, A. & Percipalle, P. The F-actin severing protein cofilin-1 is required for RNA polymerase II transcription elongation. Nucleus 2, 72–79 (2011).
Arber, S. et al. Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase. Nature 393, 805–809 (1998).
Nagaoka, R., Minami, N., Hayakawa, K., Abe, H. & Obinata, T. Quantitative analysis of low molecular weight G-actin-binding proteins, cofilin, ADF and profilin, expressed in developing and degenerating chicken skeletal muscles. J. Muscle Res. Cell Motil. 17, 463–473 (1996).
Moriyama, K., Iida, K. & Yahara, I. Phosphorylation of Ser-3 of cofilin regulates its essential function on actin. Genes Cells 1, 73–86 (1996).
Niwa, R., Nagata-Ohashi, K., Takeichi, M., Mizuno, K. & Uemura, T. Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin. Cell 108, 233–246 (2002).
Gohla, A., Birkenfeld, J. & Bokoch, G. M. Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics. Nature Cell Biol. 7, 21–29 (2005).
Ambach, A. et al. The serine phosphatases PP1 and PP2A associate with and activate the actin-binding protein cofilin in human T lymphocytes. Eur. J. Immunol. 30, 3422–3431 (2000).
Mizuno, K. Signaling mechanisms and functional roles of cofilin phosphorylation and dephosphorylation. Cell. Signal. 25, 457–469 (2012).
Reviews the mechanisms regulating the activity of LIMK and SSH and how these proteins influence cofilin activity.
Cai, L., Marshall, T. W., Uetrecht, A. C., Schafer, D. A. & Bear, J. E. Coronin 1B coordinates Arp2/3 complex and cofilin activities at the leading edge. Cell 128, 915–929 (2007).
Nagata-Ohashi, K. et al. A pathway of neuregulin-induced activation of cofilin-phosphatase Slingshot and cofilin in lamellipodia. J. Cell Biol. 165, 465–471 (2004).
Eiseler, T. et al. Protein kinase D1 regulates cofilin-mediated F-actin reorganization and cell motility through slingshot. Nature Cell Biol. 11, 545–556 (2009).
Spratley, S. J., Bastea, L. I., Doppler, H., Mizuno, K. & Storz, P. Protein kinase D regulates cofilin activity through p21-activated kinase 4. J. Biol. Chem. 286, 34254–34261 (2011).
Peterburs, P. et al. Protein kinase D regulates cell migration by direct phosphorylation of the cofilin phosphatase slingshot 1 like. Cancer Res. 69, 5634–5638 (2009).
Wang, Y., Shibasaki, F. & Mizuno, K. Calcium signal-induced cofilin dephosphorylation is mediated by Slingshot via calcineurin. J. Biol. Chem. 280, 12683–12689 (2005).
Zhao, J. W. et al. Regulation of cofilin activity by CaMKII and calcineurin. Am. J. Med. Sci. 344, 462–472 (2012).
Zoudilova, M. et al. β-arrestin-dependent regulation of the cofilin pathway downstream of protease-activated receptor-2. J. Biol. Chem. 282, 20634–20646 (2007).
Hirayama, A., Adachi, R., Otani, S., Kasahara, T. & Suzuki, K. Cofilin plays a critical role in IL-8-dependent chemotaxis of neutrophilic HL-60 cells through changes in phosphorylation. J. Leukoc. Biol. 81, 720–728 (2007).
Boldt, K., Rist, W., Weiss, S. M., Weith, A. & Lenter, M. C. FPRL-1 induces modifications of migration-associated proteins in human neutrophils. Proteomics 6, 4790–4799 (2006).
Sun, C. X., Magalhaes, M. A. & Glogauer, M. Rac1 and Rac2 differentially regulate actin free barbed end formation downstream of the fMLP receptor. J. Cell Biol. 179, 239–245 (2007).
Tang, W. et al. A PLCβ/PI3Kγ–GSK3 signaling pathway regulates cofilin phosphatase slingshot2 and neutrophil polarization and chemotaxis. Dev. Cell 21, 1038–1050 (2011).
Nishita, M. et al. Phosphoinositide 3-kinase-mediated activation of cofilin phosphatase Slingshot and its role for insulin-induced membrane protrusion. J. Biol. Chem. 279, 7193–7198 (2004).
Scott, R. W. et al. LIM kinases are required for invasive path generation by tumor and tumor-associated stromal cells. J. Cell Biol. 191, 169–185 (2010).
Toshima, J. et al. Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation. Mol. Biol. Cell 12, 1131–1145 (2001).
Toshima, J., Toshima, J. Y., Takeuchi, K., Mori, R. & Mizuno, K. Cofilin phosphorylation and actin reorganization activities of testicular protein kinase 2 and its predominant expression in testicular Sertoli cells. J. Biol. Chem. 276, 31449–31458 (2001).
Maekawa, M. et al. Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase. Science 285, 895–898 (1999).
Dan, C., Kelly, A., Bernard, O. & Minden, A. Cytoskeletal changes regulated by the PAK4 serine/threonine kinase are mediated by LIM kinase 1 and cofilin. J. Biol. Chem. 276, 32115–32121 (2001).
Edwards, D. C., Sanders, L. C., Bokoch, G. M. & Gill, G. N. Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Nature Cell Biol. 1, 253–259 (1999).
Sumi, T., Matsumoto, K., Shibuya, A. & Nakamura, T. Activation of LIM kinases by myotonic dystrophy kinase-related Cdc42-binding kinase α. J. Biol. Chem. 276, 23092–23096 (2001).
Kobayashi, M., Nishita, M., Mishima, T., Ohashi, K. & Mizuno, K. MAPKAPK-2-mediated LIM-kinase activation is critical for VEGF-induced actin remodeling and cell migration. EMBO J. 25, 713–726 (2006).
Wang, W., Eddy, R. & Condeelis, J. The cofilin pathway in breast cancer invasion and metastasis. Nature Rev. Cancer 7, 429–440 (2007).
Gorbatyuk, V. Y. et al. Mapping the phosphoinositide-binding site on chick cofilin explains how PIP2 regulates the cofilin–actin interaction. Mol. Cell 24, 511–522 (2006).
Yonezawa, N., Nishida, E., Iida, K., Yahara, I. & Sakai, H. Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides. J. Biol. Chem. 265, 8382–8386 (1990).
Sun, H. Q., Yamamoto, M., Mejillano, M. & Yin, H. L. Gelsolin, a multifunctional actin regulatory protein. J. Biol. Chem. 274, 33179–33182 (1999).
Yin, H. L. & Janmey, P. A. Phosphoinositide regulation of the actin cytoskeleton. Annu. Rev. Physiol. 65, 761–789 (2003).
Leyman, S. et al. Unbalancing the phosphatidylinositol-4,5-bisphosphate–cofilin interaction impairs cell steering. Mol. Biol. Cell 20, 4509–4523 (2009).
Ghosh, M. et al. Cofilin promotes actin polymerization and defines the direction of cell motility. Science 304, 743–746 (2004).
Chen, H. et al. In vitro activity differences between proteins of the ADF/cofilin family define two distinct subgroups. Biochemistry 43, 7127–7142 (2004).
Hawkins, M., Pope, B., Maciver, S. K. & Weeds, A. G. Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments. Biochemistry 32, 9985–9993 (1993).
Maciver, S. K., Pope, B. J., Whytock, S. & Weeds, A. G. The effect of two actin depolymerizing factors (ADF/cofilins) on actin filament turnover: pH sensitivity of F-actin binding by human ADF, but not of Acanthamoeba actophorin. Eur. J. Biochem. 256, 388–397 (1998).
Bernstein, B. W. et al. Intracellular pH modulation of ADF/cofilin proteins. Cell Motil. Cytoskeleton 47, 319–336 (2000).
Frantz, C. et al. Cofilin is a pH sensor for actin free barbed end formation: role of phosphoinositide binding. J. Cell Biol. 183, 865–879 (2008).
Magalhaes, M. A. et al. Cortactin phosphorylation regulates cell invasion through a pH-dependent pathway. J. Cell Biol. 195, 903–920 (2011).
Shows that the recruitment of NHE1 to invadopodia locally increases the pH, which releases the inhibitory interacting of cofilin with cortactin and leads to the activation of cofilin severing activity.
Kemp, G., Young, H. & Fliegel, L. Structure and function of the human Na+/H+ exchanger isoform 1. Channels (Austin) 2, 329–336 (2008).
Zhao, H., Hakala, M. & Lappalainen, P. ADF/cofilin binds phosphoinositides in a multivalent manner to act as a PIP2-density sensor. Biophys. J. 98, 2327–2336 (2010).
Webb, B. A., Chimenti, M., Jacobson, M. P. & Barber, D. L. Dysregulated pH: a perfect storm for cancer progression. Nature Rev. Cancer 11, 671–677 (2011).
Wang, W. et al. The activity status of cofilin is directly related to invasion, intravasation, and metastasis of mammary tumors. J. Cell Biol. 173, 395–404 (2006).
Wang, W. et al. Coordinated regulation of pathways for enhanced cell motility and chemotaxis is conserved in rat and mouse mammary tumors. Cancer Res. 67, 3505–3511 (2007).
Buccione, R., Caldieri, G. & Ayala, I. Invadopodia: specialized tumor cell structures for the focal degradation of the extracellular matrix. Cancer Metastasis Rev. 28, 137–149 (2009).
Linder, S., Wiesner, C. & Himmel, M. Degrading devices: invadosomes in proteolytic cell invasion. Annu. Rev. Cell Dev. Biol. 27, 185–211 (2011).
Murphy, D. A. & Courtneidge, S. A. The 'ins' and 'outs' of podosomes and invadopodia: characteristics, formation and function. Nature Rev. Mol. Cell Biol. 12, 413–426 (2011).
Weaver, A. M. Invadopodia: specialized cell structures for cancer invasion. Clin. Exp. Metastasis 23, 97–105 (2006).
References 109–112 review invasive protrusions.
Oser, M. et al. Cortactin regulates cofilin and N-WASp activities to control the stages of invadopodium assembly and maturation. J. Cell Biol. 186, 571–587 (2009).
Mader, C. C. et al. An EGFR–Src–Arg–cortactin pathway mediates functional maturation of invadopodia and breast cancer cell invasion. Cancer Res. 71, 1730–1741 (2011).
Pollard, T. D., Blanchoin, L. & Mullins, R. D. Molecular mechanisms controlling actin filament dynamics in nonmuscle cells. Annu. Rev. Biophys. Biomol. Struct. 29, 545–576 (2000).
Pollard, T. D. & Borisy, G. G. Cellular motility driven by assembly and disassembly of actin filaments. Cell 112, 453–465 (2003).
Mouneimne, G. et al. Phospholipase C and cofilin are required for carcinoma cell directionality in response to EGF stimulation. J. Cell Biol. 166, 697–708 (2004).
Shao, D., Forge, A., Munro, P. M. & Bailly, M. Arp2/3 complex-mediated actin polymerisation occurs on specific pre-existing networks in cells and requires spatial restriction to sustain functional lamellipod extension. Cell Motil. Cytoskeleton 63, 395–414 (2006).
Wu, C. et al. Arp2/3 is critical for lamellipodia and response to extracellular matrix cues but is dispensable for chemotaxis. Cell 148, 973–987 (2012).
van Rheenen, J., Condeelis, J. & Glogauer, M. A common cofilin activity cycle in invasive tumor cells and inflammatory cells. J. Cell Sci. 122, 305–311 (2009).
Lai, F. P. et al. Arp2/3 complex interactions and actin network turnover in lamellipodia. EMBO J. 27, 982–992 (2008).
Okreglak, V. & Drubin, D. G. Cofilin recruitment and function during actin-mediated endocytosis dictated by actin nucleotide state. J. Cell Biol. 178, 1251–1264 (2007).
Ohashi, K., Kiuchi, T., Shoji, K., Sampei, K. & Mizuno, K. Visualization of cofilin-actin and Ras–Raf interactions by bimolecular fluorescence complementation assays using a new pair of split Venus fragments. Biotechniques 52, 45–50 (2012).
Soderberg, O. et al. Direct observation of individual endogenous protein complexes in situ by proximity ligation. Nature Methods 3, 995–1000 (2006).