메뉴 건너뛰기




Volumn 9, Issue 7, 2014, Pages

Specific interaction with cardiolipin triggers functional activation of dynamin-related protein 1

Author keywords

[No Author keywords available]

Indexed keywords

CARDIOLIPIN; DYNAMIN; DYNAMIN RELATED PROTEIN 1; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; LIPOSOME; LYSINE; UNCLASSIFIED DRUG; LIPID BILAYER; MICROTUBULE ASSOCIATED PROTEIN; MITOCHONDRIAL PROTEIN;

EID: 84904580385     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0102738     Document Type: Article
Times cited : (132)

References (72)
  • 1
    • 0033525924 scopus 로고    scopus 로고
    • Oxidative phosphorylation at the fin de siecle
    • Saraste M (1999) Oxidative phosphorylation at the fin de siecle. Science 283: 1488-1493.
    • (1999) Science , vol.283 , pp. 1488-1493
    • Saraste, M.1
  • 3
    • 84858376953 scopus 로고    scopus 로고
    • Mitochondria: In sickness and in health
    • Nunnari J, Suomalainen A (2012) Mitochondria: in sickness and in health. Cell 148: 1145-1159.
    • (2012) Cell , vol.148 , pp. 1145-1159
    • Nunnari, J.1    Suomalainen, A.2
  • 4
    • 42049092501 scopus 로고    scopus 로고
    • Mitochondrial dynamics: To be in good shape to survive
    • DOI 10.2174/156652408783769625
    • Herzig S, Martinou JC (2008) Mitochondrial dynamics: to be in good shape to survive. Curr Mol Med 8: 131-137. (Pubitemid 351516832)
    • (2008) Current Molecular Medicine , vol.8 , Issue.2 , pp. 131-137
    • Herzig, S.1    Martinou, J.-C.2
  • 5
    • 84865544952 scopus 로고    scopus 로고
    • Mitochondrial fission, fusion, and stress
    • Youle RJ, van der Bliek AM (2012) Mitochondrial fission, fusion, and stress. Science 337: 1062-1065.
    • (2012) Science , vol.337 , pp. 1062-1065
    • Youle, R.J.1    Van Der Bliek, A.M.2
  • 6
    • 77951896551 scopus 로고    scopus 로고
    • Expression of mitofusin 2(R94Q) in a transgenic mouse leads to Charcot-Marie-Tooth neuropathy type 2A
    • Cartoni R, Arnaud E, Medard JJ, Poirot O, Courvoisier DS, et al. (2010) Expression of mitofusin 2(R94Q) in a transgenic mouse leads to Charcot-Marie-Tooth neuropathy type 2A. Brain 133: 1460-1469.
    • (2010) Brain , vol.133 , pp. 1460-1469
    • Cartoni, R.1    Arnaud, E.2    Medard, J.J.3    Poirot, O.4    Courvoisier, D.S.5
  • 8
    • 0033772264 scopus 로고    scopus 로고
    • OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28
    • Alexander C, Votruba M, Pesch UE, Thiselton DL, Mayer S, et al. (2000) OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28. Nat Genet 26: 211-215.
    • (2000) Nat Genet , vol.26 , pp. 211-215
    • Alexander, C.1    Votruba, M.2    Pesch, U.E.3    Thiselton, D.L.4    Mayer, S.5
  • 10
    • 55749090654 scopus 로고    scopus 로고
    • The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila
    • Deng H, Dodson MW, Huang H, Guo M (2008) The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila. Proc Natl Acad Sci U S A 105: 14503-14508.
    • (2008) Proc Natl Acad Sci U S a , vol.105 , pp. 14503-14508
    • Deng, H.1    Dodson, M.W.2    Huang, H.3    Guo, M.4
  • 11
    • 64249133725 scopus 로고    scopus 로고
    • S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury
    • Cho DH, Nakamura T, Fang J, Cieplak P, Godzik A, et al. (2009) S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury. Science 324: 102-105.
    • (2009) Science , vol.324 , pp. 102-105
    • Cho, D.H.1    Nakamura, T.2    Fang, J.3    Cieplak, P.4    Godzik, A.5
  • 12
    • 34250204271 scopus 로고    scopus 로고
    • The machines that divide and fuse mitochondria
    • Hoppins S, Lackner L, Nunnari J (2007) The machines that divide and fuse mitochondria. Annu Rev Biochem 76: 751-780.
    • (2007) Annu Rev Biochem , vol.76 , pp. 751-780
    • Hoppins, S.1    Lackner, L.2    Nunnari, J.3
  • 13
    • 68149103297 scopus 로고    scopus 로고
    • Mitofusins and OPA1 mediate sequential steps in mitochondrial membrane fusion
    • Song Z, Ghochani M, McCaffery JM, Frey TG, Chan DC (2009) Mitofusins and OPA1 mediate sequential steps in mitochondrial membrane fusion. Mol Biol Cell 20: 3525-3532.
    • (2009) Mol Biol Cell , vol.20 , pp. 3525-3532
    • Song, Z.1    Ghochani, M.2    McCaffery, J.M.3    Frey, T.G.4    Chan, D.C.5
  • 14
    • 0032547754 scopus 로고    scopus 로고
    • A human dynamin-related protein controls the distribution of mitochondria
    • DOI 10.1083/jcb.143.2.351
    • Smirnova E, Shurland DL, Ryazantsev SN, van der Bliek AM (1998) A human dynamin-related protein controls the distribution of mitochondria. J Cell Biol 143: 351-358. (Pubitemid 28487855)
    • (1998) Journal of Cell Biology , vol.143 , Issue.2 , pp. 351-358
    • Smirnova, E.1    Shurland, D.-L.2    Ryazantsev, S.N.3    Van Der, B.A.M.4
  • 15
    • 0035166814 scopus 로고    scopus 로고
    • Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells
    • Smirnova E, Griparic L, Shurland DL, van der Bliek AM (2001) Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells. Mol Biol Cell 12: 2245-2256. (Pubitemid 33051954)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.8 , pp. 2245-2256
    • Smirnova, E.1    Griparic, L.2    Shurland, D.-L.3    Van Der, B.A.M.4
  • 17
    • 68949217889 scopus 로고    scopus 로고
    • Mechanistic analysis of a dynamin effector
    • Lackner LL, Horner JS, Nunnari J (2009) Mechanistic analysis of a dynamin effector. Science 325: 874-877.
    • (2009) Science , vol.325 , pp. 874-877
    • Lackner, L.L.1    Horner, J.S.2    Nunnari, J.3
  • 18
    • 68249087424 scopus 로고    scopus 로고
    • Mitochondrial fission factor Drp1 is essential for embryonic development and synapse formation in mice
    • Ishihara N, Nomura M, Jofuku A, Kato H, Suzuki SO, et al. (2009) Mitochondrial fission factor Drp1 is essential for embryonic development and synapse formation in mice. Nat Cell Biol 11: 958-966.
    • (2009) Nat Cell Biol , vol.11 , pp. 958-966
    • Ishihara, N.1    Nomura, M.2    Jofuku, A.3    Kato, H.4    Suzuki, S.O.5
  • 19
    • 70349944660 scopus 로고    scopus 로고
    • The dynamin-related GTPase Drp1 is required for embryonic and brain development in mice
    • Wakabayashi J, Zhang Z, Wakabayashi N, Tamura Y, Fukaya M, et al. (2009) The dynamin-related GTPase Drp1 is required for embryonic and brain development in mice. J Cell Biol 186: 805-816.
    • (2009) J Cell Biol , vol.186 , pp. 805-816
    • Wakabayashi, J.1    Zhang, Z.2    Wakabayashi, N.3    Tamura, Y.4    Fukaya, M.5
  • 20
    • 79960230433 scopus 로고    scopus 로고
    • Mitochondria in apoptosis: Bcl-2 family members and mitochondrial dynamics
    • Martinou JC, Youle RJ (2011) Mitochondria in apoptosis: Bcl-2 family members and mitochondrial dynamics. Dev Cell 21: 92-101.
    • (2011) Dev Cell , vol.21 , pp. 92-101
    • Martinou, J.C.1    Youle, R.J.2
  • 21
    • 77956634444 scopus 로고    scopus 로고
    • Membrane remodeling induced by the dynamin-related protein Drp1 stimulates Bax oligomerization
    • Montessuit S, Somasekharan SP, Terrones O, Lucken-Ardjomande S, Herzig S, et al. (2010) Membrane remodeling induced by the dynamin-related protein Drp1 stimulates Bax oligomerization. Cell 142: 889-901.
    • (2010) Cell , vol.142 , pp. 889-901
    • Montessuit, S.1    Somasekharan, S.P.2    Terrones, O.3    Lucken-Ardjomande, S.4    Herzig, S.5
  • 22
    • 33745699393 scopus 로고    scopus 로고
    • OPA1 controls apoptotic cristae remodeling independently from mitochondrial fusion
    • Frezza C, Cipolat S, Martins de Brito O, Micaroni M, Beznoussenko GV, et al. (2006) OPA1 controls apoptotic cristae remodeling independently from mitochondrial fusion. Cell 126: 177-189.
    • (2006) Cell , vol.126 , pp. 177-189
    • Frezza, C.1    Cipolat, S.2    Martins De Brito, O.3    Micaroni, M.4    Beznoussenko, G.V.5
  • 23
    • 49349112331 scopus 로고    scopus 로고
    • Opa1-mediated cristae opening is Bax/Bak and BH3 dependent, required for apoptosis, and independent of Bak oligomerization
    • Yamaguchi R, Lartigue L, Perkins G, Scott RT, Dixit A, et al. (2008) Opa1-mediated cristae opening is Bax/Bak and BH3 dependent, required for apoptosis, and independent of Bak oligomerization. Mol Cell 31: 557-569.
    • (2008) Mol Cell , vol.31 , pp. 557-569
    • Yamaguchi, R.1    Lartigue, L.2    Perkins, G.3    Scott, R.T.4    Dixit, A.5
  • 24
    • 84877612740 scopus 로고    scopus 로고
    • Structural insights into oligomerization and mitochondrial remodelling of dynamin 1-like protein
    • Frohlich C, Grabiger S, Schwefel D, Faelber K, Rosenbaum E, et al. (2013) Structural insights into oligomerization and mitochondrial remodelling of dynamin 1-like protein. EMBO J.
    • (2013) EMBO J
    • Frohlich, C.1    Grabiger, S.2    Schwefel, D.3    Faelber, K.4    Rosenbaum, E.5
  • 26
    • 84872769447 scopus 로고    scopus 로고
    • An actin-dependent step in mitochondrial fission mediated by the ER-associated formin INF2
    • Korobova F, Ramabhadran V, Higgs HN (2013) An actin-dependent step in mitochondrial fission mediated by the ER-associated formin INF2. Science 339: 464-467.
    • (2013) Science , vol.339 , pp. 464-467
    • Korobova, F.1    Ramabhadran, V.2    Higgs, H.N.3
  • 28
    • 70350543964 scopus 로고    scopus 로고
    • SUMOylation of the mitochondrial fission protein Drp1 occurs at multiple nonconsensus sites within the B domain and is linked to its activity cycle
    • Figueroa-Romero C, Iniguez-Lluhi JA, Stadler J, Chang CR, Arnoult D, et al. (2009) SUMOylation of the mitochondrial fission protein Drp1 occurs at multiple nonconsensus sites within the B domain and is linked to its activity cycle. FASEB J 23: 3917-3927.
    • (2009) FASEB J , vol.23 , pp. 3917-3927
    • Figueroa-Romero, C.1    Iniguez-Lluhi, J.A.2    Stadler, J.3    Chang, C.R.4    Arnoult, D.5
  • 29
    • 84878597289 scopus 로고    scopus 로고
    • SENP3-mediated deSUMOylation of dynamin-related protein 1 promotes cell death following ischaemia
    • Guo C, Hildick KL, Luo J, Dearden L, Wilkinson KA, et al. (2013) SENP3-mediated deSUMOylation of dynamin-related protein 1 promotes cell death following ischaemia. EMBO J.
    • (2013) EMBO J
    • Guo, C.1    Hildick, K.L.2    Luo, J.3    Dearden, L.4    Wilkinson, K.A.5
  • 30
    • 33749253910 scopus 로고    scopus 로고
    • MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change mitochondrial morphology
    • DOI 10.1038/sj.embor.7400790, PII 7400790
    • Nakamura N, Kimura Y, Tokuda M, Honda S, Hirose S (2006) MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change mitochondrial morphology. EMBO Rep 7: 1019-1022. (Pubitemid 44480517)
    • (2006) EMBO Reports , vol.7 , Issue.10 , pp. 1019-1022
    • Nakamura, N.1    Kimura, Y.2    Tokuda, M.3    Honda, S.4    Hirose, S.5
  • 31
    • 84865457924 scopus 로고    scopus 로고
    • Modulation of dynamin-related protein 1 (DRP1) function by increased O-linked-beta-N-acetylglucosamine modification (O-GlcNAc) in cardiac myocytes
    • Gawlowski T, Suarez J, Scott B, Torres-Gonzalez M, Wang H, et al. (2012) Modulation of dynamin-related protein 1 (DRP1) function by increased O-linked-beta-N-acetylglucosamine modification (O-GlcNAc) in cardiac myocytes. J Biol Chem 287: 30024-30034.
    • (2012) J Biol Chem , vol.287 , pp. 30024-30034
    • Gawlowski, T.1    Suarez, J.2    Scott, B.3    Torres-Gonzalez, M.4    Wang, H.5
  • 32
    • 77955298543 scopus 로고    scopus 로고
    • Dynamic regulation of mitochondrial fission through modification of the dynamin-related protein Drp1
    • Chang CR, Blackstone C (2010) Dynamic regulation of mitochondrial fission through modification of the dynamin-related protein Drp1. Ann N Y Acad Sci 1201: 34-39.
    • (2010) Ann N Y Acad Sci , vol.1201 , pp. 34-39
    • Chang, C.R.1    Blackstone, C.2
  • 33
    • 84875581921 scopus 로고    scopus 로고
    • Fis1 acts as mitochondrial recruitment factor for TBC1D15 that involved in regulation of mitochondrial morphology
    • Onoue K, Jofuku A, Ban-Ishihara R, Ishihara T, Maeda M, et al. (2012) Fis1 acts as mitochondrial recruitment factor for TBC1D15 that involved in regulation of mitochondrial morphology. J Cell Sci.
    • (2012) J Cell Sci
    • Onoue, K.1    Jofuku, A.2    Ban-Ishihara, R.3    Ishihara, T.4    Maeda, M.5
  • 34
    • 84876066609 scopus 로고    scopus 로고
    • Interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission
    • Koirala S, Guo Q, Kalia R, Bui HT, Eckert DM, et al. (2013) Interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission. Proc Natl Acad Sci U S A 110: E1342-1351.
    • (2013) Proc Natl Acad Sci U S a , vol.110
    • Koirala, S.1    Guo, Q.2    Kalia, R.3    Bui, H.T.4    Eckert, D.M.5
  • 35
    • 78650167618 scopus 로고    scopus 로고
    • Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells
    • Otera H, Wang C, Cleland MM, Setoguchi K, Yokota S, et al. (2010) Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells. J Cell Biol 191: 1141-1158.
    • (2010) J Cell Biol , vol.191 , pp. 1141-1158
    • Otera, H.1    Wang, C.2    Cleland, M.M.3    Setoguchi, K.4    Yokota, S.5
  • 37
    • 77956876861 scopus 로고    scopus 로고
    • Dynamin GTPase regulation is altered by PH domain mutations found in centronuclear myopathy patients
    • Kenniston JA, Lemmon MA (2010) Dynamin GTPase regulation is altered by PH domain mutations found in centronuclear myopathy patients. EMBO J 29: 3054-3067.
    • (2010) EMBO J , vol.29 , pp. 3054-3067
    • Kenniston, J.A.1    Lemmon, M.A.2
  • 38
  • 39
    • 77953526521 scopus 로고    scopus 로고
    • OPA1 disease alleles causing dominant optic atrophy have defects in cardiolipin-stimulated GTP hydrolysis and membrane tubulation
    • Ban T, Heymann JA, Song Z, Hinshaw JE, Chan DC (2010) OPA1 disease alleles causing dominant optic atrophy have defects in cardiolipin-stimulated GTP hydrolysis and membrane tubulation. Hum Mol Genet 19: 2113-2122.
    • (2010) Hum Mol Genet , vol.19 , pp. 2113-2122
    • Ban, T.1    Heymann, J.A.2    Song, Z.3    Hinshaw, J.E.4    Chan, D.C.5
  • 40
    • 70349930116 scopus 로고    scopus 로고
    • Coassembly of Mgm1 isoforms requires cardiolipin and mediates mitochondrial inner membrane fusion
    • DeVay RM, Dominguez-Ramirez L, Lackner LL, Hoppins S, Stahlberg H, et al. (2009) Coassembly of Mgm1 isoforms requires cardiolipin and mediates mitochondrial inner membrane fusion. J Cell Biol 186: 793-803.
    • (2009) J Cell Biol , vol.186 , pp. 793-803
    • DeVay, R.M.1    Dominguez-Ramirez, L.2    Lackner, L.L.3    Hoppins, S.4    Stahlberg, H.5
  • 41
    • 70350418769 scopus 로고    scopus 로고
    • Phospholipid association is essential for dynamin-related protein Mgm1 to function in mitochondrial membrane fusion
    • Rujiviphat J, Meglei G, Rubinstein JL, McQuibban GA (2009) Phospholipid association is essential for dynamin-related protein Mgm1 to function in mitochondrial membrane fusion. J Biol Chem 284: 28682-28686.
    • (2009) J Biol Chem , vol.284 , pp. 28682-28686
    • Rujiviphat, J.1    Meglei, G.2    Rubinstein, J.L.3    McQuibban, G.A.4
  • 42
    • 78651287877 scopus 로고    scopus 로고
    • Making heads or tails of phospholipids in mitochondria
    • Osman C, Voelker DR, Langer T (2011) Making heads or tails of phospholipids in mitochondria. J Cell Biol 192: 7-16.
    • (2011) J Cell Biol , vol.192 , pp. 7-16
    • Osman, C.1    Voelker, D.R.2    Langer, T.3
  • 43
    • 84855581252 scopus 로고    scopus 로고
    • The complexity of cardiolipin in health and disease
    • Claypool SM, Koehler CM (2012) The complexity of cardiolipin in health and disease. Trends Biochem Sci 37: 32-41.
    • (2012) Trends Biochem Sci , vol.37 , pp. 32-41
    • Claypool, S.M.1    Koehler, C.M.2
  • 46
    • 42149094346 scopus 로고    scopus 로고
    • Contributions to Bax insertion and oligomerization of lipids of the mitochondrial outer membrane
    • DOI 10.1038/cdd.2008.9, PII CDD20089
    • Lucken-Ardjomande S, Montessuit S, Martinou JC (2008) Contributions to Bax insertion and oligomerization of lipids of the mitochondrial outer membrane. Cell Death Differ 15: 929-937. (Pubitemid 351524434)
    • (2008) Cell Death and Differentiation , vol.15 , Issue.5 , pp. 929-937
    • Lucken-Ardjomande, S.1    Montessuit, S.2    Martinou, J.-C.3
  • 47
    • 0023047980 scopus 로고
    • Vesicles of variable sizes produced by a rapid extrusion procedure
    • Mayer LD, Hope MJ, Cullis PR (1986) Vesicles of variable sizes produced by a rapid extrusion procedure. Biochim Biophys Acta 858: 161-168.
    • (1986) Biochim Biophys Acta , vol.858 , pp. 161-168
    • Mayer, L.D.1    Hope, M.J.2    Cullis, P.R.3
  • 48
    • 70449232257 scopus 로고
    • Colorimetric assay methods for free and phosphorylated glyceric acids
    • Bartlett GR (1959) Colorimetric assay methods for free and phosphorylated glyceric acids. J Biol Chem 234: 469-471.
    • (1959) J Biol Chem , vol.234 , pp. 469-471
    • Bartlett, G.R.1
  • 49
    • 30544447100 scopus 로고    scopus 로고
    • Robust colorimetric assays for dynamin's basal and stimulated GTPase activities
    • DOI 10.1016/S0076-6879(05)04005-X, PII S0076687905040437, 43, GTPases Regulating Membrane Dynamics
    • Leonard M, Song BD, Ramachandran R, Schmid SL (2005) Robust colorimetric assays for dynamin's basal and stimulated GTPase activities. Methods Enzymol 404: 490-503. (Pubitemid 43082009)
    • (2006) Methods in Enzymology , vol.404 , pp. 490-503
    • Leonard, M.1    Doo, S.B.2    Ramachandran, R.3    Schmid, S.L.4
  • 51
    • 42049102578 scopus 로고    scopus 로고
    • Role of phospholipid scramblase 3 in the regulation of tumor necrosis factor-alpha-induced apoptosis
    • DOI 10.1021/bi701962c
    • Liu J, Epand RF, Durrant D, Grossman D, Chi NW, et al. (2008) Role of phospholipid scramblase 3 in the regulation of tumor necrosis factor-alpha-induced apoptosis. Biochemistry 47: 4518-4529. (Pubitemid 351522102)
    • (2008) Biochemistry , vol.47 , Issue.15 , pp. 4518-4529
    • Liu, J.1    Epand, R.F.2    Durrant, D.3    Grossman, D.4    Chi, N.-W.5    Epand, R.M.6    Lee, R.M.7
  • 52
    • 84885176082 scopus 로고    scopus 로고
    • Cardiolipin externalization to the outer mitochondrial membrane acts as an elimination signal for mitophagy in neuronal cells
    • Chu CT, Ji J, Dagda RK, Jiang JF, Tyurina YY, et al. (2013) Cardiolipin externalization to the outer mitochondrial membrane acts as an elimination signal for mitophagy in neuronal cells. Nat Cell Biol 15: 1197-1205.
    • (2013) Nat Cell Biol , vol.15 , pp. 1197-1205
    • Chu, C.T.1    Ji, J.2    Dagda, R.K.3    Jiang, J.F.4    Tyurina, Y.Y.5
  • 53
    • 33747226797 scopus 로고    scopus 로고
    • Real-time monitoring of the membrane-binding and insertion properties of the cholesterol-dependent cytolysin anthrolysin O from Bacillus anthracis
    • Cocklin S, Jost M, Robertson NM, Weeks SD, Weber HW, et al. (2006) Real-time monitoring of the membrane-binding and insertion properties of the cholesterol-dependent cytolysin anthrolysin O from Bacillus anthracis. J Mol Recognit 19: 354-362.
    • (2006) J Mol Recognit , vol.19 , pp. 354-362
    • Cocklin, S.1    Jost, M.2    Robertson, N.M.3    Weeks, S.D.4    Weber, H.W.5
  • 54
    • 49649095215 scopus 로고    scopus 로고
    • Molecular determinants of sphingomyelin specificity of a eukaryotic pore-forming toxin
    • Bakrac B, Gutierrez-Aguirre I, Podlesek Z, Sonnen AF, Gilbert RJ, et al. (2008) Molecular determinants of sphingomyelin specificity of a eukaryotic pore-forming toxin. J Biol Chem 283: 18665-18677.
    • (2008) J Biol Chem , vol.283 , pp. 18665-18677
    • Bakrac, B.1    Gutierrez-Aguirre, I.2    Podlesek, Z.3    Sonnen, A.F.4    Gilbert, R.J.5
  • 55
    • 79953152683 scopus 로고    scopus 로고
    • Reconstitution of proapoptotic BAK function in liposomes reveals a dual role for mitochondrial lipids in the BAK-driven membrane permeabilization process
    • Landeta O, Landajuela A, Gil D, Taneva S, Di Primo C, et al. (2011) Reconstitution of proapoptotic BAK function in liposomes reveals a dual role for mitochondrial lipids in the BAK-driven membrane permeabilization process. J Biol Chem 286: 8213-8230.
    • (2011) J Biol Chem , vol.286 , pp. 8213-8230
    • Landeta, O.1    Landajuela, A.2    Gil, D.3    Taneva, S.4    Di Primo, C.5
  • 56
    • 0033128097 scopus 로고    scopus 로고
    • Nucleotide-dependent conformational changes in dynamin: Evidence for a mechanochemical molecular spring
    • Stowell MH, Marks B, Wigge P, McMahon HT (1999) Nucleotide-dependent conformational changes in dynamin: evidence for a mechanochemical molecular spring. Nat Cell Biol 1: 27-32. (Pubitemid 129495006)
    • (1999) Nature Cell Biology , vol.1 , Issue.1 , pp. 27-32
    • Stowell, M.H.B.1    Marks, B.2    Wigge, P.3    McMahon, H.T.4
  • 57
    • 77953023419 scopus 로고    scopus 로고
    • G domain dimerization controls dynamin's assembly-stimulated GTPase activity
    • Chappie JS, Acharya S, Leonard M, Schmid SL, Dyda F (2010) G domain dimerization controls dynamin's assembly-stimulated GTPase activity. Nature 465: 435-440.
    • (2010) Nature , vol.465 , pp. 435-440
    • Chappie, J.S.1    Acharya, S.2    Leonard, M.3    Schmid, S.L.4    Dyda, F.5
  • 58
    • 84872012439 scopus 로고    scopus 로고
    • A novel motif in the yeast mitochondrial dynamin Dnm1 is essential for adaptor binding and membrane recruitment
    • Bui HT, Karren MA, Bhar D, Shaw JM (2012) A novel motif in the yeast mitochondrial dynamin Dnm1 is essential for adaptor binding and membrane recruitment. J Cell Biol 199: 613-622.
    • (2012) J Cell Biol , vol.199 , pp. 613-622
    • Bui, H.T.1    Karren, M.A.2    Bhar, D.3    Shaw, J.M.4
  • 59
    • 78650987611 scopus 로고    scopus 로고
    • Conformational changes in Dnm1 support a contractile mechanism for mitochondrial fission
    • Mears JA, Lackner LL, Fang S, Ingerman E, Nunnari J, et al. (2011) Conformational changes in Dnm1 support a contractile mechanism for mitochondrial fission. Nat Struct Mol Biol 18: 20-26.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 20-26
    • Mears, J.A.1    Lackner, L.L.2    Fang, S.3    Ingerman, E.4    Nunnari, J.5
  • 60
    • 84858434492 scopus 로고    scopus 로고
    • Allosteric modulation of Drp1 mechanoenzyme assembly and mitochondrial fission by the variable domain
    • Strack S, Cribbs JT (2012) Allosteric modulation of Drp1 mechanoenzyme assembly and mitochondrial fission by the variable domain. J Biol Chem 287: 10990-11001.
    • (2012) J Biol Chem , vol.287 , pp. 10990-11001
    • Strack, S.1    Cribbs, J.T.2
  • 61
    • 80054078476 scopus 로고    scopus 로고
    • Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega
    • Sievers F, Wilm A, Dineen D, Gibson TJ, Karplus K, et al. (2011) Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega. Mol Syst Biol 7: 539.
    • (2011) Mol Syst Biol , vol.7 , pp. 539
    • Sievers, F.1    Wilm, A.2    Dineen, D.3    Gibson, T.J.4    Karplus, K.5
  • 62
    • 84872115717 scopus 로고    scopus 로고
    • Pleckstrin homology (PH) domains and phosphoinositides
    • Lemmon MA (2007) Pleckstrin homology (PH) domains and phosphoinositides. Biochem Soc Symp: 81-93.
    • (2007) Biochem Soc Symp , pp. 81-93
    • Lemmon, M.A.1
  • 64
    • 0028836142 scopus 로고
    • Reversibility of the binding of cytochrome c to liposomes. Implications for lipid-protein interactions
    • Rytomaa M, Kinnunen PK (1995) Reversibility of the binding of cytochrome c to liposomes. Implications for lipid-protein interactions. J Biol Chem 270: 3197-3202.
    • (1995) J Biol Chem , vol.270 , pp. 3197-3202
    • Rytomaa, M.1    Kinnunen, P.K.2
  • 66
    • 58149201240 scopus 로고    scopus 로고
    • Cardiolipin provides an essential activating platform for caspase-8 on mitochondria
    • Gonzalvez F, Schug ZT, Houtkooper RH, MacKenzie ED, Brooks DG, et al. (2008) Cardiolipin provides an essential activating platform for caspase-8 on mitochondria. J Cell Biol 183: 681-696.
    • (2008) J Cell Biol , vol.183 , pp. 681-696
    • Gonzalvez, F.1    Schug, Z.T.2    Houtkooper, R.H.3    MacKenzie, E.D.4    Brooks, D.G.5
  • 67
    • 77949627892 scopus 로고    scopus 로고
    • Mechanistic issues of the interaction of the hairpin-forming domain of tBid with mitochondrial cardiolipin
    • Gonzalvez F, Pariselli F, Jalmar O, Dupaigne P, Sureau F, et al. (2010) Mechanistic issues of the interaction of the hairpin-forming domain of tBid with mitochondrial cardiolipin. PLoS One 5: e9342.
    • (2010) PLoS One , vol.5
    • Gonzalvez, F.1    Pariselli, F.2    Jalmar, O.3    Dupaigne, P.4    Sureau, F.5
  • 68
    • 80054828458 scopus 로고    scopus 로고
    • Stalk domain of the dynamin-like MxA GTPase protein mediates membrane binding and liposome tubulation via the unstructured L4 loop
    • von der Malsburg A, Abutbul-Ionita I, Haller O, Kochs G, Danino D (2011) Stalk domain of the dynamin-like MxA GTPase protein mediates membrane binding and liposome tubulation via the unstructured L4 loop. J Biol Chem 286: 37858-37865.
    • (2011) J Biol Chem , vol.286 , pp. 37858-37865
    • Von Der Malsburg, A.1    Abutbul-Ionita, I.2    Haller, O.3    Kochs, G.4    Danino, D.5
  • 69
    • 84902682341 scopus 로고    scopus 로고
    • A dimeric equilibrium intermediate nucleates Drp1 reassembly on mitochondrial membranes for fission
    • Macdonald PJ, Stepanyants N, Mehrotra N, Mears JA, Qi X, et al. (2014) A dimeric equilibrium intermediate nucleates Drp1 reassembly on mitochondrial membranes for fission. Mol Biol Cell 25: 1905-1915.
    • (2014) Mol Biol Cell , vol.25 , pp. 1905-1915
    • Macdonald, P.J.1    Stepanyants, N.2    Mehrotra, N.3    Mears, J.A.4    Qi, X.5
  • 71
    • 34248182897 scopus 로고    scopus 로고
    • Bax/Bak promote sumoylation of DRP1 and its stable association with mitochondria during apoptotic cell death
    • DOI 10.1083/jcb.200610042
    • Wasiak S, Zunino R, McBride HM (2007) Bax/Bak promote sumoylation of DRP1 and its stable association with mitochondria during apoptotic cell death. J Cell Biol 177: 439-450. (Pubitemid 46718273)
    • (2007) Journal of Cell Biology , vol.177 , Issue.3 , pp. 439-450
    • Wasiak, S.1    Zunino, R.2    McBride, H.M.3
  • 72
    • 0033615965 scopus 로고    scopus 로고
    • Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins
    • Johnson ES, Blobel G (1999) Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins. J Cell Biol 147: 981-994.
    • (1999) J Cell Biol , vol.147 , pp. 981-994
    • Johnson, E.S.1    Blobel, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.