Cofilin Acts as a Booster for Progression of Malignant Tumors Represented by Glioma

References

• Nishida E, Maekawa S, Sakai H. Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin. Biochemistry. 1984;23(22):5307–5313. doi:10.1021/bi00317a032
   PubMed Web of Science ®Google Scholar
• Bamburg JR, Harris HE, Weeds AG. Partial purification and characterization of an actin depolymerizing factor from brain. FEBS Lett. 1980;121(1):178–182. doi:10.1016/0014-5793(80)81292-0
   PubMed Web of Science ®Google Scholar
• Bamburg JR. Proteins of the ADF/cofilin family: essential regulators of actin dynamics. Annu Rev Cell Dev Biol. 1999;15:185–230. doi:10.1146/annurev.cellbio.15.1.185
   PubMed Web of Science ®Google Scholar
• Maciver SK, Hussey PJ. The ADF/cofilin family: actin-remodeling proteins. Genome Biol. 2002;3(5):3007. doi:10.1186/gb-2002-3-5-reviews3007
   Web of Science ®Google Scholar
• Pollard TD, Blanchoin L, Mullins RD. Molecular mechanisms controlling actin filament dynamics in nonmuscle cells. Annu Rev Biophys Biomol Struct. 2000;29:545–576. doi:10.1146/annurev.biophys.29.1.545
   PubMedGoogle Scholar
• Bamburg JR, Bray D. Distribution and cellular localization of actin depolymerizing factor. J Cell Biol. 1987;105(6 Pt 1):2817–2825. doi:10.1083/jcb.105.6.2817
   PubMed Web of Science ®Google Scholar
• Svitkina TM, Borisy GG. Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. J Cell Biol. 1999;145(5):1009–1026. doi:10.1083/jcb.145.5.1009
   PubMed Web of Science ®Google Scholar
• Carlier MF, Laurent V, Santolini J, et al. Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility. J Cell Biol. 1997;136(6):1307–1322. doi:10.1083/jcb.136.6.1307
   PubMed Web of Science ®Google Scholar
• Maciver SK. How ADF/cofilin depolymerizes actin filaments. Curr Opin Cell Biol. 1998;10(1):140–144. doi:10.1016/s0955-0674(98)80097-5
   PubMed Web of Science ®Google Scholar
• Wioland H, Guichard B, Senju Y, et al. ADF/Cofilin accelerates actin dynamics by severing filaments and promoting their depolymerization at both ends. Curr Biol. 2017;27(13):1956–67.e7. doi:10.1016/j.cub.2017.05.048
   PubMed Web of Science ®Google Scholar
• Bernstein BW, Painter WB, Chen H, Minamide LS, Abe H, Bamburg JR. Intracellular pH modulation of ADF/cofilin proteins. Cell Motil Cytoskeleton. 2000;47(4):319–336. doi:10.1002/1097-0169(200012)47:4<319::Aid-cm6>3.0.Co;2-i
   PubMed Web of Science ®Google Scholar
• Yoo Y, Ho HJ, Wang C, Guan JL. Tyrosine phosphorylation of cofilin at Y68 by v-Src leads to its degradation through ubiquitin-proteasome pathway. Oncogene. 2010;29(2):263–272. doi:10.1038/onc.2009.319
   PubMed Web of Science ®Google Scholar
• Frantz C, Barreiro G, Dominguez L, et al. Cofilin is a pH sensor for actin free barbed end formation: role of phosphoinositide binding. J Cell Biol. 2008;183(5):865–879. doi:10.1083/jcb.200804161
   PubMed Web of Science ®Google Scholar
• Ishikawa-Ankerhold HC, Daszkiewicz W, Schleicher M, Müller-Taubenberger A. Actin-interacting protein 1 contributes to intranuclear rod assembly in dictyostelium discoideum. Sci Rep. 2017;7(1):40310. doi:10.1038/srep40310
   PubMed Web of Science ®Google Scholar
• Zhu Y, Xu Y, Chen T, et al. TSG101 promotes the proliferation, migration, and invasion of human glioma cells by regulating the AKT/GSK3β/β-catenin and RhoC/cofilin pathways. Mol Neurobiol. 2021;58(5):2118–2132. doi:10.1007/s12035-020-02231-7
   PubMed Web of Science ®Google Scholar
• Lee MH, Kundu JK, Chae JI, Shim JH. Targeting ROCK/LIMK/cofilin signaling pathway in cancer. Arch Pharm Res. 2019;42(6):481–491. doi:10.1007/s12272-019-01153-w
   PubMed Web of Science ®Google Scholar
• Sousa-Squiavinato ACM, Rocha MR, Barcellos-de-souza P, de Souza WF, Morgado-Diaz JA. Cofilin-1 signaling mediates epithelial-mesenchymal transition by promoting actin cytoskeleton reorganization and cell-cell adhesion regulation in colorectal cancer cells. Biochim Biophys Acta Mol Cell Res. 2019;1866(3):418–429. doi:10.1016/j.bbamcr.2018.10.003
   PubMed Web of Science ®Google Scholar
• Popow-Woźniak A, Mazur AJ, Mannherz HG, Malicka-Błaszkiewicz M, Nowak D. Cofilin overexpression affects actin cytoskeleton organization and migration of human colon adenocarcinoma cells. Histochem Cell Biol. 2012;138(5):725–736. doi:10.1007/s00418-012-0988-2
   PubMed Web of Science ®Google Scholar
• Wicki A, Lehembre F, Wick N, Hantusch B, Kerjaschki D, Christofori G. Tumor invasion in the absence of epithelial-mesenchymal transition: podoplanin-mediated remodeling of the actin cytoskeleton. Cancer Cell. 2006;9(4):261–272. doi:10.1016/j.ccr.2006.03.010
   PubMed Web of Science ®Google Scholar
• Yu X, Zech T, McDonald L, et al. N-WASP coordinates the delivery and F-actin-mediated capture of MT1-MMP at invasive pseudopods. J Cell Biol. 2012;199(3):527–544. doi:10.1083/jcb.201203025
   PubMed Web of Science ®Google Scholar
• Dalaka E, Kronenberg NM, Liehm P, Segall JE, Prystowsky MB, Gather MC. Direct measurement of vertical forces shows correlation between mechanical activity and proteolytic ability of invadopodia. Sci Adv. 2020;6(11):eaax6912. doi:10.1126/sciadv.aax6912
   PubMed Web of Science ®Google Scholar
• Ono S, Minami N, Abe H, Obinata T. Characterization of a novel cofilin isoform that is predominantly expressed in mammalian skeletal muscle. J Biol Chem. 1994;269(21):15280–15286.
   PubMed Web of Science ®Google Scholar
• Gillett GT, Fox MF, Rowe PS, Casimir CM, Povey S. Mapping of human non-muscle type cofilin (CFL1) to chromosome 11q13 and muscle-type cofilin (CFL2) to chromosome 14. Ann Hum Genet. 1996;60(3):201–211. doi:10.1111/j.1469-1809.1996.tb00423.x
   PubMed Web of Science ®Google Scholar
• Thirion C, Stucka R, Mendel B, et al. Characterization of human muscle type cofilin (CFL2) in normal and regenerating muscle. Eur J Biochem. 2001;268(12):3473–3482. doi:10.1046/j.1432-1327.2001.02247.x
   PubMedGoogle Scholar
• Goroncy AK, Koshiba S, Tochio N, et al. NMR solution structures of actin depolymerizing factor homology domains. Protein Sci. 2009;18(11):2384–2392. doi:10.1002/pro.248
   PubMed Web of Science ®Google Scholar
• Singh BK, Sattler JM, Chatterjee M, Huttu J, Schüler H, Kursula I. Crystal structures explain functional differences in the two actin depolymerization factors of the malaria parasite. J Biol Chem. 2011;286(32):28256–28264. doi:10.1074/jbc.M111.211730
   PubMed Web of Science ®Google Scholar
• Peitsch WK, Grund C, Kuhn C, et al. Drebrin is a widespread actin-associating protein enriched at junctional plaques, defining a specific microfilament Anchorage system in polar epithelial cells. Eur J Cell Biol. 1999;78(11):767–778. doi:10.1016/s0171-9335(99)80027-2
   PubMed Web of Science ®Google Scholar
• Lappalainen P, Kessels MM, Cope MJ, Drubin DG. The ADF homology (ADF-H) domain: a highly exploited actin-binding module. Mol Biol Cell. 1998;9(8):1951–1959. doi:10.1091/mbc.9.8.1951
   PubMed Web of Science ®Google Scholar
• Dos Remedios CG, Chhabra D, Kekic M, et al. Actin binding proteins: regulation of cytoskeletal microfilaments. Physiol Rev. 2003;83(2):433–473. doi:10.1152/physrev.00026.2002
   PubMed Web of Science ®Google Scholar
• Pope BJ, Zierler-Gould KM, Kühne R, Weeds AG, Ball LJ. Solution structure of human cofilin: actin binding, pH sensitivity, and relationship to actin-depolymerizing factor. J Biol Chem. 2004;279(6):4840–4848. doi:10.1074/jbc.M310148200
   PubMed Web of Science ®Google Scholar
• Van Troys M, Dewitte D, Verschelde JL, Goethals M, Vandekerckhove J, Ampe C. The competitive interaction of actin and PIP2 with actophorin is based on overlapping target sites: design of a gain-of-function mutant. Biochemistry. 2000;39(40):12181–12189. doi:10.1021/bi000816c
   PubMed Web of Science ®Google Scholar
• Wegner A. Treadmilling of actin at physiological salt concentrations. An analysis of the critical concentrations of actin filaments. J Mol Biol. 1982;161(4):607–615. doi:10.1016/0022-2836(82)90411-9
   PubMed Web of Science ®Google Scholar
• Neuhaus JM, Wanger M, Keiser T, Wegner A. Treadmilling of actin. J Muscle Res Cell Motil. 1983;4(5):507–527. doi:10.1007/bf00712112
   PubMed Web of Science ®Google Scholar
• Pollard TD, Borisy GG. Cellular motility driven by assembly and disassembly of actin filaments. Cell. 2003;112(4):453–465. doi:10.1016/s0092-8674(03)00120-x
   PubMed Web of Science ®Google Scholar
• Plastino J, Blanchoin L. Dynamic stability of the actin ecosystem. J Cell Sci. 2018;132(4). doi:10.1242/jcs.219832
   PubMed Web of Science ®Google Scholar
• Pollard TD, Cooper JA. Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation. Biochemistry. 1984;23(26):6631–6641. doi:10.1021/bi00321a054
   PubMed Web of Science ®Google Scholar
• Buracco S, Claydon S, Insall R. Control of actin dynamics during cell motility. F1000Res. 2019;8. doi:10.12688/f1000research.18669.1.
   PubMedGoogle Scholar
• Pollard TD. Regulation of actin filament assembly by Arp2/3 complex and formins. Annu Rev Biophys Biomol Struct. 2007;36:451–477. doi:10.1146/annurev.biophys.35.040405.101936
   PubMedGoogle Scholar
• Van Troys M, Huyck L, Leyman S, Dhaese S, Vandekerkhove J, Ampe C. Ins and outs of ADF/cofilin activity and regulation. Eur J Cell Biol. 2008;87(8–9):649–667. doi:10.1016/j.ejcb.2008.04.001
   PubMed Web of Science ®Google Scholar
• Kueh HY, Brieher WM, Mitchison TJ. Dynamic stabilization of actin filaments. Proc Natl Acad Sci USA. 2008;105(43):16531–16536. doi:10.1073/pnas.0807394105
   PubMed Web of Science ®Google Scholar
• Rotty JD, Wu C, Haynes EM, et al. Profilin-1 serves as a gatekeeper for actin assembly by Arp2/3-dependent and -independent pathways. Dev Cell. 2015;32(1):54–67. doi:10.1016/j.devcel.2014.10.026
   PubMed Web of Science ®Google Scholar
• Pollard TD. Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments. J Cell Biol. 1986;103(6 Pt 2):2747–2754. doi:10.1083/jcb.103.6.2747
   PubMed Web of Science ®Google Scholar
• Fujiwara I, Takahashi S, Tadakuma H, Funatsu T, Ishiwata S. Microscopic analysis of polymerization dynamics with individual actin filaments. Nat Cell Biol. 2002;4(9):666–673. doi:10.1038/ncb841
   PubMed Web of Science ®Google Scholar
• Wang R, Carlsson AE. How capping protein enhances actin filament growth and nucleation on biomimetic beads. Phys Biol. 2015;12(6):066008. doi:10.1088/1478-3975/12/6/066008
   PubMed Web of Science ®Google Scholar
• Roland J, Berro J, Michelot A, Blanchoin L, Martiel JL. Stochastic severing of actin filaments by actin depolymerizing factor/cofilin controls the emergence of a steady dynamical regime. Biophys J. 2008;94(6):2082–2094. doi:10.1529/biophysj.107.121988
   PubMed Web of Science ®Google Scholar
• McGough A, Pope B, Chiu W, Weeds A. Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function. J Cell Biol. 1997;138(4):771–781. doi:10.1083/jcb.138.4.771
   PubMed Web of Science ®Google Scholar
• Blanchoin L, Pollard TD, Mullins RD. Interactions of ADF/cofilin, Arp2/3 complex, capping protein and profilin in remodeling of branched actin filament networks. Curr Biol. 2000;10(20):1273–1282. doi:10.1016/s0960-9822(00)00749-1
   PubMed Web of Science ®Google Scholar
• Bernstein BW, Bamburg JR. ADF/cofilin: a functional node in cell biology. Trends Cell Biol. 2010;20(4):187–195. doi:10.1016/j.tcb.2010.01.001
   PubMed Web of Science ®Google Scholar
• Rosenblatt J, Peluso P, Mitchison TJ. The bulk of unpolymerized actin in Xenopus egg extracts is ATP-bound. Mol Biol Cell. 1995;6(2):227–236. doi:10.1091/mbc.6.2.227
   PubMed Web of Science ®Google Scholar
• Sept D, McCammon JA. Thermodynamics and kinetics of actin filament nucleation. Biophys J. 2001;81(2):667–674. doi:10.1016/s0006-3495(01)75731-1
   PubMed Web of Science ®Google Scholar
• Fedorov AA, Lappalainen P, Fedorov EV, Drubin DG, Almo SC. Structure determination of yeast cofilin. Nat Struct Biol. 1997;4(5):366–369. doi:10.1038/nsb0597-366
   PubMedGoogle Scholar
• Pope BJ, Gonsior SM, Yeoh S, McGough A, Weeds AG. Uncoupling actin filament fragmentation by cofilin from increased subunit turnover. J Mol Biol. 2000;298(4):649–661. doi:10.1006/jmbi.2000.3688
   PubMed Web of Science ®Google Scholar
• Andrianantoandro E, Pollard TD. Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin. Mol Cell. 2006;24(1):13–23. doi:10.1016/j.molcel.2006.08.006
   PubMed Web of Science ®Google Scholar
• Bamburg JR, Bernstein BW. ADF/cofilin. Curr Biol. 2008;18(7):R273–5. doi:10.1016/j.cub.2008.02.002
   PubMed Web of Science ®Google Scholar
• Agnew BJ, Minamide LS, Bamburg JR. Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site. J Biol Chem. 1995;270(29):17582–17587. doi:10.1074/jbc.270.29.17582
   PubMed Web of Science ®Google Scholar
• Kanellos G, Frame MC. Cellular functions of the ADF/cofilin family at a glance. J Cell Sci. 2016;129(17):3211–3218. doi:10.1242/jcs.187849
   PubMed Web of Science ®Google Scholar
• Arber S, Barbayannis FA, Hanser H, et al. Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase. Nature. 1998;393(6687):805–809. doi:10.1038/31729
   PubMed Web of Science ®Google Scholar
• Yang N, Higuchi O, Ohashi K, et al. Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization. Nature. 1998;393(6687):809–812. doi:10.1038/31735
   PubMed Web of Science ®Google Scholar
• Toshima J, Toshima JY, 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. 2001;276(33):31449–31458. doi:10.1074/jbc.M102988200
   PubMed Web of Science ®Google Scholar
• Scott RW, Olson MF. LIM kinases: function, regulation and association with human disease. J Mol Med (Berl). 2007;85(6):555–568. doi:10.1007/s00109-007-0165-6
   PubMed Web of Science ®Google Scholar
• Po’uha ST, Shum MS, Goebel A, Bernard O, Kavallaris M. LIM-kinase 2, a regulator of actin dynamics, is involved in mitotic spindle integrity and sensitivity to microtubule-destabilizing drugs. Oncogene. 2010;29(4):597–607. doi:10.1038/onc.2009.367
   PubMed Web of Science ®Google Scholar
• Hamill S, Lou HJ, Turk BE, Boggon TJ. Structural basis for noncanonical substrate recognition of Cofilin/ADF proteins by LIM kinases. Mol Cell. 2016;62(3):397–408. doi:10.1016/j.molcel.2016.04.001
   PubMed Web of Science ®Google Scholar
• Maekawa M, Ishizaki T, Boku S, et al. Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase. Science. 1999;285(5429):895–898. doi:10.1126/science.285.5429.895
   PubMed Web of Science ®Google Scholar
• Edwards DC, Sanders LC, Bokoch GM, Gill GN. Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Nat Cell Biol. 1999;1(5):253–259. doi:10.1038/12963
   PubMed Web of Science ®Google Scholar
• Amano T, Tanabe K, Eto T, Narumiya S, Mizuno K. LIM-kinase 2 induces formation of stress fibres, focal adhesions and membrane blebs, dependent on its activation by Rho-associated kinase-catalysed phosphorylation at threonine-505. Biochem J. 2001;354(Pt 1):149–159. doi:10.1042/0264-6021:
   PubMedGoogle Scholar
• Sumi T, Matsumoto K, Nakamura T. Specific activation of LIM kinase 2 via phosphorylation of threonine 505 by ROCK, a Rho-dependent protein kinase. J Biol Chem. 2001;276(1):670–676. doi:10.1074/jbc.M007074200
   PubMed Web of Science ®Google Scholar
• Ahmed T, Shea K, Masters JR, Jones GE, Wells CM. A PAK4-LIMK1 pathway drives prostate cancer cell migration downstream of HGF. Cell Signal. 2008;20(7):1320–1328. doi:10.1016/j.cellsig.2008.02.021
   PubMed Web of Science ®Google Scholar
• Sumi T, Matsumoto K, Shibuya A, Nakamura T. Activation of LIM kinases by myotonic dystrophy kinase-related Cdc42-binding kinase alpha. J Biol Chem. 2001;276(25):23092–23096. doi:10.1074/jbc.C100196200
   PubMed Web of Science ®Google Scholar
• Ohashi K, Nagata K, Maekawa M, Ishizaki T, Narumiya S, Mizuno K. Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop. J Biol Chem. 2000;275(5):3577–3582. doi:10.1074/jbc.275.5.3577
   PubMed Web of Science ®Google Scholar
• Foletta VC, Lim MA, Soosairajah J, et al. Direct signaling by the BMP type II receptor via the cytoskeletal regulator LIMK1. J Cell Biol. 2003;162(6):1089–1098. doi:10.1083/jcb.200212060
   PubMed Web of Science ®Google Scholar
• Schlau M, Terheyden-Keighley D, Theis V, Mannherz HG, Theiss C. VEGF triggers the activation of cofilin and the Arp2/3 complex within the growth cone. Int J Mol Sci. 2018;19(2). doi:10.3390/ijms19020384
   PubMed Web of Science ®Google Scholar
• Song IS, Kang SS, Kim ES, et al. Heat shock protein 27 phosphorylation is involved in epithelial cell apoptosis as well as epithelial migration during corneal epithelial wound healing. Exp Eye Res. 2014;118:36–41. doi:10.1016/j.exer.2013.11.002
   PubMed Web of Science ®Google Scholar
• Pandey D, Goyal P, Siess W. Lysophosphatidic acid stimulation of platelets rapidly induces Ca2+-dependent dephosphorylation of cofilin that is independent of dense granule secretion and aggregation. Blood Cells Mol Dis. 2007;38(3):269–279. doi:10.1016/j.bcmd.2007.01.002
   PubMed Web of Science ®Google Scholar
• Reschke CR, Silva LFA, Vangoor VR, et al. Systemic delivery of antagomirs during blood-brain barrier disruption is disease-modifying in experimental epilepsy. Mol Ther. 2021;29(6):2041–2052. doi:10.1016/j.ymthe.2021.02.021
   PubMed Web of Science ®Google Scholar
• Castañeda P, Muñoz M, García-Rojo G, et al. Association of N-cadherin levels and downstream effectors of Rho GTPases with dendritic spine loss induced by chronic stress in rat hippocampal neurons. J Neurosci Res. 2015;93(10):1476–1491. doi:10.1002/jnr.23602
   PubMed Web of Science ®Google Scholar
• Toshima J, Toshima JY, Amano T, Yang N, Narumiya S, Mizuno K. Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation. Mol Biol Cell. 2001;12(4):1131–1145. doi:10.1091/mbc.12.4.1131
   PubMed Web of Science ®Google Scholar
• Huang TY, DerMardirossian C, Bokoch GM. Cofilin phosphatases and regulation of actin dynamics. Curr Opin Cell Biol. 2006;18(1):26–31. doi:10.1016/j.ceb.2005.11.005
   PubMed Web of Science ®Google Scholar
• 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. 2002;108(2):233–246. doi:10.1016/s0092-8674(01)00638-9
   PubMed Web of Science ®Google Scholar
• Ohta Y, Kousaka K, Nagata-Ohashi K, et al. Differential activities, subcellular distribution and tissue expression patterns of three members of Slingshot family phosphatases that dephosphorylate cofilin. Genes Cells. 2003;8(10):811–824. doi:10.1046/j.1365-2443.2003.00678.x
   PubMed Web of Science ®Google Scholar
• Soosairajah J, Maiti S, Wiggan O, et al. Interplay between components of a novel LIM kinase-slingshot phosphatase complex regulates cofilin. EMBO j. 2005;24(3):473–486. doi:10.1038/sj.emboj.7600543
   PubMed Web of Science ®Google Scholar
• Kurita S, Gunji E, Ohashi K, Mizuno K. Actin filaments-stabilizing and -bundling activities of cofilin-phosphatase Slingshot-1. Genes Cells. 2007;12(5):663–676. doi:10.1111/j.1365-2443.2007.01078.x
   PubMed Web of Science ®Google Scholar
• Yamamoto M, Nagata-Ohashi K, Ohta Y, Ohashi K, Mizuno K. Identification of multiple actin-binding sites in cofilin-phosphatase Slingshot-1L. FEBS Lett. 2006;580(7):1789–1794. doi:10.1016/j.febslet.2006.02.034
   PubMed Web of Science ®Google Scholar
• Kurita S, Watanabe Y, Gunji E, Ohashi K, Mizuno K. Molecular dissection of the mechanisms of substrate recognition and F-actin-mediated activation of cofilin-phosphatase Slingshot-1. J Biol Chem. 2008;283(47):32542–32552. doi:10.1074/jbc.M804627200
   PubMed Web of Science ®Google Scholar
• Mizuno K. Signaling mechanisms and functional roles of cofilin phosphorylation and dephosphorylation. Cell Signal. 2013;25(2):457–469. doi:10.1016/j.cellsig.2012.11.001
   PubMed Web of Science ®Google Scholar
• 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. 2002;12(1):79–84. doi:10.1016/s0960-9822(01)00629-7
   PubMed Web of Science ®Google Scholar
• Orlova A, Shvetsov A, Galkin VE, et al. Actin-destabilizing factors disrupt filaments by means of a time reversal of polymerization. Proc Natl Acad Sci U S A. 2004;101(51):17664–17668. doi:10.1073/pnas.0407525102
   PubMed Web of Science ®Google Scholar
• Bobkov AA, Muhlrad A, Pavlov DA, Kokabi K, Yilmaz A, Reisler E. Cooperative effects of cofilin (ADF) on actin structure suggest allosteric mechanism of cofilin function. J Mol Biol. 2006;356(2):325–334. doi:10.1016/j.jmb.2005.11.072
   PubMed Web of Science ®Google Scholar
• Chan C, Beltzner CC, Pollard TD. Cofilin dissociates Arp2/3 complex and branches from actin filaments. Curr Biol. 2009;19(7):537–545. doi:10.1016/j.cub.2009.02.060
   PubMed Web of Science ®Google Scholar
• Minamide LS, Striegl AM, Boyle JA, Meberg PJ, Bamburg JR. Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function. Nat Cell Biol. 2000;2(9):628–636. doi:10.1038/35023579
   PubMed Web of Science ®Google Scholar
• Park JB, Agnihotri S, Golbourn B, et al. Transcriptional profiling of GBM invasion genes identifies effective inhibitors of the LIM kinase-Cofilin pathway. Oncotarget. 2014;5(19):9382–9395. doi:10.18632/oncotarget.2412
   PubMedGoogle Scholar
• Liu W, Zhang Q, Tang Q, et al. Lycorine inhibits cell proliferation and migration by inhibiting ROCK1/cofilin‑induced actin dynamics in HepG2 hepatoblastoma cells. Oncol Rep. 2018;40(4):2298–2306. doi:10.3892/or.2018.6609
   PubMed Web of Science ®Google Scholar
• Wei R, Zhang Y, Shen L, et al. Comparative proteomic and radiobiological analyses in human lung adenocarcinoma cells. Mol Cell Biochem. 2012;359(1–2):151–159. doi:10.1007/s11010-011-1008-x
   PubMed Web of Science ®Google Scholar
• Collazo J, Zhu B, Larkin S, et al. Cofilin drives cell-invasive and metastatic responses to TGF-β in prostate cancer. Cancer Res. 2014;74(8):2362–2373. doi:10.1158/0008-5472.Can-13-3058
   PubMed Web of Science ®Google Scholar
• Maimaiti Y, Tan J, Liu Z, et al. Overexpression of cofilin correlates with poor survival in breast cancer: a tissue microarray analysis. Oncol Lett. 2017;14(2):2288–2294. doi:10.3892/ol.2017.6413
   PubMed Web of Science ®Google Scholar
• Lu LI, Fu NI, Luo XU, Li XY, Li XP. Overexpression of cofilin 1 in prostate cancer and the corresponding clinical implications. Oncol Lett. 2015;9(6):2757–2761. doi:10.3892/ol.2015.3133
   PubMed Web of Science ®Google Scholar
• Zhang Y, Tong X. Expression of the actin-binding proteins indicates that cofilin and fascin are related to breast tumour size. J Int Med Res. 2010;38(3):1042–1048. doi:10.1177/147323001003800331
   PubMed Web of Science ®Google Scholar
• Wu Q, Jiang Y, Cui S, Wang Y, Wu X. The role of cofilin-l in vulvar squamous cell carcinoma: a marker of carcinogenesis, progression and targeted therapy. Oncol Rep. 2016;35(5):2743–2754. doi:10.3892/or.2016.4625
   PubMed Web of Science ®Google Scholar
• Satoh M, Takano S, Sogawa K, et al. Immune-complex level of cofilin-1 in sera is associated with cancer progression and poor prognosis in pancreatic cancer. Cancer Sci. 2017;108(4):795–803. doi:10.1111/cas.13181
   PubMed Web of Science ®Google Scholar
• Sun W, Yan H, Qian C, et al. Cofilin-1 and phosphoglycerate kinase 1 as promising indicators for glioma radiosensibility and prognosis. Oncotarget. 2017;8(33):55073–55083. doi:10.18632/oncotarget.19025
   PubMedGoogle Scholar
• Xu H, Chen Y, Tan C, et al. High expression of WDR1 in primary glioblastoma is associated with poor prognosis. Am J Transl Res. 2016;8(2):1253–1264.
   PubMed Web of Science ®Google Scholar
• Erkutlu I, Cigiloglu A, Kalender ME, et al. Correlation between Rho-kinase pathway gene expressions and development and progression of glioblastoma multiforme. Tumour Biol. 2013;34(2):1139–1144. doi:10.1007/s13277-013-0655-9
   PubMedGoogle Scholar
• Tang Z, Araysi LM, Fathallah-Shaykh HM. c-Src and neural Wiskott-Aldrich syndrome protein (N-WASP) promote low oxygen-induced accelerated brain invasion by gliomas. PLoS One. 2013;8(9):e75436. doi:10.1371/journal.pone.0075436
   PubMed Web of Science ®Google Scholar
• Yan H, Yang K, Xiao H, Zou YJ, Zhang WB, Liu HY. Over-expression of cofilin-1 and phosphoglycerate kinase 1 in astrocytomas involved in pathogenesis of radioresistance. CNS Neurosci Ther. 2012;18(9):729–736. doi:10.1111/j.1755-5949.2012.00353.x
   PubMed Web of Science ®Google Scholar
• Yang ZL, Miao X, Xiong L, et al. CFL1 and Arp3 are biomarkers for metastasis and poor prognosis of squamous cell/adenosquamous carcinomas and adenocarcinomas of gallbladder. Cancer Invest. 2013;31(2):132–139. doi:10.3109/07357907.2012.756113
   PubMed Web of Science ®Google Scholar
• Tsai CH, Lin LT, Wang CY, et al. Over-expression of cofilin-1 suppressed growth and invasion of cancer cells is associated with up-regulation of let-7 microRNA. Biochim Biophys Acta. 2015;1852(5):851–861. doi:10.1016/j.bbadis.2015.01.007
   PubMed Web of Science ®Google Scholar
• Chung H, Kim B, Jung SH, et al. Does phosphorylation of cofilin affect the progression of human bladder cancer? BMC Cancer. 2013;13(1):45. doi:10.1186/1471-2407-13-45
   PubMed Web of Science ®Google Scholar
• Zheng Y, Fang Y, Li S, Zheng B. 血浆cofilin蛋白检测在肺癌诊断中的价值. 南方医科大学学报 [Detection of plasma cofilin protein for diagnosis of lung cancer]. Nan Fang Yi Ke Da Xue Xue Bao. 2013;33(10):1551–1553. Chinese
   PubMedGoogle Scholar
• Becker M, De Bastiani MA, Müller CB, Markoski MM, Castro MA, Klamt F. High cofilin-1 levels correlate with cisplatin resistance in lung adenocarcinomas. Tumour Biol. 2014;35(2):1233–1238. doi:10.1007/s13277-013-1164-6
   PubMedGoogle Scholar
• Ding SJ, Li Y, Shao XX, et al. Proteome analysis of hepatocellular carcinoma cell strains, MHCC97-H and MHCC97-L, with different metastasis potentials. Proteomics. 2004;4(4):982–994. doi:10.1002/pmic.200300653
   PubMed Web of Science ®Google Scholar
• Yamaguchi H, Condeelis J. Regulation of the actin cytoskeleton in cancer cell migration and invasion. Biochim Biophys Acta. 2007;1773(5):642–652. doi:10.1016/j.bbamcr.2006.07.001
   PubMed Web of Science ®Google Scholar
• Yamaguchi H, Lorenz M, Kempiak S, et al. Molecular mechanisms of invadopodium formation: the role of the N-WASP-Arp2/3 complex pathway and cofilin. J Cell Biol. 2005;168(3):441–452. doi:10.1083/jcb.200407076
   PubMed Web of Science ®Google Scholar
• Yap CT, Simpson TI, Pratt T, Price DJ, Maciver SK. The motility of glioblastoma tumour cells is modulated by intracellular cofilin expression in a concentration-dependent manner. Cell Motil Cytoskeleton. 2005;60(3):153–165. doi:10.1002/cm.20053
   PubMed Web of Science ®Google Scholar
• Bisi S, Disanza A, Malinverno C, Frittoli E, Palamidessi A, Scita G. Membrane and actin dynamics interplay at lamellipodia leading edge. Curr Opin Cell Biol. 2013;25(5):565–573. doi:10.1016/j.ceb.2013.04.001
   PubMed Web of Science ®Google Scholar
• Ideses Y, Brill-Karniely Y, Haviv L, Ben-Shaul A, Bernheim-Groswasser A. Arp2/3 branched actin network mediates filopodia-like bundles formation in vitro. PLoS One. 2008;3(9):e3297. doi:10.1371/journal.pone.0003297
   PubMed Web of Science ®Google Scholar
• Kiuchi T, Nagai T, Ohashi K, Mizuno K. Measurements of spatiotemporal changes in G-actin concentration reveal its effect on stimulus-induced actin assembly and lamellipodium extension. J Cell Biol. 2011;193(2):365–380. doi:10.1083/jcb.201101035
   PubMed Web of Science ®Google Scholar
• Shishkin S, Eremina L, Pashintseva N, Kovalev L, Kovaleva M. Cofilin-1 and other ADF/cofilin superfamily members in human malignant cells. Int J Mol Sci. 2016;18(1):10. doi:10.3390/ijms18010010
   PubMed Web of Science ®Google Scholar
• Ghosh M, Ichetovkin I, Song X, Condeelis JS, Lawrence DS. A new strategy for caging proteins regulated by kinases. J Am Chem Soc. 2002;124(11):2440–2441. doi:10.1021/ja017592l
   PubMed Web of Science ®Google Scholar
• Delorme V, Machacek M, DerMardirossian C, et al. Cofilin activity downstream of Pak1 regulates cell protrusion efficiency by organizing lamellipodium and lamella actin networks. Dev Cell. 2007;13(5):646–662. doi:10.1016/j.devcel.2007.08.011
   PubMed Web of Science ®Google Scholar
• Hoffmann L, Rust MB, Culmsee C. Actin(g) on mitochondria - A role for cofilin1 in neuronal cell death pathways. Biol Chem. 2019;400(9):1089–1097. doi:10.1515/hsz-2019-0120
   PubMed Web of Science ®Google Scholar
• Mardilovich K, Gabrielsen M, McGarry L, et al. Elevated LIM kinase 1 in nonmetastatic prostate cancer reflects its role in facilitating androgen receptor nuclear translocation. Mol Cancer Ther. 2015;14(1):246–258. doi:10.1158/1535-7163.Mct-14-0447
   PubMed Web of Science ®Google Scholar
• Yoshioka K, Foletta V, Bernard O, Itoh K. A role for LIM kinase in cancer invasion. Proc Natl Acad Sci U S A. 2003;100(12):7247–7252. doi:10.1073/pnas.1232344100
   PubMed Web of Science ®Google Scholar
• Manetti F. Recent findings confirm LIM domain kinases as emerging target candidates for cancer therapy. Curr Cancer Drug Targets. 2012;12(5):543–560. doi:10.2174/156800912800673266
   PubMed Web of Science ®Google Scholar
• Zhang W, Gan N, Zhou J. Immunohistochemical investigation of the correlation between LIM kinase 1 expression and development and progression of human ovarian carcinoma. J Int Med Res. 2012;40(3):1067–1073. doi:10.1177/147323001204000325
   PubMed Web of Science ®Google Scholar
• Guo H, Gu F, Li W, et al. Reduction of protein kinase C zeta inhibits migration and invasion of human glioblastoma cells. J Neurochem. 2009;109(1):203–213. doi:10.1111/j.1471-4159.2009.05946.x
   PubMed Web of Science ®Google Scholar
• Ma Y, Wang B, Li W, et al. Intersectin1-s is involved in migration and invasion of human glioma cells. J Neurosci Res. 2011;89(7):1079–1090. doi:10.1002/jnr.22616
   PubMed Web of Science ®Google Scholar
• Scott RW, Hooper S, Crighton D, et al. LIM kinases are required for invasive path generation by tumor and tumor-associated stromal cells. J Cell Biol. 2010;191(1):169–185. doi:10.1083/jcb.201002041
   PubMed Web of Science ®Google Scholar
• Choi JA, Lim IK. TIS21/BTG2 inhibits invadopodia formation by downregulating reactive oxygen species level in MDA-MB-231 cells. J Cancer Res Clin Oncol. 2013;139(10):1657–1665. doi:10.1007/s00432-013-1484-3
   PubMed Web of Science ®Google Scholar
• Aung A, Seo YN, Lu S, et al. 3D traction stresses activate protease-dependent invasion of cancer cells. Biophys J. 2014;107(11):2528–2537. doi:10.1016/j.bpj.2014.07.078
   PubMed Web of Science ®Google Scholar
• Kłopocka W, Korczyński J, Pomorski P. Cytoskeleton and nucleotide signaling in glioma C6 cells. Adv Exp Med Biol. 2020;1202:109–128. doi:10.1007/978-3-030-30651-9_6
   PubMed Web of Science ®Google Scholar
• Jin SG, Ryu HH, Li SY, et al. Nogo-A inhibits the migration and invasion of human malignant glioma U87MG cells. Oncol Rep. 2016;35(6):3395–3402. doi:10.3892/or.2016.4737
   PubMed Web of Science ®Google Scholar
• Schiapparelli P, Guerrero-Cazares H, Magaña-Maldonado R, et al. NKCC1 regulates migration ability of glioblastoma cells by modulation of actin dynamics and interacting with cofilin. EBioMedicine. 2017;21:94–103. doi:10.1016/j.ebiom.2017.06.020
   PubMed Web of Science ®Google Scholar
• Zhao K, Wang L, Li T, et al. The role of miR-451 in the switching between proliferation and migration in malignant glioma cells: AMPK signaling, mTOR modulation and Rac1 activation required. Int J Oncol. 2017;50(6):1989–1999. doi:10.3892/ijo.2017.3973
   PubMed Web of Science ®Google Scholar
• Glogowska A, Thanasupawat T, Beiko J, Pitz M, Hombach-Klonisch S, Klonisch T. Novel CTRP8-RXFP1-JAK3-STAT3 axis promotes Cdc42-dependent actin remodeling for enhanced filopodia formation and motility in human glioblastoma cells. Mol Oncol. 2022;16(2):368–387. doi:10.1002/1878-0261.12981
   PubMed Web of Science ®Google Scholar
• Shi C, Ren L, Sun C, et al. miR-29a/b/c function as invasion suppressors for gliomas by targeting CDC42 and predict the prognosis of patients. Br J Cancer. 2017;117(7):1036–1047. doi:10.1038/bjc.2017.255
   PubMed Web of Science ®Google Scholar
• Hou M, Liu X, Cao J, Chen B. SEPT7 overexpression inhibits glioma cell migration by targeting the actin cytoskeleton pathway. Oncol Rep. 2016;35(4):2003–2010. doi:10.3892/or.2016.4609
   PubMed Web of Science ®Google Scholar
• Zhang B, Gu F, She C, et al. Reduction of Akt2 inhibits migration and invasion of glioma cells. Int J Cancer. 2009;125(3):585–595. doi:10.1002/ijc.24314
   PubMed Web of Science ®Google Scholar
• Schulze M, Fedorchenko O, Zink TG, et al. Chronophin is a glial tumor modifier involved in the regulation of glioblastoma growth and invasiveness. Oncogene. 2016;35(24):3163–3177. doi:10.1038/onc.2015.376
   PubMed Web of Science ®Google Scholar
• Schulze M, Hutterer M, Sabo A, et al. Chronophin regulates active vitamin B6 levels and transcriptomic features of glioblastoma cell lines cultured under non-adherent, serum-free conditions. BMC Cancer. 2018;18(1):524. doi:10.1186/s12885-018-4440-4
   PubMed Web of Science ®Google Scholar
• Gondi CS, Kandhukuri N, Kondraganti S, et al. Down-regulation of uPAR and cathepsin B retards cofilin dephosphorylation. Int J Oncol. 2006;28(3):633–639.
   PubMed Web of Science ®Google Scholar
• Piña-Medina AG, Hansberg-Pastor V, González-Arenas A, Cerbón M, Camacho-Arroyo I. Progesterone promotes cell migration, invasion and cofilin activation in human astrocytoma cells. Steroids. 2016;105:19–25. doi:10.1016/j.steroids.2015.11.008
   PubMed Web of Science ®Google Scholar
• Sun J, He D, Fu Y, et al. A novel lncRNA ARST represses glioma progression by inhibiting ALDOA-mediated actin cytoskeleton integrity. J Exp Clin Cancer Res. 2021;40(1):187. doi:10.1186/s13046-021-01977-9
   PubMed Web of Science ®Google Scholar
• Peterburs P, Heering J, Link G, Pfizenmaier K, Olayioye MA, Hausser A. Protein kinase D regulates cell migration by direct phosphorylation of the cofilin phosphatase slingshot 1 like. Cancer Res. 2009;69(14):5634–5638. doi:10.1158/0008-5472.Can-09-0718
   PubMed Web of Science ®Google Scholar
• Zhuang H, Li Q, Zhang X, et al. Downregulation of glycine decarboxylase enhanced cofilin-mediated migration in hepatocellular carcinoma cells. Free Radic Biol Med. 2018;120:1–12. doi:10.1016/j.freeradbiomed.2018.03.003
   PubMed Web of Science ®Google Scholar
• Takahashi K, Okabe H, Kanno SI, Nagai T, Mizuno K. A pleckstrin homology-like domain is critical for F-actin binding and cofilin-phosphatase activity of Slingshot-1. Biochem Biophys Res Commun. 2017;482(4):686–692. doi:10.1016/j.bbrc.2016.11.095
   PubMed Web of Science ®Google Scholar
• Hayakawa K, Tatsumi H, Sokabe M. Actin filaments function as a tension sensor by tension-dependent binding of cofilin to the filament. J Cell Biol. 2011;195(5):721–727. doi:10.1083/jcb.201102039
   PubMed Web of Science ®Google Scholar
• Matsushita S, Inoue Y, Hojo M, Sokabe M, Adachi T. Effect of tensile force on the mechanical behavior of actin filaments. J Biomech. 2011;44(9):1776–1781. doi:10.1016/j.jbiomech.2011.04.012
   PubMed Web of Science ®Google Scholar
• Pastushenko I, Blanpain C. EMT transition states during tumor progression and metastasis. Trends Cell Biol. 2019;29(3):212–226. doi:10.1016/j.tcb.2018.12.001
   PubMed Web of Science ®Google Scholar
• Kalluri R, Weinberg RA. The basics of epithelial-mesenchymal transition. J Clin Invest. 2009;119(6):1420–1428. doi:10.1172/jci39104
   PubMed Web of Science ®Google Scholar
• Lamouille S, Xu J, Derynck R. Molecular mechanisms of epithelial-mesenchymal transition. Nat Rev Mol Cell Biol. 2014;15(3):178–196. doi:10.1038/nrm3758
   PubMed Web of Science ®Google Scholar
• Aiello NM, Maddipati R, Norgard RJ, et al. EMT subtype influences epithelial plasticity and mode of cell migration. Dev Cell. 2018;45(6):681–95.e4. doi:10.1016/j.devcel.2018.05.027
   PubMed Web of Science ®Google Scholar
• Cervantes-Arias A, Pang LY, Argyle DJ. Epithelial-mesenchymal transition as a fundamental mechanism underlying the cancer phenotype. Vet Comp Oncol. 2013;11(3):169–184. doi:10.1111/j.1476-5829.2011.00313.x
   PubMed Web of Science ®Google Scholar
• Kahlert UD, Nikkhah G, Maciaczyk J. Epithelial-to-mesenchymal(-like) transition as a relevant molecular event in malignant gliomas. Cancer Lett. 2013;331(2):131–138. doi:10.1016/j.canlet.2012.12.010
   PubMed Web of Science ®Google Scholar
• Tso CL, Shintaku P, Chen J, et al. Primary glioblastomas express mesenchymal stem-like properties. Mol Cancer Res. 2006;4(9):607–619. doi:10.1158/1541-7786.Mcr-06-0005
   PubMed Web of Science ®Google Scholar
• Iser IC, Pereira MB, Lenz G, Wink MR. The epithelial-to-mesenchymal transition-like process in glioblastoma: an updated systematic review and in silico investigation. Med Res Rev. 2017;37(2):271–313. doi:10.1002/med.21408
   PubMed Web of Science ®Google Scholar
• Lewis-Tuffin LJ, Rodriguez F, Giannini C, et al. Misregulated E-cadherin expression associated with an aggressive brain tumor phenotype. PLoS One. 2010;5(10):e13665. doi:10.1371/journal.pone.0013665
   PubMed Web of Science ®Google Scholar
• Mikheeva SA, Mikheev AM, Petit A, et al. TWIST1 promotes invasion through mesenchymal change in human glioblastoma. Mol Cancer. 2010;9:194. doi:10.1186/1476-4598-9-194
   PubMed Web of Science ®Google Scholar
• Yadav AK, Desai NS. Cancer stem cells: acquisition, characteristics, therapeutic implications, targeting strategies and future prospects. Stem Cell Rev Rep. 2019;15(3):331–355. doi:10.1007/s12015-019-09887-2
   PubMed Web of Science ®Google Scholar
• Lau EY, Ho NP, Lee TK. Cancer stem cells and their microenvironment: biology and therapeutic implications. Stem Cells Int. 2017;2017:3714190. doi:10.1155/2017/3714190
   PubMed Web of Science ®Google Scholar
• Mani SA, Guo W, Liao MJ, et al. The epithelial-mesenchymal transition generates cells with properties of stem cells. Cell. 2008;133(4):704–715. doi:10.1016/j.cell.2008.03.027
   PubMed Web of Science ®Google Scholar
• Gupta PB, Onder TT, Jiang G, et al. Identification of selective inhibitors of cancer stem cells by high-throughput screening. Cell. 2009;138(4):645–659. doi:10.1016/j.cell.2009.06.034
   PubMed Web of Science ®Google Scholar
• Lee KH, Ahn EJ, Oh SJ, et al. KITENIN promotes glioma invasiveness and progression, associated with the induction of EMT and stemness markers. Oncotarget. 2015;6(5):3240–3253. doi:10.18632/oncotarget.3087
   PubMedGoogle Scholar
• Zhang XH, Qian Y, Li Z, Zhang NN, Xie YJ. Let-7g-5p inhibits epithelial-mesenchymal transition consistent with reduction of glioma stem cell phenotypes by targeting VSIG4 in glioblastoma. Oncol Rep. 2016;36(5):2967–2975. doi:10.3892/or.2016.5098
   PubMed Web of Science ®Google Scholar
• Zhu T, Li X, Luo L, et al. Reversion of malignant phenotypes of human glioblastoma cells by β-elemene through β-catenin-mediated regulation of stemness-, differentiation- and epithelial-to-mesenchymal transition-related molecules. J Transl Med. 2015;13(1):356. doi:10.1186/s12967-015-0727-2
   PubMed Web of Science ®Google Scholar
• Tania M, Khan MA, Fu J. Epithelial to mesenchymal transition inducing transcription factors and metastatic cancer. Tumour Biol. 2014;35(8):7335–7342. doi:10.1007/s13277-014-2163-y
   PubMedGoogle Scholar
• Derynck R, Muthusamy BP, Saeteurn KY. Signaling pathway cooperation in TGF-β-induced epithelial-mesenchymal transition. Curr Opin Cell Biol. 2014;31:56–66. doi:10.1016/j.ceb.2014.09.001
   PubMed Web of Science ®Google Scholar
• Xu Z, Gu C, Yao X, et al. CD73 promotes tumor metastasis by modulating RICS/RhoA signaling and EMT in gastric cancer. Cell Death Dis. 2020;11(3):202. doi:10.1038/s41419-020-2403-6
   PubMed Web of Science ®Google Scholar
• Islam SU, Ahmed MB, Lee SJ, et al. PRP4 kinase induces actin rearrangement and epithelial-mesenchymal transition through modulation of the actin-binding protein cofilin. Exp Cell Res. 2018;369(1):158–165. doi:10.1016/j.yexcr.2018.05.018
   PubMed Web of Science ®Google Scholar
• Häcker G. The morphology of apoptosis. Cell Tissue Res. 2000;301(1):5–17. doi:10.1007/s004410000193
   PubMed Web of Science ®Google Scholar
• Nijhawan D, Honarpour N, Wang X. Apoptosis in neural development and disease. Annu Rev Neurosci. 2000;23(1):73–87. doi:10.1146/annurev.neuro.23.1.73
   PubMed Web of Science ®Google Scholar
• Pistritto G, Trisciuoglio D, Ceci C, Garufi A, D’Orazi G. Apoptosis as anticancer mechanism: function and dysfunction of its modulators and targeted therapeutic strategies. Aging. 2016;8(4):603–619. doi:10.18632/aging.100934
   PubMedGoogle Scholar
• Igney FH, Krammer PH. Death and anti-death: tumour resistance to apoptosis. Nat Rev Cancer. 2002;2(4):277–288. doi:10.1038/nrc776
   PubMed Web of Science ®Google Scholar
• Nezhat F, Cohen C, Rahaman J, Gretz H, Cole P, Kalir T. Comparative immunohistochemical studies of bcl-2 and p53 proteins in benign and malignant ovarian endometriotic cysts. Cancer. 2002;94(11):2935–2940. doi:10.1002/cncr.10566
   PubMed Web of Science ®Google Scholar
• Nasu K, Nishida M, Kawano Y, et al. Aberrant expression of apoptosis-related molecules in endometriosis: a possible mechanism underlying the pathogenesis of endometriosis. Reprod Sci. 2011;18(3):206–218. doi:10.1177/1933719110392059
   PubMed Web of Science ®Google Scholar
• Chua BT, Volbracht C, Tan KO, Li R, Yu VC, Li P. Mitochondrial translocation of cofilin is an early step in apoptosis induction. Nat Cell Biol. 2003;5(12):1083–1089. doi:10.1038/ncb1070
   PubMed Web of Science ®Google Scholar
• Hatch AL, Gurel PS, Higgs HN. Novel roles for actin in mitochondrial fission. J Cell Sci. 2014;127(Pt 21):4549–4560. doi:10.1242/jcs.153791
   PubMed Web of Science ®Google Scholar
• Hu C, Huang Y, Li L. Drp1-Dependent Mitochondrial Fission Plays Critical Roles in Physiological and Pathological Progresses in Mammals. Int J Mol Sci. 2017;18(1):144. doi:10.3390/ijms18010144
   PubMed Web of Science ®Google Scholar
• Guo L, Cui C, Wang J, et al. PINCH-1 regulates mitochondrial dynamics to promote proline synthesis and tumor growth. Nat Commun. 2020;11(1):4913. doi:10.1038/s41467-020-18753-6
   PubMed Web of Science ®Google Scholar
• Taguchi N, Ishihara N, Jofuku A, Oka T, Mihara K. Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission. J Biol Chem. 2007;282(15):11521–11529. doi:10.1074/jbc.M607279200
   PubMed Web of Science ®Google Scholar
• Hu J, Zhang H, Li J, et al. ROCK1 activation-mediated mitochondrial translocation of Drp1 and cofilin are required for arnidiol-induced mitochondrial fission and apoptosis. J Exp Clin Cancer Res. 2020;39(1):37. doi:10.1186/s13046-020-01545-7
   PubMed Web of Science ®Google Scholar
• Zhang L, Cao H, Tao H, Yang J, Gong W, Hu Q. Effect of the interference with DRP1 expression on the biological characteristics of glioma stem cells. Exp Ther Med. 2021;22(1):696. doi:10.3892/etm.2021.10128
   PubMed Web of Science ®Google Scholar
• Otera H, Miyata N, Kuge O, Mihara K. Drp1-dependent mitochondrial fission via MiD49/51 is essential for apoptotic cristae remodeling. J Cell Biol. 2016;212(5):531–544. doi:10.1083/jcb.201508099
   PubMed Web of Science ®Google Scholar
• Stupp R, Hegi ME, Mason WP, et al. Effects of radiotherapy with concomitant and adjuvant temozolomide versus radiotherapy alone on survival in glioblastoma in a randomised Phase III study: 5-year analysis of the EORTC-NCIC trial. Lancet Oncol. 2009;10(5):459–466. doi:10.1016/s1470-2045(09)70025-7
   PubMed Web of Science ®Google Scholar
• Stupp R, Mason WP, van den Bent MJ, et al. Radiotherapy plus concomitant and adjuvant temozolomide for glioblastoma. N Engl J Med. 2005;352(10):987–996. doi:10.1056/NEJMoa043330
   PubMed Web of Science ®Google Scholar
• Du HQ, Chen L, Wang Y, et al. Increasing radiosensitivity with the downregulation of cofilin-1 in U251 human glioma cells. Mol Med Rep. 2015;11(5):3354–3360. doi:10.3892/mmr.2014.3125
   PubMed Web of Science ®Google Scholar
• Zhou T, Wang CH, Yan H, et al. Inhibition of the Rac1-WAVE2-Arp2/3 signaling pathway promotes radiosensitivity via downregulation of cofilin-1 in U251 human glioma cells. Mol Med Rep. 2016;13(5):4414–4420. doi:10.3892/mmr.2016.5088
   PubMed Web of Science ®Google Scholar
• Abbott NJ, Rönnbäck L, Hansson E. Astrocyte-endothelial interactions at the blood-brain barrier. Nat Rev Neurosci. 2006;7(1):41–53. doi:10.1038/nrn1824
   PubMed Web of Science ®Google Scholar
• Arvanitis CD, Ferraro GB, Jain RK. The blood-brain barrier and blood-tumour barrier in brain tumours and metastases. Nat Rev Cancer. 2020;20(1):26–41. doi:10.1038/s41568-019-0205-x
   PubMed Web of Science ®Google Scholar
• Idbaih A, Ducray F, Sierra Del Rio M, Hoang-Xuan K, Delattre JY. Therapeutic application of noncytotoxic molecular targeted therapy in gliomas: growth factor receptors and angiogenesis inhibitors. Oncologist. 2008;13(9):978–992. doi:10.1634/theoncologist.2008-0056
   PubMed Web of Science ®Google Scholar
• Xie H, Xue YX, Liu LB, Liu YH, Wang P. Role of RhoA/ROCK signaling in endothelial-monocyte-activating polypeptide II opening of the blood-tumor barrier: role of RhoA/ROCK signaling in EMAP II opening of the BTB. J Mol Neurosci. 2012;46(3):666–676. doi:10.1007/s12031-011-9564-9
   PubMed Web of Science ®Google Scholar
• Li Z, Liu YH, Xue YX, Liu LB, Wang P. Signal mechanisms underlying low-dose endothelial monocyte-activating polypeptide-II-induced opening of the blood-tumor barrier. J Mol Neurosci. 2012;48(1):291–301. doi:10.1007/s12031-012-9776-7
   PubMed Web of Science ®Google Scholar
• Li Z, Liu XB, Liu YH, et al. Low-dose endothelial monocyte-activating polypeptide-II increases blood-tumor barrier permeability by activating the RhoA/ROCK/PI3K signaling pathway. J Mol Neurosci. 2016;59(2):193–202. doi:10.1007/s12031-015-0668-5
   PubMed Web of Science ®Google Scholar
• Kim JW, Gao P, Liu YC, Semenza GL, Dang CV. Hypoxia-inducible factor 1 and dysregulated c-Myc cooperatively induce vascular endothelial growth factor and metabolic switches hexokinase 2 and pyruvate dehydrogenase kinase 1. Mol Cell Biol. 2007;27(21):7381–7393. doi:10.1128/mcb.00440-07
   PubMed Web of Science ®Google Scholar
• Wolf A, Agnihotri S, Micallef J, et al. Hexokinase 2 is a key mediator of aerobic glycolysis and promotes tumor growth in human glioblastoma multiforme. J Exp Med. 2011;208(2):313–326. doi:10.1084/jem.20101470
   PubMed Web of Science ®Google Scholar
• Ghosh S, Paul A, Sen E. Tumor necrosis factor α-induced hypoxia-inducible factor 1α-β-catenin axis regulates major histocompatibility complex class I gene activation through chromatin remodeling. Mol Cell Biol. 2013;33(14):2718–2731. doi:10.1128/mcb.01254-12
   PubMed Web of Science ®Google Scholar
• Ghosh S, Gupta P, Sen E. TNFα driven HIF-1α-hexokinase II axis regulates MHC-I cluster stability through actin cytoskeleton. Exp Cell Res. 2016;340(1):116–124. doi:10.1016/j.yexcr.2015.11.016
   PubMed Web of Science ®Google Scholar
• Lewinska A, Klukowska-Rötzler J, Deregowska A, Adamczyk-Grochala J, Wnuk M. c-Myc activation promotes cofilin-mediated F-actin cytoskeleton remodeling and telomere homeostasis as a response to oxidant-based DNA damage in medulloblastoma cells. Redox Biol. 2019;24:101163. doi:10.1016/j.redox.2019.101163
   PubMed Web of Science ®Google Scholar
• Obrdlik A, The PP. F-actin severing protein cofilin-1 is required for RNA polymerase II transcription elongation. Nucleus. 2011;2(1):72–79. doi:10.4161/nucl.2.1.14508
   PubMed Web of Science ®Google Scholar
• Müller CB, de Barros RL, Castro MA, et al. Validation of cofilin-1 as a biomarker in non-small cell lung cancer: application of quantitative method in a retrospective cohort. J Cancer Res Clin Oncol. 2011;137(9):1309–1316. doi:10.1007/s00432-011-1001-5
   PubMed Web of Science ®Google Scholar
• Rak R, Haklai R, Elad-Tzfadia G, Wolfson HJ, Carmeli S, Novel KY. LIMK2 Inhibitor blocks Panc-1 tumor growth in a mouse xenograft model. Oncoscience. 2014;1(1):39–48. doi:10.18632/oncoscience.7
   PubMedGoogle Scholar
• Wang X, Zou S, Ren T, et al. Alantolactone suppresses the metastatic phenotype and induces the apoptosis of glioblastoma cells by targeting LIMK kinase activity and activating the cofilin/G‑actin signaling cascade. Int J Mol Med. 2021;47(5). doi:10.3892/ijmm.2021.4901
   Web of Science ®Google Scholar
• Porcù E, Maule F, Boso D, et al. BMP9 counteracts the tumorigenic and pro-angiogenic potential of glioblastoma. Cell Death Differ. 2018;25(10):1808–1822. doi:10.1038/s41418-018-0149-9
   PubMed Web of Science ®Google Scholar
• Hua D, Zhao Q, Yu Y, et al. Eucalyptal A inhibits glioma by rectifying oncogenic splicing of MYO1B mRNA via suppressing SRSF1 expression. Eur J Pharmacol. 2021;890:173669. doi:10.1016/j.ejphar.2020.173669
   PubMed Web of Science ®Google Scholar
• Xing JS, Wang X, Lan YL, et al. Isoalantolactone inhibits IKKβ kinase activity to interrupt the NF-κB/COX-2-mediated signaling cascade and induces apoptosis regulated by the mitochondrial translocation of cofilin in glioblastoma. Cancer Med. 2019;8(4):1655–1670. doi:10.1002/cam4.2013
   PubMed Web of Science ®Google Scholar
• Tang Q, Ji Q, Tang Y, et al. Mitochondrial translocation of cofilin-1 promotes apoptosis of gastric cancer BGC-823 cells induced by ursolic acid. Tumour Biol. 2014;35(3):2451–2459. doi:10.1007/s13277-013-1325-7
   PubMedGoogle Scholar
• Li R, Wang X, Zhang XH, Chen HH, Liu YD. Ursolic acid promotes apoptosis of SGC-7901 gastric cancer cells through ROCK/PTEN mediated mitochondrial translocation of cofilin-1. Asian Pac J Cancer Prev. 2014;15(22):9593–9597. doi:10.7314/apjcp.2014.15.22.9593
   PubMedGoogle Scholar
• Prełowska M, Kaczyńska A, Herman-Antosiewicz A. 4-(Methylthio)butyl isothiocyanate inhibits the proliferation of breast cancer cells with different receptor status. Pharmacol Rep. 2017;69(5):1059–1066. doi:10.1016/j.pharep.2017.04.014
   PubMed Web of Science ®Google Scholar
• Wang Q, Gao S, Wu GZ, et al. Total sesquiterpene lactones isolated from Inula helenium L. attenuates 2,4-dinitrochlorobenzene-induced atopic dermatitis-like skin lesions in mice. Phytomedicine. 2018;46:78–84. doi:10.1016/j.phymed.2018.04.036
   PubMed Web of Science ®Google Scholar
• Wang J, Cui L, Feng L, et al. Isoalantolactone inhibits the migration and invasion of human breast cancer MDA-MB-231 cells via suppression of the p38 MAPK/NF-κB signaling pathway. Oncol Rep. 2016;36(3):1269–1276. doi:10.3892/or.2016.4954
   PubMed Web of Science ®Google Scholar
• Li Z, Qin B, Qi X, Mao J, Wu D. Isoalantolactone induces apoptosis in human breast cancer cells via ROS-mediated mitochondrial pathway and downregulation of SIRT1. Arch Pharm Res. 2016;39(10):1441–1453. doi:10.1007/s12272-016-0815-8
   PubMed Web of Science ®Google Scholar
• Fan Y, Weng Z, Gao H, et al. Isoalantolactone enhances the radiosensitivity of UMSCC-10A Cells via specific inhibition of Erk1/2 phosphorylation. PLoS One. 2015;10(12):e0145790. doi:10.1371/journal.pone.0145790
   PubMed Web of Science ®Google Scholar
• Li GB, Cheng Q, Liu L, et al. Mitochondrial translocation of cofilin is required for allyl isothiocyanate-mediated cell death via ROCK1/PTEN/PI3K signaling pathway. Cell Commun Signal. 2013;11:50. doi:10.1186/1478-811x-11-50
   PubMed Web of Science ®Google Scholar
• Chen J, Ananthanarayanan B, Springer KS, et al. Suppression of LIM kinase 1 and LIM kinase 2 limits glioblastoma invasion. Cancer Res. 2020;80(1):69–78. doi:10.1158/0008-5472.Can-19-1237
   PubMed Web of Science ®Google Scholar
• Zebda N, Bernard O, Bailly M, Welti S, Lawrence DS, Condeelis JS. Phosphorylation of ADF/cofilin abolishes EGF-induced actin nucleation at the leading edge and subsequent lamellipod extension. J Cell Biol. 2000;151(5):1119–1128. doi:10.1083/jcb.151.5.1119
   PubMed Web of Science ®Google Scholar
• Wang W, Mouneimne G, Sidani M, et al. The activity status of cofilin is directly related to invasion, intravasation, and metastasis of mammary tumors. J Cell Biol. 2006;173(3):395–404. doi:10.1083/jcb.200510115
   PubMed Web of Science ®Google Scholar