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Volumn 114, Issue 10, 2013, Pages 2415-2429

Formation of cofilin-actin rods following cucurbitacin-B-induced actin aggregation depends on slingshot homolog 1-mediated cofilin hyperactivation

Author keywords

ACTIN AGGREGATION; COFILIN; COFILIN ACTIN RODS; CUCURBITACIN B; MELANOMA; SLINGSHOT HOMOLOG 1

Indexed keywords

ACETYLCYSTEINE; ACTIN; CHRONOPHIN; COFILIN; CUCURBITACIN; CUCURBITACIN B; LIM KINASE; PHOSPHATASE; REACTIVE OXYGEN METABOLITE; RHO KINASE; SCAVENGER; SLINGSHOT HOMOLOG 1; THIOL; THIOL GROUP; UNCLASSIFIED DRUG;

EID: 84882424327     PISSN: 07302312     EISSN: 10974644     Source Type: Journal    
DOI: 10.1002/jcb.24587     Document Type: Article
Times cited : (21)

References (45)
  • 1
    • 33749046492 scopus 로고    scopus 로고
    • Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin
    • Andrianantoandro E, Pollard TD,. 2006. Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin. Mol Cell 24: 13-23.
    • (2006) Mol Cell , vol.24 , pp. 13-23
    • Andrianantoandro, E.1    Pollard, T.D.2
  • 2
    • 56349167502 scopus 로고    scopus 로고
    • N-acetyl cysteine prevents suppression of oral fibroblast function on poly(methylmethacrylate) resin
    • Att W, Yamada M, Kojima N, Ogawa T,. 2009. N-acetyl cysteine prevents suppression of oral fibroblast function on poly(methylmethacrylate) resin. Acta Biomater 5: 391-398.
    • (2009) Acta Biomater , vol.5 , pp. 391-398
    • Att, W.1    Yamada, M.2    Kojima, N.3    Ogawa, T.4
  • 3
    • 0033280237 scopus 로고    scopus 로고
    • Proteins of the ADF/cofilin family: Essential regulators of actin dynamics
    • Bamburg JR,. 1999. Proteins of the ADF/cofilin family: Essential regulators of actin dynamics. Annu Rev Cell Dev Biol 15: 185-230.
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 185-230
    • Bamburg, J.R.1
  • 4
    • 78649373184 scopus 로고    scopus 로고
    • Roles of ADF/cofilin in actin polymerization and beyond
    • Bamburg JR, Bernstein BW,. 2010. Roles of ADF/cofilin in actin polymerization and beyond. F1000 Biol Rep 2: 62.
    • (2010) F1000 Biol Rep , vol.2 , pp. 62
    • Bamburg, J.R.1    Bernstein, B.W.2
  • 6
    • 84860657462 scopus 로고    scopus 로고
    • Incorporation of cofilin into rods depends on disulfide intermolecular bonds: Implications for actin regulation and neurodegenerative disease
    • Bernstein BW, Shaw AE, Minamide LS, Pak CW, Bamburg JR,. 2012. Incorporation of cofilin into rods depends on disulfide intermolecular bonds: Implications for actin regulation and neurodegenerative disease. J Neurosci 32: 6670-6681.
    • (2012) J Neurosci , vol.32 , pp. 6670-6681
    • Bernstein, B.W.1    Shaw, A.E.2    Minamide, L.S.3    Pak, C.W.4    Bamburg, J.R.5
  • 7
    • 79952281492 scopus 로고    scopus 로고
    • Cucurbitacin IIa: A novel class of anti-cancer drug inducing non-reversible actin aggregation and inhibiting survivin independent of JAK2/STAT3 phosphorylation
    • Boykin C, Zhang G, Chen YH, Zhang RW, Fan XE, Yang WM, Lu Q,. 2011. Cucurbitacin IIa: A novel class of anti-cancer drug inducing non-reversible actin aggregation and inhibiting survivin independent of JAK2/STAT3 phosphorylation. Br J Cancer 104: 781-789.
    • (2011) Br J Cancer , vol.104 , pp. 781-789
    • Boykin, C.1    Zhang, G.2    Chen, Y.H.3    Zhang, R.W.4    Fan, X.E.5    Yang, W.M.6    Lu, Q.7
  • 8
    • 21244470815 scopus 로고    scopus 로고
    • Cucurbitacins and cucurbitane glycosides: Structures and biological activities
    • Chen JC, Chiu MH, Nie RL, Cordell GA, Qiu SX,. 2005. Cucurbitacins and cucurbitane glycosides: Structures and biological activities. Nat Prod Rep 22: 386-399.
    • (2005) Nat Prod Rep , vol.22 , pp. 386-399
    • Chen, J.C.1    Chiu, M.H.2    Nie, R.L.3    Cordell, G.A.4    Qiu, S.X.5
  • 9
    • 84864409461 scopus 로고    scopus 로고
    • Biological activities and potential molecular targets of cucurbitacins: A focus on cancer
    • Chen X, Bao J, Guo J, Ding Q, Lu J, Huang M, Wang Y,. 2012. Biological activities and potential molecular targets of cucurbitacins: A focus on cancer. Anticancer Drugs 23: 777-787.
    • (2012) Anticancer Drugs , vol.23 , pp. 777-787
    • Chen, X.1    Bao, J.2    Guo, J.3    Ding, Q.4    Lu, J.5    Huang, M.6    Wang, Y.7
  • 10
    • 0028972851 scopus 로고
    • 2-treated actin: Assembly and polymer interactions with cross-linking proteins
    • 2-treated actin: Assembly and polymer interactions with cross-linking proteins. Biophys J 69: 2710-2719.
    • (1995) Biophys J , vol.69 , pp. 2710-2719
    • Dalledonne, I.1    Milzani, A.2    Colombo, R.3
  • 12
    • 0030598398 scopus 로고    scopus 로고
    • Cucurbitacin E-induced disruption of the actin and vimentin cytoskeleton in prostate carcinoma cells
    • Duncan KL, Duncan MD, Alley MC, Sausville EA,. 1996. Cucurbitacin E-induced disruption of the actin and vimentin cytoskeleton in prostate carcinoma cells. Biochem Pharmacol 52: 1553-1560.
    • (1996) Biochem Pharmacol , vol.52 , pp. 1553-1560
    • Duncan, K.L.1    Duncan, M.D.2    Alley, M.C.3    Sausville, E.A.4
  • 13
    • 2342436150 scopus 로고    scopus 로고
    • Cofilin promotes actin polymerization and defines the direction of cell motility
    • Ghosh M, Song X, Mouneimne G, Sidani M, Lawrence DS, Condeelis JS,. 2004. Cofilin promotes actin polymerization and defines the direction of cell motility. Science 304: 743-746.
    • (2004) Science , vol.304 , pp. 743-746
    • Ghosh, M.1    Song, X.2    Mouneimne, G.3    Sidani, M.4    Lawrence, D.S.5    Condeelis, J.S.6
  • 14
    • 12344250639 scopus 로고    scopus 로고
    • Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics
    • Gohla A, Birkenfeld J, Bokoch GM,. 2005. Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics. Nat Cell Biol 7: 21-29.
    • (2005) Nat Cell Biol , vol.7 , pp. 21-29
    • Gohla, A.1    Birkenfeld, J.2    Bokoch, G.M.3
  • 15
    • 68549126922 scopus 로고    scopus 로고
    • The cytoskeleton and cancer
    • Hall A,. 2009. The cytoskeleton and cancer. Cancer Metastasis Rev 28: 5-14.
    • (2009) Cancer Metastasis Rev , vol.28 , pp. 5-14
    • Hall, A.1
  • 16
    • 43049175018 scopus 로고    scopus 로고
    • Cucurbitacin B induces differentiation, cell cycle arrest, and actin cytoskeletal alterations in myeloid leukemia cells
    • Haritunians T, Gueller S, Zhang L, Badr R, Yin D, Xing H, Fung MC, Koeffler HP,. 2008. Cucurbitacin B induces differentiation, cell cycle arrest, and actin cytoskeletal alterations in myeloid leukemia cells. Leuk Res 32: 1366-1373.
    • (2008) Leuk Res , vol.32 , pp. 1366-1373
    • Haritunians, T.1    Gueller, S.2    Zhang, L.3    Badr, R.4    Yin, D.5    Xing, H.6    Fung, M.C.7    Koeffler, H.P.8
  • 17
    • 77952882851 scopus 로고    scopus 로고
    • N-acetyl cysteine mitigates curcumin-mediated telomerase inhibition through rescuing of Sp1 reduction in A549 cells
    • Hsin IL, Sheu G-T, Chen H-H, Chiu L-Y, Wang H-D, Chan H-W, Hsu C-P, Ko J-L,. 2010. N-acetyl cysteine mitigates curcumin-mediated telomerase inhibition through rescuing of Sp1 reduction in A549 cells. Mutat Res 688: 72-77.
    • (2010) Mutat Res , vol.688 , pp. 72-77
    • Hsin, I.L.1    Sheu, G.-T.2    Chen, H.-H.3    Chiu, L.-Y.4    Wang, H.-D.5    Chan, H.-W.6    Hsu, C.-P.7    Ko, J.-L.8
  • 19
    • 55549091059 scopus 로고    scopus 로고
    • Chronophin mediates an ATP-sensing mechanism for cofilin dephosphorylation and neuronal cofilin-actin rod formation
    • Huang TY, Minamide LS, Bamburg JR, Bokoch GM,. 2008. Chronophin mediates an ATP-sensing mechanism for cofilin dephosphorylation and neuronal cofilin-actin rod formation. Dev Cell 15: 691-703.
    • (2008) Dev Cell , vol.15 , pp. 691-703
    • Huang, T.Y.1    Minamide, L.S.2    Bamburg, J.R.3    Bokoch, G.M.4
  • 20
    • 27644495116 scopus 로고    scopus 로고
    • Cofilin expression induces cofilin-actin rod formation and disrupts synaptic structure and function in aplysia synapses
    • Jang DH, Han JH, Lee SH, Lee YS, Park H, Lee SH, Kim H, Kaang BK,. 2005. Cofilin expression induces cofilin-actin rod formation and disrupts synaptic structure and function in aplysia synapses. Proc Natl Acad Sci USA 102: 16072-16077.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 16072-16077
    • Jang, D.H.1    Han, J.H.2    Lee, S.H.3    Lee, Y.S.4    Park, H.5    Lee, S.H.6    Kim, H.7    Kaang, B.K.8
  • 21
    • 0037427563 scopus 로고    scopus 로고
    • Anticancer and antiinflammatory activities of cucurbitacins from Cucurbita andreana
    • Jayaprakasam B, Seeram NP, Nair MG,. 2003. Anticancer and antiinflammatory activities of cucurbitacins from Cucurbita andreana. Cancer Lett 189: 11-16.
    • (2003) Cancer Lett , vol.189 , pp. 11-16
    • Jayaprakasam, B.1    Seeram, N.P.2    Nair, M.G.3
  • 22
    • 66349108700 scopus 로고    scopus 로고
    • Reactive oxygen species regulate a slingshot-cofilin activation pathway
    • Kim JS, Huang TY, Bokoch GM,. 2009. Reactive oxygen species regulate a slingshot-cofilin activation pathway. Mol Biol Cell 20: 2650-2660.
    • (2009) Mol Biol Cell , vol.20 , pp. 2650-2660
    • Kim, J.S.1    Huang, T.Y.2    Bokoch, G.M.3
  • 24
    • 2142765951 scopus 로고    scopus 로고
    • A syntaxin 1, Galpha(o), and N-type calcium channel complex at a presynaptic nerve terminal: Analysis by quantitative immunocolocalization
    • Li Q, Lau A, Morris TJ, Guo L, Fordyce CB, Stanley EF,. 2004. A syntaxin 1, Galpha(o), and N-type calcium channel complex at a presynaptic nerve terminal: Analysis by quantitative immunocolocalization. J Neurosci 24: 4070-4081.
    • (2004) J Neurosci , vol.24 , pp. 4070-4081
    • Li, Q.1    Lau, A.2    Morris, T.J.3    Guo, L.4    Fordyce, C.B.5    Stanley, E.F.6
  • 25
    • 0037786965 scopus 로고    scopus 로고
    • Rho-ROCK-LIMK-cofilin pathway regulates shear stress activation of sterol regulatory element binding proteins
    • Lin T, Zeng L, Liu Y, DeFea K, Schwartz MA, Chien S, Shyy JY,. 2003. Rho-ROCK-LIMK-cofilin pathway regulates shear stress activation of sterol regulatory element binding proteins. Circ Res 92: 1296-1304.
    • (2003) Circ Res , vol.92 , pp. 1296-1304
    • Lin, T.1    Zeng, L.2    Liu, Y.3    Defea, K.4    Schwartz, M.A.5    Chien, S.6    Shyy, J.Y.7
  • 26
    • 0035023063 scopus 로고    scopus 로고
    • Oxidant stress and endothelial cell dysfunction
    • Lum H, Roebuck KA,. 2001. Oxidant stress and endothelial cell dysfunction. Am J Physiol Cell Physiol 280: C719-C741.
    • (2001) Am J Physiol Cell Physiol , vol.280
    • Lum, H.1    Roebuck, K.A.2
  • 27
    • 30544447666 scopus 로고    scopus 로고
    • Beta-secretase-cleaved amyloid precursor protein accumulates at actin inclusions induced in neurons by stress or amyloid beta: A feedforward mechanism for Alzheimer's disease
    • Maloney MT, Minamide LS, Kinley AW, Boyle JA, Bamburg JR,. 2005. Beta-secretase-cleaved amyloid precursor protein accumulates at actin inclusions induced in neurons by stress or amyloid beta: A feedforward mechanism for Alzheimer's disease. J Neurosci 25: 11313-11321.
    • (2005) J Neurosci , vol.25 , pp. 11313-11321
    • Maloney, M.T.1    Minamide, L.S.2    Kinley, A.W.3    Boyle, J.A.4    Bamburg, J.R.5
  • 28
    • 0031952055 scopus 로고    scopus 로고
    • Actin depolymerizing factor and cofilin phosphorylation dynamics: Response to signals that regulate neurite extension
    • Meberg PJ, Ono S, Minamide LS, Takahashi M, Bamburg JR,. 1998. Actin depolymerizing factor and cofilin phosphorylation dynamics: Response to signals that regulate neurite extension. Cell Motil Cytoskeleton 39: 172-190.
    • (1998) Cell Motil Cytoskeleton , vol.39 , pp. 172-190
    • Meberg, P.J.1    Ono, S.2    Minamide, L.S.3    Takahashi, M.4    Bamburg, J.R.5
  • 29
    • 0034282106 scopus 로고    scopus 로고
    • Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function
    • Minamide LS, Striegl AM, Boyle JA, Meberg PJ, Bamburg JR,. 2000. Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function. Nat Cell Biol 2: 628-636.
    • (2000) Nat Cell Biol , vol.2 , pp. 628-636
    • Minamide, L.S.1    Striegl, A.M.2    Boyle, J.A.3    Meberg, P.J.4    Bamburg, J.R.5
  • 34
    • 0023387681 scopus 로고
    • Cofilin is a component of intranuclear and cytoplasmic actin rods induced in cultured cells
    • Nishida E, Iida K, Yonezawa N, Koyasu S, Yahara I, Sakai H,. 1987. Cofilin is a component of intranuclear and cytoplasmic actin rods induced in cultured cells. Proc Natl Acad Sci USA 84: 5262-5266.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5262-5266
    • Nishida, E.1    Iida, K.2    Yonezawa, N.3    Koyasu, S.4    Yahara, I.5    Sakai, H.6
  • 35
    • 0037169335 scopus 로고    scopus 로고
    • Control of actin reorganization by slingshot, a family of phosphatases that dephosphorylate ADF/cofilin
    • Niwa R, Nagata-Ohashi K, Takeichi M, Mizuno K, Uemura T,. 2002. Control of actin reorganization by slingshot, a family of phosphatases that dephosphorylate ADF/cofilin. Cell 108: 233-246.
    • (2002) Cell , vol.108 , pp. 233-246
    • Niwa, R.1    Nagata-Ohashi, K.2    Takeichi, M.3    Mizuno, K.4    Uemura, T.5
  • 36
    • 0030425905 scopus 로고    scopus 로고
    • Stimulus-dependent disorganization of actin filaments induced by overexpression of cofilin in C2 myoblasts
    • Ono S, Abe H, Obinata T,. 1996. Stimulus-dependent disorganization of actin filaments induced by overexpression of cofilin in C2 myoblasts. Cell Struct Funct 21: 491-499.
    • (1996) Cell Struct Funct , vol.21 , pp. 491-499
    • Ono, S.1    Abe, H.2    Obinata, T.3
  • 37
    • 34249887660 scopus 로고    scopus 로고
    • LIM kinases: Function, regulation and association with human disease
    • Scott RW, Olson MF,. 2007. LIM kinases: Function, regulation and association with human disease. J Mol Med (Berl) 85: 555-568.
    • (2007) J Mol Med (Berl) , vol.85 , pp. 555-568
    • Scott, R.W.1    Olson, M.F.2
  • 40
    • 84859207907 scopus 로고    scopus 로고
    • Off-target thiol alkylation by the NADPH oxidase inhibitor 3-benzyl-7-(2-benzoxazolyl)thio-1,2,3-triazolo[4,5-d]pyrimidine (VAS2870)
    • Sun QA, Hess DT, Wang B, Miyagi M, Stamler JS,. 2012. Off-target thiol alkylation by the NADPH oxidase inhibitor 3-benzyl-7-(2-benzoxazolyl)thio-1,2,3- triazolo[4,5-d]pyrimidine (VAS2870). Free Radic Biol Med 52: 1897-1902.
    • (2012) Free Radic Biol Med , vol.52 , pp. 1897-1902
    • Sun, Q.A.1    Hess, D.T.2    Wang, B.3    Miyagi, M.4    Stamler, J.S.5
  • 42
    • 34249281332 scopus 로고    scopus 로고
    • The cofilin pathway in breast cancer invasion and metastasis
    • Wang W, Eddy R, Condeelis J,. 2007. The cofilin pathway in breast cancer invasion and metastasis. Nat Rev Cancer 7: 429-440.
    • (2007) Nat Rev Cancer , vol.7 , pp. 429-440
    • Wang, W.1    Eddy, R.2    Condeelis, J.3
  • 43
    • 49749119221 scopus 로고    scopus 로고
    • Cucurbitacin B markedly inhibits growth and rapidly affects the cytoskeleton in glioblastoma multiforme
    • Yin D, Wakimoto N, Xing H, Lu D, Huynh T, Wang X, Black KL, Koeffler HP,. 2008. Cucurbitacin B markedly inhibits growth and rapidly affects the cytoskeleton in glioblastoma multiforme. Int J Cancer 123: 1364-1375.
    • (2008) Int J Cancer , vol.123 , pp. 1364-1375
    • Yin, D.1    Wakimoto, N.2    Xing, H.3    Lu, D.4    Huynh, T.5    Wang, X.6    Black, K.L.7    Koeffler, H.P.8
  • 44
    • 77953593973 scopus 로고    scopus 로고
    • Importance of cofilin oxidation for oxidant-induced apoptosis
    • Zdanov S, Klamt F, Shacter E,. 2010. Importance of cofilin oxidation for oxidant-induced apoptosis. Cell Cycle 9: 1675-1677.
    • (2010) Cell Cycle , vol.9 , pp. 1675-1677
    • Zdanov, S.1    Klamt, F.2    Shacter, E.3
  • 45
    • 79960122371 scopus 로고    scopus 로고
    • Cucurbitacin B induces rapid depletion of the G-actin pool through reactive oxygen species-dependent actin aggregation in melanoma cells
    • Zhang Y, Ouyang D, Xu L, Ji Y, Zha Q, Cai J, He X,. 2011. Cucurbitacin B induces rapid depletion of the G-actin pool through reactive oxygen species-dependent actin aggregation in melanoma cells. Acta Biochim Biophys Sin (Shanghai) 43: 556-567.
    • (2011) Acta Biochim Biophys Sin (Shanghai) , vol.43 , pp. 556-567
    • Zhang, Y.1    Ouyang, D.2    Xu, L.3    Ji, Y.4    Zha, Q.5    Cai, J.6    He, X.7


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