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Volumn 19, Issue 12, 2008, Pages 5143-5155

Erratum: The cardiolipin transacylase, tafazzin, associates with two distinct respiratory components providing insight into barth syndrome (Molecular Biology of the Cell (2008) 19 (5143-5155) DOI: 10.1091/mbc.E08-09-0896);The cardiolipin transacylase, tafazzin, associates with two distinct respiratory components providing insight into Barth syndrome

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; CARDIOLIPIN; HOMODIMER; OLIGOMER; PHOSPHOLIPID; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; TAFAZZIN; UNCLASSIFIED DRUG;

EID: 59449108212     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E08-09-0896     Document Type: Erratum
Times cited : (93)

References (53)
  • 1
    • 33845752499 scopus 로고    scopus 로고
    • Comparison of lymphoblast mitochondria from normal subjects and patients with Barth syndrome using electron microscopic tomography
    • Acehan, D., Xu, Y., Stokes, D. L., and Schlame, M. (2007). Comparison of lymphoblast mitochondria from normal subjects and patients with Barth syndrome using electron microscopic tomography. Lab. Invest. 87, 40-48.
    • (2007) Lab. Invest , vol.87 , pp. 40-48
    • Acehan, D.1    Xu, Y.2    Stokes, D.L.3    Schlame, M.4
  • 8
    • 0022427458 scopus 로고
    • ADP/ATP carrier protein from beef heart mitochondria has high amounts of tightly bound cardiolipin, as revealed by 31P nuclear magnetic resonance
    • Beyer, K., and Klingenberg, M. (1985). ADP/ATP carrier protein from beef heart mitochondria has high amounts of tightly bound cardiolipin, as revealed by 31P nuclear magnetic resonance. Biochemistry 24, 3821-3826.
    • (1985) Biochemistry , vol.24 , pp. 3821-3826
    • Beyer, K.1    Klingenberg, M.2
  • 9
    • 0032570865 scopus 로고    scopus 로고
    • The respiratory chain in yeast behaves as a single functional unit
    • Boumans, H., Grivell, L. A., and Berden, J. A. (1998). The respiratory chain in yeast behaves as a single functional unit. J. Biol. Chem. 273, 4872-4877.
    • (1998) J. Biol. Chem , vol.273 , pp. 4872-4877
    • Boumans, H.1    Grivell, L.A.2    Berden, J.A.3
  • 10
    • 27644437287 scopus 로고    scopus 로고
    • Taz1, an outer mitochondrial membrane protein, affects stability and assembly of inner membrane protein complexes: Implications for Barth Syndrome
    • Brandner, K., Mick, D. U., Frazier, A. E., Taylor, R. D., Meisinger, C., and Rehling, P. (2005). Taz1, an outer mitochondrial membrane protein, affects stability and assembly of inner membrane protein complexes: implications for Barth Syndrome. Mol. Biol. Cell 16, 5202-5214.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5202-5214
    • Brandner, K.1    Mick, D.U.2    Frazier, A.E.3    Taylor, R.D.4    Meisinger, C.5    Rehling, P.6
  • 11
    • 42549160157 scopus 로고    scopus 로고
    • Loss of tafazzin in yeast leads to increased oxidative stress during respiratory growth
    • Chen, S., He, Q., and Greenberg, M. L. (2008). Loss of tafazzin in yeast leads to increased oxidative stress during respiratory growth. Mol. Microbiol. 68, 1061-1072.
    • (2008) Mol. Microbiol , vol.68 , pp. 1061-1072
    • Chen, S.1    He, Q.2    Greenberg, M.L.3
  • 12
    • 27544473312 scopus 로고    scopus 로고
    • Membrane hemifusion: Crossing a chasm in two leaps
    • Chernomordik, L. V., and Kozlov, M. M. (2005). Membrane hemifusion: crossing a chasm in two leaps. Cell 123, 375-382.
    • (2005) Cell , vol.123 , pp. 375-382
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 15
    • 33746606474 scopus 로고    scopus 로고
    • Mitochondrial mislocalization and altered assembly of a cluster of Barth syndrome mutant tafazzins
    • Claypool, S. M., McCaffery, J. M., and Koehler, C. M. (2006). Mitochondrial mislocalization and altered assembly of a cluster of Barth syndrome mutant tafazzins. J. Cell Biol. 174, 379-390.
    • (2006) J. Cell Biol , vol.174 , pp. 379-390
    • Claypool, S.M.1    McCaffery, J.M.2    Koehler, C.M.3
  • 16
    • 51649096941 scopus 로고    scopus 로고
    • Cardiolipin defines the interactome of the major ADP/ATP carrier protein of the mitochondrial inner membrane
    • Claypool, S. M., Oktay, Y., Boontheung, P., Loo, J. A., and Koehler, C. M. (2008). Cardiolipin defines the interactome of the major ADP/ATP carrier protein of the mitochondrial inner membrane. J. Cell Biol. 182, 937-950.
    • (2008) J. Cell Biol , vol.182 , pp. 937-950
    • Claypool, S.M.1    Oktay, Y.2    Boontheung, P.3    Loo, J.A.4    Koehler, C.M.5
  • 17
    • 0343964750 scopus 로고
    • Tightly associated cardiolipin in the bovine heart mitochondrial ATP synthase as analyzed by 31P nuclear magnetic resonance spectroscopy
    • Eble, K. S., Coleman, W. B., Hantgan, R. R., and Cunningham, C. C. (1990). Tightly associated cardiolipin in the bovine heart mitochondrial ATP synthase as analyzed by 31P nuclear magnetic resonance spectroscopy. J. Biol. Chem. 265, 19434-19440.
    • (1990) J. Biol. Chem , vol.265 , pp. 19434-19440
    • Eble, K.S.1    Coleman, W.B.2    Hantgan, R.R.3    Cunningham, C.C.4
  • 18
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product
    • Evan, G. I., Lewis, G. K., Ramsay, G., and Bishop, J. M. (1985). Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell Biol. 5, 3610-3616.
    • (1985) Mol. Cell Biol , vol.5 , pp. 3610-3616
    • Evan, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 19
    • 44349182647 scopus 로고    scopus 로고
    • Yeast cells depleted in Atp14p Fail to assemble Atp6p within the ATP synthase and exhibit altered mitochondrial cristae morphology
    • Goyon, V., Fronzes, R., Salin, B., di-Rago, J.-P., Velours, J., and Brethes, D. (2008). Yeast cells depleted in Atp14p Fail to assemble Atp6p within the ATP synthase and exhibit altered mitochondrial cristae morphology. J. Biol. Chem. 283, 9749-9758.
    • (2008) J. Biol. Chem , vol.283 , pp. 9749-9758
    • Goyon, V.1    Fronzes, R.2    Salin, B.3    di-Rago, J.-P.4    Velours, J.5    Brethes, D.6
  • 21
    • 0037174138 scopus 로고    scopus 로고
    • Cardiolipin: A proton trap for oxidative phosphorylation
    • Haines, T. H., and Dencher, N. A. (2002). Cardiolipin: a proton trap for oxidative phosphorylation. FEBS Lett. 528, 35-39.
    • (2002) FEBS Lett , vol.528 , pp. 35-39
    • Haines, T.H.1    Dencher, N.A.2
  • 22
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R. (1989). Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 23
    • 0028084988 scopus 로고
    • The reconstituted ADP/ATP carrier activity has an absolute requirement for cardiolipin as shown in cysteine mutants
    • Hoffmann, B., Stockl, A., Schlame, M., Beyer, K., and Klingenberg, M. (1994). The reconstituted ADP/ATP carrier activity has an absolute requirement for cardiolipin as shown in cysteine mutants. J. Biol. Chem. 269, 1940-1944.
    • (1994) J. Biol. Chem , vol.269 , pp. 1940-1944
    • Hoffmann, B.1    Stockl, A.2    Schlame, M.3    Beyer, K.4    Klingenberg, M.5
  • 24
    • 0038584862 scopus 로고    scopus 로고
    • Protection from inactivation of the adenine nucleotide translocator during hypoglycaemia-induced apoptosis by mitochondrial phospholipid hydroperoxide glutathione peroxidase
    • Imai, H., Koumura, T., Nakajima, R., Nomura, K., and Nakagawa, Y. (2003). Protection from inactivation of the adenine nucleotide translocator during hypoglycaemia-induced apoptosis by mitochondrial phospholipid hydroperoxide glutathione peroxidase. Biochem. J. 371, 799-809.
    • (2003) Biochem. J , vol.371 , pp. 799-809
    • Imai, H.1    Koumura, T.2    Nakajima, R.3    Nomura, K.4    Nakagawa, Y.5
  • 25
    • 0034698098 scopus 로고    scopus 로고
    • Absence of cardiolipin in the crd1 null mutant results in decreased mitochondrial membrane potential and reduced mitochondrial function
    • Jiang, F., Ryan, M. T., Schlame, M., Zhao, M., Gu, Z., Klingenberg, M., Pfanner, N., and Greenberg, M. L. (2000). Absence of cardiolipin in the crd1 null mutant results in decreased mitochondrial membrane potential and reduced mitochondrial function. J. Biol. Chem. 275, 22387-22394.
    • (2000) J. Biol. Chem , vol.275 , pp. 22387-22394
    • Jiang, F.1    Ryan, M.T.2    Schlame, M.3    Zhao, M.4    Gu, Z.5    Klingenberg, M.6    Pfanner, N.7    Greenberg, M.L.8
  • 26
    • 33747593581 scopus 로고    scopus 로고
    • A zebrafish model of human Barth syndrome reveals the essential role of tafazzin in cardiac development and function
    • Khuchua, Z., Yue, Z., Batts, L., and Strauss, A. W. (2006). A zebrafish model of human Barth syndrome reveals the essential role of tafazzin in cardiac development and function. Circ. Res. 99, 201-208.
    • (2006) Circ. Res , vol.99 , pp. 201-208
    • Khuchua, Z.1    Yue, Z.2    Batts, L.3    Strauss, A.W.4
  • 27
    • 33746327466 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain supercomplexes are destabilized in Barth Syndrome patients
    • McKenzie, M., Lazarou, M., Thorburn, D. R., and Ryan, M. T. (2006). Mitochondrial respiratory chain supercomplexes are destabilized in Barth Syndrome patients. J. Mol. Biol. 361, 462-469.
    • (2006) J. Mol. Biol , vol.361 , pp. 462-469
    • McKenzie, M.1    Lazarou, M.2    Thorburn, D.R.3    Ryan, M.T.4
  • 28
    • 27544484570 scopus 로고    scopus 로고
    • Structural basis for lipid-mediated interactions between mitochondrial ADP/ATP carrier monomers
    • Nury, H., Dahout-Gonzalez, C., Trezeguet, V., Lauquin, G., Brandolin, G., and Pebay-Peyroula, E. (2005). Structural basis for lipid-mediated interactions between mitochondrial ADP/ATP carrier monomers. FEBS Lett. 579, 6031-6036.
    • (2005) FEBS Lett , vol.579 , pp. 6031-6036
    • Nury, H.1    Dahout-Gonzalez, C.2    Trezeguet, V.3    Lauquin, G.4    Brandolin, G.5    Pebay-Peyroula, E.6
  • 29
    • 0032861535 scopus 로고    scopus 로고
    • Membrane fusion and the lamellar-to-inverted-hexagonal phase transition in cardiolipin vesicle systems induced by divalent cations
    • Ortiz, A., Killian, J. A., Verkleij, A. J., and Wilschut, J. (1999). Membrane fusion and the lamellar-to-inverted-hexagonal phase transition in cardiolipin vesicle systems induced by divalent cations. Biophys. J. 77, 2003-2014.
    • (1999) Biophys. J , vol.77 , pp. 2003-2014
    • Ortiz, A.1    Killian, J.A.2    Verkleij, A.J.3    Wilschut, J.4
  • 30
    • 0037225928 scopus 로고    scopus 로고
    • Choline head groups stabilize the matrix loop regions of the ATP/ADP carrier ScAAC2
    • Panneels, V., Schussler, U., Costagliola, S., and Sinning, I. (2003). Choline head groups stabilize the matrix loop regions of the ATP/ADP carrier ScAAC2. Biochem. Biophys. Res. Commun. 300, 65-74.
    • (2003) Biochem. Biophys. Res. Commun , vol.300 , pp. 65-74
    • Panneels, V.1    Schussler, U.2    Costagliola, S.3    Sinning, I.4
  • 33
    • 33745851905 scopus 로고    scopus 로고
    • Toward the complete yeast mitochondrial proteome: Multidimensional separation techniques for mitochondrial proteomics
    • Reinders, J., Zahedi, R. P., Pfanner, N., Meisinger, C., and Sickmann, A. (2006). Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J. Proteome Res. 5, 1543-1554.
    • (2006) J. Proteome Res , vol.5 , pp. 1543-1554
    • Reinders, J.1    Zahedi, R.P.2    Pfanner, N.3    Meisinger, C.4    Sickmann, A.5
  • 34
    • 0029954332 scopus 로고    scopus 로고
    • Multilamellar endosome-like compartment accumulates in the yeast vps28 vacuolar protein sorting mutant
    • Rieder, S. E., Banta, L. M., Kohrer, K., McCaffery, J. M., and Emr, S. D. (1996). Multilamellar endosome-like compartment accumulates in the yeast vps28 vacuolar protein sorting mutant. Mol. Biol. Cell 7, 985-999.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 985-999
    • Rieder, S.E.1    Banta, L.M.2    Kohrer, K.3    McCaffery, J.M.4    Emr, S.D.5
  • 35
    • 0027497625 scopus 로고
    • Cardiolipin is synthesized on the matrix side of the inner membrane in rat liver mitochondria
    • Schlame, M., and Haldar, D. (1993). Cardiolipin is synthesized on the matrix side of the inner membrane in rat liver mitochondria. J. Biol. Chem. 268, 74-79.
    • (1993) J. Biol. Chem , vol.268 , pp. 74-79
    • Schlame, M.1    Haldar, D.2
  • 37
    • 33749061065 scopus 로고    scopus 로고
    • Barth syndrome, a human disorder of cardiolipin metabolism
    • Schlame, M., and Ren, M. (2006). Barth syndrome, a human disorder of cardiolipin metabolism. FEBS Lett. 580, 5450-5455.
    • (2006) FEBS Lett , vol.580 , pp. 5450-5455
    • Schlame, M.1    Ren, M.2
  • 39
    • 0034193996 scopus 로고    scopus 로고
    • The biosynthesis and functional role of cardiolipin
    • Schlame, M., Rua, D., and Greenberg, M. L. (2000). The biosynthesis and functional role of cardiolipin. Prog. Lipid Res. 39, 257-288.
    • (2000) Prog. Lipid Res , vol.39 , pp. 257-288
    • Schlame, M.1    Rua, D.2    Greenberg, M.L.3
  • 40
    • 0033539647 scopus 로고    scopus 로고
    • Phospholipase A(2) digestion of cardiolipin bound to bovine cytochrome c oxidase alters both activity and quaternary structure
    • Sedlak, E., and Robinson, N. C. (1999). Phospholipase A(2) digestion of cardiolipin bound to bovine cytochrome c oxidase alters both activity and quaternary structure. Biochemistry 38, 14966-14972.
    • (1999) Biochemistry , vol.38 , pp. 14966-14972
    • Sedlak, E.1    Robinson, N.C.2
  • 41
    • 0025871358 scopus 로고
    • Mitochondrial membrane contact sites of yeast. Characterization of lipid components and possible involvement in intramitochondrial translocation of phospholipids
    • Simbeni, R., Pon, L., Zinser, E., Paltauf, F., and Daum, G. (1991). Mitochondrial membrane contact sites of yeast. Characterization of lipid components and possible involvement in intramitochondrial translocation of phospholipids. J. Biol. Chem. 266, 10047-10049.
    • (1991) J. Biol. Chem , vol.266 , pp. 10047-10049
    • Simbeni, R.1    Pon, L.2    Zinser, E.3    Paltauf, F.4    Daum, G.5
  • 42
    • 0024294841 scopus 로고
    • Lipid topology and physical properties of the outer mitochondrial membrane of the yeast, Saccharomyces cerevisiae
    • Sperka-Gottlieb, C. D., Hermetter, A., Paltauf, F., and Daum, G. (1988). Lipid topology and physical properties of the outer mitochondrial membrane of the yeast, Saccharomyces cerevisiae. Biochim. Biophys. Acta 946, 227-234.
    • (1988) Biochim. Biophys. Acta , vol.946 , pp. 227-234
    • Sperka-Gottlieb, C.D.1    Hermetter, A.2    Paltauf, F.3    Daum, G.4
  • 43
    • 41949123425 scopus 로고    scopus 로고
    • Dimer ribbons of ATP synthase shape the inner mitochondrial membrane
    • Strauss, M., Hofhaus, G., Schroder, R. R., and Kuhlbrandt, W. (2008). Dimer ribbons of ATP synthase shape the inner mitochondrial membrane. EMBO J. 27, 1154-1160.
    • (2008) EMBO J , vol.27 , pp. 1154-1160
    • Strauss, M.1    Hofhaus, G.2    Schroder, R.R.3    Kuhlbrandt, W.4
  • 44
    • 18844391214 scopus 로고    scopus 로고
    • Ypr140wp, 'the yeast tafazzin', displays a mitochondrial lysophosphatidylcholine (lyso-PC) acyltransferase activity related to triacylglycerol and mitochondrial lipid synthesis
    • Testet, E., Laroche-Traineau, J., Noubhani, A., Coulon, D., Bunoust, O., Camougrand, N., Manon, S., Lessire, R., and Bessoule, J. J. (2005). Ypr140wp, 'the yeast tafazzin', displays a mitochondrial lysophosphatidylcholine (lyso-PC) acyltransferase activity related to triacylglycerol and mitochondrial lipid synthesis. Biochem. J. 387, 617-626.
    • (2005) Biochem. J , vol.387 , pp. 617-626
    • Testet, E.1    Laroche-Traineau, J.2    Noubhani, A.3    Coulon, D.4    Bunoust, O.5    Camougrand, N.6    Manon, S.7    Lessire, R.8    Bessoule, J.J.9
  • 45
    • 24944563130 scopus 로고    scopus 로고
    • Monolysocardiolipins accumulate in Barth syndrome but do not lead to enhanced apoptosis
    • Valianpour, F. et al. (2005). Monolysocardiolipins accumulate in Barth syndrome but do not lead to enhanced apoptosis. J. Lipid Res. 46, 1182-1195.
    • (2005) J. Lipid Res , vol.46 , pp. 1182-1195
    • Valianpour, F.1
  • 46
    • 0036721531 scopus 로고    scopus 로고
    • Quantitative and compositional study of cardiolipin in platelets by electrospray ionization mass spectrometry: Application for the identification of Barth syndrome patients
    • Valianpour, F., Wanders, R. J., Barth, P. G., Overmars, H., and van Gennip, A. H. (2002). Quantitative and compositional study of cardiolipin in platelets by electrospray ionization mass spectrometry: application for the identification of Barth syndrome patients. Clin. Chem. 48, 1390-1397.
    • (2002) Clin. Chem , vol.48 , pp. 1390-1397
    • Valianpour, F.1    Wanders, R.J.2    Barth, P.G.3    Overmars, H.4    van Gennip, A.H.5
  • 47
    • 0242322008 scopus 로고    scopus 로고
    • Only one splice variant of the human TAZ gene encodes a functional protein with a role in cardiolipin metabolism
    • Vaz, F. M., Houtkooper, R. H., Valianpour, F., Barth, P. G., and Wanders, R. J. (2003). Only one splice variant of the human TAZ gene encodes a functional protein with a role in cardiolipin metabolism. J. Biol. Chem. 278, 43089-43094.
    • (2003) J. Biol. Chem , vol.278 , pp. 43089-43094
    • Vaz, F.M.1    Houtkooper, R.H.2    Valianpour, F.3    Barth, P.G.4    Wanders, R.J.5
  • 49
    • 0028676232 scopus 로고
    • New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae
    • Wach, A., Brachat, A., Pohlmann, R., and Philippsen, P. (1994). New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae. Yeast 10, 1793-1808.
    • (1994) Yeast , vol.10 , pp. 1793-1808
    • Wach, A.1    Brachat, A.2    Pohlmann, R.3    Philippsen, P.4
  • 51
    • 33845983684 scopus 로고    scopus 로고
    • The enzymatic function of tafazzin
    • Xu, Y., Malhotra, A., Ren, M., and Schlame, M. (2006b). The enzymatic function of tafazzin. J. Biol. Chem. 281, 39217-39224.
    • (2006) J. Biol. Chem , vol.281 , pp. 39217-39224
    • Xu, Y.1    Malhotra, A.2    Ren, M.3    Schlame, M.4
  • 52
    • 0037113864 scopus 로고    scopus 로고
    • Gluing the respiratory chain together. Cardiolipin is required for supercomplex formation in the inner mitochondrial membrane
    • Zhang, M., Mileykovskaya, E., and Dowhan, W. (2002). Gluing the respiratory chain together. Cardiolipin is required for supercomplex formation in the inner mitochondrial membrane. J. Biol. Chem. 277, 43553-43556.
    • (2002) J. Biol. Chem , vol.277 , pp. 43553-43556
    • Zhang, M.1    Mileykovskaya, E.2    Dowhan, W.3
  • 53
    • 23844540312 scopus 로고    scopus 로고
    • Cardiolipin is essential for organization of complexes III and IV into a supercomplex in intact yeast mitochondria
    • Zhang, M., Mileykovskaya, E., and Dowhan, W. (2005). Cardiolipin is essential for organization of complexes III and IV into a supercomplex in intact yeast mitochondria. J. Biol. Chem. 280, 29403-29408.
    • (2005) J. Biol. Chem , vol.280 , pp. 29403-29408
    • Zhang, M.1    Mileykovskaya, E.2    Dowhan, W.3


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