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Volumn 174, Issue 3, 2006, Pages 379-390

Mitochondrial mislocalization and altered assembly of a cluster of Barth syndrome mutant tafazzins

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; MUTANT PROTEIN; PROTEIN TAZ1P; UNCLASSIFIED DRUG;

EID: 33746606474     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200605043     Document Type: Article
Times cited : (123)

References (40)
  • 1
    • 0032934819 scopus 로고    scopus 로고
    • A revised model of the active site of alternative oxidase
    • Andersson, M.E., and P. Nordlund. 1999. A revised model of the active site of alternative oxidase. FEBS Lett. 449:17-22.
    • (1999) FEBS Lett. , vol.449 , pp. 17-22
    • Andersson, M.E.1    Nordlund, P.2
  • 7
    • 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., D.U. Mick, A.E. Frazier, R.D. Taylor, C. Meisinger, and P. Rehling. 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
  • 8
    • 0037008670 scopus 로고    scopus 로고
    • Functional reconstitution of human FcRn in Madin-Darby canine kidney cells requires co-expressed human beta 2-microglobulin
    • Claypool, S.M., B.L. Dickinson, M. Yoshida, W.I. Lencer, and R.S. Blumberg. 2002. Functional reconstitution of human FcRn in Madin-Darby canine kidney cells requires co-expressed human beta 2-microglobulin. J. Biol. Chem. 277:28038-28050.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28038-28050
    • Claypool, S.M.1    Dickinson, B.L.2    Yoshida, M.3    Lencer, W.I.4    Blumberg, R.S.5
  • 9
    • 0020479807 scopus 로고
    • Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria
    • Daum, G., P. Bohni, and G. Schatz. 1982. Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria. J. Biol. Chem. 257:13028-13033.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13028-13033
    • Daum, G.1    Bohni, P.2    Schatz, G.3
  • 10
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product
    • Evan, G.I., G.K. Lewis, G. Ramsay, and J.M. Bishop. 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
  • 11
    • 0035911154 scopus 로고    scopus 로고
    • Connection of the mitochondrial outer and inner membranes by Fzo1 is critical for organellar fusion
    • Fritz, S., D. Rapaport, E. Klanner, W. Neupert, and B. Westermann. 2001. Connection of the mitochondrial outer and inner membranes by Fzo1 is critical for organellar fusion. J. Cell Biol. 152:683-692.
    • (2001) J. Cell Biol. , vol.152 , pp. 683-692
    • Fritz, S.1    Rapaport, D.2    Klanner, E.3    Neupert, W.4    Westermann, B.5
  • 12
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • Fujiki, Y., A.L. Hubbard, S. Fowler, and P.B. Lazarow. 1982. Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. J. Cell Biol. 93:97-102.
    • (1982) J. Cell Biol. , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 13
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz, D., A. St Jean, R.A. Woods, and R.H. Schiestl. 1992. Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res. 20:1425.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1425
    • Gietz, D.1    St Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 14
    • 0026611680 scopus 로고
    • Cytochromes c1 and b2 are sorted to the intermembrane space of yeast mitochondria by a stop-transfer mechanism
    • Glick, B.S., A. Brandt, K. Cunningham, S. Muller, R.L. Hallberg, and G. Schatz. 1992. Cytochromes c1 and b2 are sorted to the intermembrane space of yeast mitochondria by a stop-transfer mechanism. Cell. 69:809-822.
    • (1992) Cell , vol.69 , pp. 809-822
    • Glick, B.S.1    Brandt, A.2    Cunningham, K.3    Muller, S.4    Hallberg, R.L.5    Schatz, G.6
  • 16
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S.N., H.D. Hunt, R.M. Horton, J.K. Pullen, and L.R. Pease. 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
  • 17
    • 7544219638 scopus 로고    scopus 로고
    • New developments in mitochondrial assembly
    • Koehler, C.M. 2004. New developments in mitochondrial assembly. Annu. Rev. Cell Dev. Biol. 20:309-335.
    • (2004) Annu. Rev. Cell Dev. Biol. , vol.20 , pp. 309-335
    • Koehler, C.M.1
  • 18
    • 7244224978 scopus 로고    scopus 로고
    • The human TAZ gene complements mitochondrial dysfunction in the yeast taz1Delta mutant. Implications for Barth syndrome
    • Ma, L., F.M. Vaz, Z. Gu, R.J. Wanders, and M.L. Greenberg. 2004. The human TAZ gene complements mitochondrial dysfunction in the yeast taz1Delta mutant. Implications for Barth syndrome. J. Biol. Chem. 279:44394-44399.
    • (2004) J. Biol. Chem. , vol.279 , pp. 44394-44399
    • Ma, L.1    Vaz, F.M.2    Gu, Z.3    Wanders, R.J.4    Greenberg, M.L.5
  • 19
    • 0031204998 scopus 로고    scopus 로고
    • Barth syndrome may be due to an acyltransferase deficiency
    • Neuwald, A.F. 1997. Barth syndrome may be due to an acyltransferase deficiency. Curr. Biol. 7:R465-R466.
    • (1997) Curr. Biol. , vol.7
    • Neuwald, A.F.1
  • 20
    • 0033802790 scopus 로고    scopus 로고
    • Anchoring of a monotopic membrane protein: The binding of prostaglandin H2 synthase-1 to the surface of a phospholipid bilayer
    • Nina, M., S. Berneche, and B. Roux. 2000. Anchoring of a monotopic membrane protein: the binding of prostaglandin H2 synthase-1 to the surface of a phospholipid bilayer. Eur. Biophys. J. 29:439-454.
    • (2000) Eur. Biophys. J. , vol.29 , pp. 439-454
    • Nina, M.1    Berneche, S.2    Roux, B.3
  • 21
    • 0024829751 scopus 로고
    • Protein import into mitochondria: ATP-dependent protein translocation activity in a submitochondrial fraction enriched in membrane contact sites and specific proteins
    • Pon, L., T. Moll, D. Vestweber, B. Marshallsay, and G. Schatz. 1989. Protein import into mitochondria: ATP-dependent protein translocation activity in a submitochondrial fraction enriched in membrane contact sites and specific proteins. J. Cell Biol. 109:2603-2616.
    • (1989) J. Cell Biol. , vol.109 , pp. 2603-2616
    • Pon, L.1    Moll, T.2    Vestweber, D.3    Marshallsay, B.4    Schatz, G.5
  • 22
    • 0029954332 scopus 로고    scopus 로고
    • Multilamellar endosome-like compartment accumulates in the yeast vps28 vacuolar protein sorting mutant
    • Rieder, S.E., L.M. Banta, K. Kohrer, J.M. McCaffery, and S.D. Emr. 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
  • 23
    • 0014939016 scopus 로고
    • The intramitochondrial distribution of some enzymes involved in the biosynthesis of rat-liver phospholipids
    • Sarzala, M.G., L.M. Van Golde, B. De Kruyff, and L.L. Van Deenen. 1970. The intramitochondrial distribution of some enzymes involved in the biosynthesis of rat-liver phospholipids. Biochim. Biophys. Acta. 202:106-119.
    • (1970) Biochim. Biophys. Acta , vol.202 , pp. 106-119
    • Sarzala, M.G.1    Van Golde, L.M.2    De Kruyff, B.3    Van Deenen, L.L.4
  • 24
    • 0025650402 scopus 로고
    • Lysocardiolipin formation and reacylation in isolated rat liver mitochondria
    • Schlame, M., and B. Rustow. 1990. Lysocardiolipin formation and reacylation in isolated rat liver mitochondria. Biochem. J. 272:589-595.
    • (1990) Biochem. J. , vol.272 , pp. 589-595
    • Schlame, M.1    Rustow, B.2
  • 26
    • 0038376024 scopus 로고    scopus 로고
    • Mgm1p, a dynamin-related GTPase, is essential for fusion of the mitochondrial outer membrane
    • Sesaki, H., S.M. Southard, M.P. Yaffe, and R.E. Jensen. 2003. Mgm1p, a dynamin-related GTPase, is essential for fusion of the mitochondrial outer membrane. Mol. Biol. Cell. 14:2342-2356.
    • (2003) Mol. Biol. Cell. , vol.14 , pp. 2342-2356
    • Sesaki, H.1    Southard, S.M.2    Yaffe, M.P.3    Jensen, R.E.4
  • 28
    • 0025871358 scopus 로고
    • Mitochondrial membrane contact sites of yeast. Characterization of lipid components and possible involvement in intramitochondrial translocation of phospholipids
    • Simbeni, R., L. Pon, E. Zinser, F. Paltauf, and G. Daum. 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
  • 30
    • 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., J. Laroche-Traineau, A. Noubhani, D. Coulon, O. Bunoust, N. Camougrand, S. Manon, R. Lessire, and J.J. Bessoule. 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
  • 31
    • 0037088593 scopus 로고    scopus 로고
    • Phospholipid-cytochrome c interaction: Evidence for the extended lipid anchorage
    • Tuominen, E.K., C.J. Wallace, and P.K. Kinnunen. 2002. Phospholipid-cytochrome c interaction: evidence for the extended lipid anchorage. J. Biol. Chem. 277:8822-8826.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8822-8826
    • Tuominen, E.K.1    Wallace, C.J.2    Kinnunen, P.K.3
  • 32
    • 13644252982 scopus 로고    scopus 로고
    • Separation of yeast phospholipids using one-dimensional thin-layer chromatography
    • Vaden, D.L., V.M. Gohil, Z. Gu, and M.L. Greenberg. 2005. Separation of yeast phospholipids using one-dimensional thin-layer chromatography. Anal. Biochem. 338:162-164.
    • (2005) Anal. Biochem. , vol.338 , pp. 162-164
    • Vaden, D.L.1    Gohil, V.M.2    Gu, Z.3    Greenberg, M.L.4
  • 33
    • 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., R.H. Houtkooper, F. Valianpour, P.G. Barth, and R.J. Wanders. 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
  • 34
    • 33746649244 scopus 로고    scopus 로고
    • Lipid synthesis and transport in mitochondrial biogenesis
    • C.M. Koehler and M.F. Bauer, editors. Springer-Verlag, Heidelberg
    • Voelker, D.R. 2004. Lipid synthesis and transport in mitochondrial biogenesis. In Mitochondrial Function and Bioenergetics. Vol. 8. C.M. Koehler and M.F. Bauer, editors. Springer-Verlag, Heidelberg. pp. 267-291.
    • (2004) Mitochondrial Function and Bioenergetics , vol.8 , pp. 267-291
    • Voelker, D.R.1
  • 36
    • 0028676232 scopus 로고
    • New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae
    • Wach, A., A. Brachat, R. Pohlmann, and P. Philippsen. 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
  • 37
    • 0014952549 scopus 로고
    • Comparison of mitochondrial with microsomal acylation of monoacyl phosphoglycerides
    • Waite, M., P. Sisson, and E. Blackwell. 1970. Comparison of mitochondrial with microsomal acylation of monoacyl phosphoglycerides. Biochemistry. 9:746-753.
    • (1970) Biochemistry , vol.9 , pp. 746-753
    • Waite, M.1    Sisson, P.2    Blackwell, E.3
  • 38
    • 0345803935 scopus 로고    scopus 로고
    • Remodeling of cardiolipin by phospholipid transacylation
    • Xu, Y., R.I. Kelley, T.J. Blanck, and M. Schlame. 2003. Remodeling of cardiolipin by phospholipid transacylation. J. Biol. Chem. 278:51380-51385.
    • (2003) J. Biol. Chem. , vol.278 , pp. 51380-51385
    • Xu, Y.1    Kelley, R.I.2    Blanck, T.J.3    Schlame, M.4
  • 39
    • 20444379687 scopus 로고    scopus 로고
    • Characterization of lymphoblast mitochondria from patients with Barth syndrome
    • Xu, Y., J.J. Sutachan, H. Plesken, R.I. Kelley, and M. Schlame. 2005. Characterization of lymphoblast mitochondria from patients with Barth syndrome. Lab. Invest. 85:823-831.
    • (2005) Lab. Invest. , vol.85 , pp. 823-831
    • Xu, Y.1    Sutachan, J.J.2    Plesken, H.3    Kelley, R.I.4    Schlame, M.5
  • 40
    • 0000856498 scopus 로고
    • Two nuclear mutations that block mitochondrial protein import in yeast
    • Yaffe, M.P., and G. Schatz. 1984. Two nuclear mutations that block mitochondrial protein import in yeast. Proc. Natl. Acad. Sci. USA. 81:4819-4823.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4819-4823
    • Yaffe, M.P.1    Schatz, G.2


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