메뉴 건너뛰기




Volumn 32, Issue 40, 2013, Pages 4814-4824

Mitochondrial dynamics regulates migration and invasion of breast cancer cells

Author keywords

breast cancer; Drp1; fission and fusion; lamellipodia; metastasis; mitochondrial dynamics

Indexed keywords

ADENOSINE TRIPHOSPHATE; DYNAMIN RELATED PROTEIN 1; F ACTIN; HYBRID PROTEIN; MITOCHONDRIAL FUSION PROTEIN 1; MITOCHONDRIAL PROTEIN; UNCLASSIFIED DRUG;

EID: 84885181954     PISSN: 09509232     EISSN: 14765594     Source Type: Journal    
DOI: 10.1038/onc.2012.494     Document Type: Article
Times cited : (564)

References (45)
  • 2
    • 34247468876 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton in cancer cell migration and invasion
    • Yamaguchi H, Condeelis J. Regulation of the actin cytoskeleton in cancer cell migration and invasion. Biochim Biophys Acta 2007; 1773: 642-652.
    • (2007) Biochim Biophys Acta , vol.1773 , pp. 642-652
    • Yamaguchi, H.1    Condeelis, J.2
  • 3
    • 28444472417 scopus 로고    scopus 로고
    • The great escape: When cancer cells hijack the genes for chemotaxis and motility
    • Condeelis J, Singer RH, Segall JE. The great escape: When cancer cells hijack the genes for chemotaxis and motility. Annu Rev Cell Dev Biol 2005; 21: 695-718.
    • (2005) Annu Rev Cell Dev Biol , vol.21 , pp. 695-718
    • Condeelis, J.1    Singer, R.H.2    Segall, J.E.3
  • 4
    • 70849098888 scopus 로고    scopus 로고
    • Actin, a central player in cell shape and movement
    • Pollard TD, Cooper JA. Actin, a central player in cell shape and movement. Science 2009; 326: 1208-1212.
    • (2009) Science , vol.326 , pp. 1208-1212
    • Pollard, T.D.1    Cooper, J.A.2
  • 5
    • 0019246681 scopus 로고
    • Structure and function of the energy-converting system of mitochondria
    • Von Jagow G, Engel WD. Structure and function of the energy-converting system of mitochondria. Angew Chem Int Ed Engl 1980; 19: 659-675.
    • (1980) Angew Chem Int Ed Engl , vol.19 , pp. 659-675
    • Von Jagow, G.1    Engel, W.D.2
  • 6
    • 42049090126 scopus 로고    scopus 로고
    • Mitochondria: The hub of cellular Ca2 signaling
    • Szabadkai G, Duchen MR. Mitochondria: The hub of cellular Ca2? signaling. Physiology 2008; 23: 84-94.
    • (2008) Physiology , vol.23 , pp. 84-94
    • Szabadkai, G.1    Duchen, M.R.2
  • 7
    • 78649413837 scopus 로고    scopus 로고
    • Mitochondrial fusion and fission in cell life and Death
    • Westermann B. Mitochondrial fusion and fission in cell life and Death. Nat Rev Mol Cell Biol 2010; 11: 872-884.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 872-884
    • Westermann, B.1
  • 8
    • 33750452725 scopus 로고    scopus 로고
    • Dissecting mitochondrial fusion
    • Chan DC. Dissecting mitochondrial fusion. Dev Cell 2006; 11: 592-594.
    • (2006) Dev Cell , vol.11 , pp. 592-594
    • Chan, D.C.1
  • 9
    • 0028137817 scopus 로고
    • Mitochondria buffer physiological calcium loads in cultured rat dorsal root ganglion neurons
    • Werth JL, Thayer SA. Mitochondria buffer physiological calcium loads in cultured rat dorsal root ganglion neurons. J Neurosci 1994; 14: 348-356.
    • (1994) J Neurosci , vol.14 , pp. 348-356
    • Werth, J.L.1    Thayer, S.A.2
  • 10
    • 35448960851 scopus 로고    scopus 로고
    • Functions and dysfunctions of mitochondrial dynamics
    • de tmer SA, Chan DC. Functions and dysfunctions of mitochondrial dynamics. Nat Rev Mol Cell Biol 2007; 8: 870-879.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 870-879
    • De Tmer, S.A.1    Chan, D.C.2
  • 11
    • 84880305315 scopus 로고    scopus 로고
    • G-protein beta2 subunit interacts with mitofusin 1 to regulate mitochondrial fusion
    • Zhang J, Liu W, Liu J, Xiao W, Liu L, Jiang C et al. G-protein beta2 subunit interacts with mitofusin 1 to regulate mitochondrial fusion. Nat Commun 2010; 1: 101.
    • (2010) Nat Commun , vol.1 , pp. 101
    • Zhang, J.1    Liu, W.2    Liu, J.3    Xiao, W.4    Liu, L.5    Jiang, C.6
  • 12
    • 67349256860 scopus 로고    scopus 로고
    • Bringing up the rear: De fining the roles of the uropod
    • Sanchez-Madrid F, Serrador JM. Bringing up the rear: De fining the roles of the uropod. Nat Rev Mol Cell Biol 2009; 10: 353-359.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 353-359
    • Sanchez-Madrid, F.1    Serrador, J.M.2
  • 14
    • 30544452263 scopus 로고    scopus 로고
    • The axonal transport of mitochondria
    • Hollenbeck PJ, Saxton WM. The axonal transport of mitochondria. J Cell Sci 2005; 118: 5411-5419.
    • (2005) J Cell Sci , vol.118 , pp. 5411-5419
    • Hollenbeck, P.J.1    Saxton, W.M.2
  • 15
    • 2342525090 scopus 로고    scopus 로고
    • Mitochondrial DNA mutation and de pletion increase the susceptibility of human cells to apoptosis
    • Liu CY, Lee CF, Hong CH, Wei YH. Mitochondrial DNA mutation and de pletion increase the susceptibility of human cells to apoptosis. Ann N Y Acad Sci 2004; 1011: 133-145.
    • (2004) Ann N y Acad Sci , vol.1011 , pp. 133-145
    • Liu, C.Y.1    Lee, C.F.2    Hong, C.H.3    Wei, Y.H.4
  • 16
    • 45349094984 scopus 로고    scopus 로고
    • Mitochondrial dynamics and apoptosis
    • Suen DF, Norris KL, Youle RJ. Mitochondrial dynamics and apoptosis. Genes Dev 2008; 22: 1577-1590.
    • (2008) Genes Dev , vol.22 , pp. 1577-1590
    • Suen, D.F.1    Norris, K.L.2    Youle, R.J.3
  • 17
    • 67650868959 scopus 로고    scopus 로고
    • Mitochondrial dynamics in mammalian health and disease
    • Liesa M, Palac?́n M, Zorzano A. Mitochondrial dynamics in mammalian health and disease. Physiol Rev 2009; 89: 799-845.
    • (2009) Physiol Rev , vol.89 , pp. 799-845
    • Liesa, M.1    Palaćn, M.2    Zorzano, A.3
  • 19
    • 41149105722 scopus 로고    scopus 로고
    • Mitochondria in cancer cells: What is so special about them?
    • Gogvadze V, Orrenius S, Zhivotovsky B. Mitochondria in cancer cells: What is so special about them? Trends Cell Biol 2008; 18: 165-173.
    • (2008) Trends Cell Biol , vol.18 , pp. 165-173
    • Gogvadze, V.1    Orrenius, S.2    Zhivotovsky, B.3
  • 20
    • 84860914473 scopus 로고    scopus 로고
    • Inhibition of mitochondrial fission prevents cell cycle progression in lung cancer
    • Rehman J, Zhang HJ, Toth PT, Zhang Y, Marsboom G, Hong Z et al. Inhibition of mitochondrial fission prevents cell cycle progression in lung cancer. FASEB J 2012; 26: 2175-2186.
    • (2012) FASEB J , vol.26 , pp. 2175-2186
    • Rehman, J.1    Zhang, H.J.2    Toth, P.T.3    Zhang, Y.4    Marsboom, G.5    Hong, Z.6
  • 21
    • 34347234200 scopus 로고    scopus 로고
    • The chemoinvasion assay: A method to assess tumor and endothelial cell invasion and its modulation
    • Albini A, Benelli R. The chemoinvasion assay: A method to assess tumor and endothelial cell invasion and its modulation. Nat Protoc 2007; 2: 504-511.
    • (2007) Nat Protoc , vol.2 , pp. 504-511
    • Albini, A.1    Benelli, R.2
  • 22
    • 34249689057 scopus 로고    scopus 로고
    • Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission
    • 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: 11521-11529.
    • (2007) J Biol Chem , vol.282 , pp. 11521-11529
    • Taguchi, N.1    Ishihara, N.2    Jofuku, A.3    Oka, T.4    Mihara, K.5
  • 23
    • 38849099158 scopus 로고    scopus 로고
    • Chemical inhibition of the mitochondrial division dynamin reveals its role in Bax/Bakdependent mitochondrial outer membrane permeabilization
    • Cassidy-Stone A, Chipuk JE, Ingerman E, Song C, Yoo C, Kuwana T et al. Chemical inhibition of the mitochondrial division dynamin reveals its role in Bax/Bakdependent mitochondrial outer membrane permeabilization. Dev Cell 2008; 14: 193-204.
    • (2008) Dev Cell , vol.14 , pp. 193-204
    • Cassidy-Stone, A.1    Chipuk, J.E.2    Ingerman, E.3    Song, C.4    Yoo, C.5    Kuwana, T.6
  • 24
    • 0037455575 scopus 로고    scopus 로고
    • Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic Development
    • Chen H, de tmer SA, Ewald AJ, Griffin EE, Fraser SE, DC Chan. Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic Development. J Cell Biol 2003; 160: 189-200.
    • (2003) J Cell Biol , vol.160 , pp. 189-200
    • Chen, H.1    Detmer, S.A.2    Ewald, A.J.3    Griffin, E.E.4    Fraser, S.E.5    Chan, D.C.6
  • 25
    • 13444287961 scopus 로고    scopus 로고
    • Mitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity
    • Ishihara N, Eura Y, Mihara K. Mitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity. J Cell Sci 2004; 117: 6535-6546.
    • (2004) J Cell Sci , vol.117 , pp. 6535-6546
    • Ishihara, N.1    Eura, Y.2    Mihara, K.3
  • 26
    • 77951737783 scopus 로고    scopus 로고
    • Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations
    • Chen H, Vermulst M, Wang YE, Chomyn A, Prolla TA, McCaffery JM et al. Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations. Cell 2010; 141: 280-289.
    • (2010) Cell , vol.141 , pp. 280-289
    • Chen, H.1    Vermulst, M.2    Wang, Y.E.3    Chomyn, A.4    Prolla, T.A.5    McCaffery, J.M.6
  • 28
    • 79953180902 scopus 로고    scopus 로고
    • Assessing mitochondrial dysfunction in cells
    • Brand MD, Nicholls DG. Assessing mitochondrial dysfunction in cells. Biochem J 2011; 435: 297-312.
    • (2011) Biochem J , vol.435 , pp. 297-312
    • Brand, M.D.1    Nicholls, D.G.2
  • 29
    • 51149106133 scopus 로고    scopus 로고
    • Mitochondrial membrane potential in axons increases with local nerve growth factor or semaphorin signaling
    • Verburg J, Hollenbeck PJ. Mitochondrial membrane potential in axons increases with local nerve growth factor or semaphorin signaling. J Neurosci 2008; 28: 8306-8315.
    • (2008) J Neurosci , vol.28 , pp. 8306-8315
    • Verburg, J.1    Hollenbeck, P.J.2
  • 30
    • 0033971898 scopus 로고    scopus 로고
    • Mitochondria and neuronal survival
    • Nicholls DG, Budd SL. Mitochondria and neuronal survival. Physiol Rev 2000; 80: 315-360.
    • (2000) Physiol Rev , vol.80 , pp. 315-360
    • Nicholls, D.G.1    Budd, S.L.2
  • 31
    • 0016397204 scopus 로고
    • The mechanism of inhibition by oligomycin of oxidative phosphorylation in mitochondria
    • Bertina RM, Steenstra JA, Slater EC. The mechanism of inhibition by oligomycin of oxidative phosphorylation in mitochondria. Biochim Biophys Acta 1974; 368: 279-297.
    • (1974) Biochim Biophys Acta , vol.368 , pp. 279-297
    • Bertina, R.M.1    Steenstra, J.A.2    Slater, E.C.3
  • 32
    • 67651006540 scopus 로고    scopus 로고
    • Breast cancer migration and invasion de pend on proteasome de gradation of regulator of G-protein signaling 4
    • Xie Y, Wolff DW, Wei T, Wang B, de ng C, Kirui JK et al. Breast cancer migration and invasion de pend on proteasome de gradation of regulator of G-protein signaling 4. Cancer Res 2009; 69: 5743-5751.
    • (2009) Cancer Res , vol.69 , pp. 5743-5751
    • Xie, Y.1    Wolff, D.W.2    Wei, T.3    Wang, B.4    Deng, C.5    Kirui, J.K.6
  • 34
    • 79953705886 scopus 로고    scopus 로고
    • Choosing between glycolysis and oxidative phosphorylation: A tumors dilemma?
    • Jose C, Bellance N, Rossignol R. Choosing between glycolysis and oxidative phosphorylation: A tumor's dilemma? Biochim Biophys Acta 2011; 1807: 552-561.
    • (2011) Biochim Biophys Acta , vol.1807 , pp. 552-561
    • Jose, C.1    Bellance, N.2    Rossignol, R.3
  • 35
  • 36
    • 84860992007 scopus 로고    scopus 로고
    • Choosing the right cell line for breast cancer research
    • Holliday DL, Speirs V. Choosing the right cell line for breast cancer research. Breast Cancer Res 2011; 13: 215.
    • (2011) Breast Cancer Res , vol.13 , pp. 215
    • Holliday, D.L.1    Speirs, V.2
  • 37
    • 0037093411 scopus 로고    scopus 로고
    • Contribution by different fuels and metabolic pathways to the total ATP turnover of proliferating MCF7 breast cancer cells
    • Guppy M, Leedman P, Zu X, Russell V. Contribution by different fuels and metabolic pathways to the total ATP turnover of proliferating MCF7 breast cancer cells. Biochem J 2002; 364: 309-315.
    • (2002) Biochem J , vol.364 , pp. 309-315
    • Guppy, M.1    Leedman, P.2    Zu, X.3    Russell, V.4
  • 39
    • 2642684554 scopus 로고    scopus 로고
    • Breast cancer cell invasiveness: Correlation with protein kinase C activity and differential regulation by phorbol ester in estrogen receptor-positive and-negative cells
    • Platet N, Prevostel C, de rocq D, Joubert D, Rochefort H, Garcia M. Breast cancer cell invasiveness: Correlation with protein kinase C activity and differential regulation by phorbol ester in estrogen receptor-positive and-negative cells. Int J Cancer 1998; 75: 750-756.
    • (1998) Int J Cancer , vol.75 , pp. 750-756
    • Platet, N.1    Prevostel, C.2    Derocq, D.3    Joubert, D.4    Rochefort, H.5    Garcia, M.6
  • 40
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • de brito OM, Scorrano L. Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature 2008; 456: 605-610.
    • (2008) Nature , vol.456 , pp. 605-610
    • De Brito, O.M.1    Scorrano, L.2
  • 41
    • 0019958455 scopus 로고
    • Organelle-cytoskeleton relationships in fibroblasts: Mitochondria, golgi apparatus, and endoplasmic reticulum in phases of movement and growth
    • Couchman JR, Rees DA. Organelle-cytoskeleton relationships in fibroblasts: Mitochondria, Golgi apparatus, and endoplasmic reticulum in phases of movement and growth. Eur J Cell Biol 1982; 27: 47-54.
    • (1982) Eur J Cell Biol , vol.27 , pp. 47-54
    • Couchman, J.R.1    Rees, D.A.2
  • 42
    • 0032478648 scopus 로고    scopus 로고
    • Is absence of pyruvate de hydrogenase complex in mitochondria a possible explanation of significant aerobic glycolysis by normal human leukocytes?
    • Biswas S, Ray M, Misra S, Dutta DP, Ray S. Is absence of pyruvate De hydrogenase complex in mitochondria a possible explanation of significant aerobic glycolysis by normal human leukocytes? FEBS Lett 1998; 425: 411-414.
    • (1998) FEBS Lett , vol.425 , pp. 411-414
    • Biswas, S.1    Ray, M.2    Misra, S.3    Dutta, D.P.4    Ray, S.5
  • 44
    • 27744542635 scopus 로고    scopus 로고
    • Local calcium transients contribute to disappearance of pFAK, focal complex removal and de adhesion of neuronal growth cones and fibroblasts
    • Conklin MW, Lin MS, Spitzer NC. Local calcium transients contribute to disappearance of pFAK, focal complex removal and de adhesion of neuronal growth cones and fibroblasts. Dev Biol 2005; 287: 201-212.
    • (2005) Dev Biol , vol.287 , pp. 201-212
    • Conklin, M.W.1    Lin, M.S.2    Spitzer, N.C.3
  • 45
    • 0030756973 scopus 로고    scopus 로고
    • Role of actin polymerization and adhesion to extracellular matrix in Rac-and Rho-induced cytoskeletal reorganization
    • Machesky LM, Hall A. Role of actin polymerization and adhesion to extracellular matrix in Rac-and Rho-induced cytoskeletal reorganization. J Cell Biol 1997; 138: 913-926.
    • (1997) J Cell Biol , vol.138 , pp. 913-926
    • Machesky, L.M.1    Hall, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.