메뉴 건너뛰기




Volumn 17, Issue 9, 2006, Pages 3745-3755

Nonredundant roles of mitochondria-associated F-box proteins Mfb1 and Mdm30 in maintenance of mitochondrial morphology in yeast

Author keywords

[No Author keywords available]

Indexed keywords

F BOX PROTEIN; FUNGAL DNA; GENOMIC DNA; PROTEIN MDM30; PROTEIN MFB1; UNCLASSIFIED DRUG;

EID: 33748327051     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E06-01-0053     Document Type: Article
Times cited : (67)

References (72)
  • 1
    • 27644467457 scopus 로고    scopus 로고
    • Role of essential genes in mitochondrial morphogenesis in Saccharomyces cerevisiae
    • Altmann, K., and Westermann, B. (2005). Role of essential genes in mitochondrial morphogenesis in Saccharomyces cerevisiae. Mol. Biol. Cell 16, 5410-5417.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5410-5417
    • Altmann, K.1    Westermann, B.2
  • 2
    • 0035516771 scopus 로고    scopus 로고
    • Improved technique for electron microscope visualization of yeast membrane structure
    • Bauer, C., Herzog, V., and Bauer, M. F. (2001). Improved technique for electron microscope visualization of yeast membrane structure. Microsc. Microanal. 7, 530-534.
    • (2001) Microsc. Microanal. , vol.7 , pp. 530-534
    • Bauer, C.1    Herzog, V.2    Bauer, M.F.3
  • 3
    • 0025036216 scopus 로고
    • Behavior of mitochondria in the living cell
    • Bereiter-Hahn, J. (1990). Behavior of mitochondria in the living cell. Int. Rev. Cytol. 122, 1-63.
    • (1990) Int. Rev. Cytol. , vol.122 , pp. 1-63
    • Bereiter-Hahn, J.1
  • 5
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • Brachmann, C. B., Davies, A., Cost, G. J., Caputo, E., Li, J., Hieter, P., and Boeke, J. D. (1998). Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast 14, 115-132.
    • (1998) Yeast , vol.14 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 6
    • 2142758117 scopus 로고    scopus 로고
    • Mitochondrial dynamics in mammals
    • Chen, H., and Chan, D. C. (2004). Mitochondrial dynamics in mammals. Curr. Top. Dev. Biol. 59, 119-144.
    • (2004) Curr. Top. Dev. Biol. , vol.59 , pp. 119-144
    • Chen, H.1    Chan, D.C.2
  • 7
    • 0037455575 scopus 로고    scopus 로고
    • Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development
    • Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., and Chan, D. C. (2003). Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development. J. Cell Biol. 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
  • 8
    • 33644674439 scopus 로고    scopus 로고
    • The organization and inheritance of the mitochondrial genome
    • Chen, X. J., and Butow, R. A. (2005). The organization and inheritance of the mitochondrial genome. Nat. Rev. Genet. 6, 815-825.
    • (2005) Nat. Rev. Genet. , vol.6 , pp. 815-825
    • Chen, X.J.1    Butow, R.A.2
  • 11
    • 0037133634 scopus 로고    scopus 로고
    • Fast 100 nm resolution 3D-microscope reveals structural plasticity of mitochondria in live yeast
    • Egner, A., Jakobs, S., and Hell, S. W. (2002). Fast 100 nm resolution 3D-microscope reveals structural plasticity of mitochondria in live yeast. Proc. Natl. Acad. Sci. USA 99, 3370-3375.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3370-3375
    • Egner, A.1    Jakobs, S.2    Hell, S.W.3
  • 12
    • 33747389446 scopus 로고    scopus 로고
    • Regulation of mitochondrial fusion by the F-box protein Mdm30 involves proteasome-independent turnover of Fzol
    • Escobar-Henriques, M., Westermann, B., and Langer, T. (2006). Regulation of mitochondrial fusion by the F-box protein Mdm30 involves proteasome- independent turnover of Fzol. J. Cell Biol. 173, 645-650.
    • (2006) J. Cell Biol. , vol.173 , pp. 645-650
    • Escobar-Henriques, M.1    Westermann, B.2    Langer, T.3
  • 13
    • 0142058391 scopus 로고    scopus 로고
    • Two mitofusin proteins, mammalian homologues of FZO, with distinct functions are both required for mitochondrial fusion
    • Eura, Y., Ishihara, N., Yokota, S., and Mihara, K. (2003). Two mitofusin proteins, mammalian homologues of FZO, with distinct functions are both required for mitochondrial fusion. J. Biochem. 134, 333-344.
    • (2003) J. Biochem. , vol.134 , pp. 333-344
    • Eura, Y.1    Ishihara, N.2    Yokota, S.3    Mihara, K.4
  • 14
    • 0033553857 scopus 로고    scopus 로고
    • A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae
    • Fisk, H. A., and Yaffe, M. P. (1999). A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae. J. Cell Biol. 145, 1199-1208.
    • (1999) J. Cell Biol. , vol.145 , pp. 1199-1208
    • Fisk, H.A.1    Yaffe, M.P.2
  • 15
    • 0038037754 scopus 로고    scopus 로고
    • Mdm30 is an F-box protein required for maintenance of fusion-competent mitochondria in yeast
    • Fritz, S., Weinbach, N., and Westermann, B. (2003). Mdm30 is an F-box protein required for maintenance of fusion-competent mitochondria in yeast. Mol. Biol. Cell 14, 2303-2313.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2303-2313
    • Fritz, S.1    Weinbach, N.2    Westermann, B.3
  • 17
    • 0037173615 scopus 로고    scopus 로고
    • Functional profiling of the Saccharomyces cerevisiae genome
    • Giaever, G., et al. (2002). Functional profiling of the Saccharomyces cerevisiae genome. Nature 418, 387-391.
    • (2002) Nature , vol.418 , pp. 387-391
    • Giaever, G.1
  • 18
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz, D., Jean, A. S., Woods, R. A., and Schiestl, R. H. (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    Jean, A.S.2    Woods, R.A.3    Schiestl, R.H.4
  • 19
    • 4644229005 scopus 로고    scopus 로고
    • Importance of mitochondrial dynamics during meiosis and sporulation
    • Gorsich, S. W., and Shaw, J. M. (2004). Importance of mitochondrial dynamics during meiosis and sporulation. Mol. Biol. Cell 15, 4369-4381.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4369-4381
    • Gorsich, S.W.1    Shaw, J.M.2
  • 20
    • 0034997256 scopus 로고    scopus 로고
    • The many shapes of mitochondrial membranes
    • Griparic, L., and van der Bliek, A. M. (2001). The many shapes of mitochondrial membranes. Traffic 2, 235-244.
    • (2001) Traffic , vol.2 , pp. 235-244
    • Griparic, L.1    Van Der Bliek, A.M.2
  • 21
    • 0031440879 scopus 로고    scopus 로고
    • Developmentally regulated mitochondrial fusion mediated by a conserved, novel, predicted GTPase
    • Hales, K. G., and Fuller, M. T. (1997). Developmentally regulated mitochondrial fusion mediated by a conserved, novel, predicted GTPase. Cell 90, 121-129.
    • (1997) Cell , vol.90 , pp. 121-129
    • Hales, K.G.1    Fuller, M.T.2
  • 22
    • 2142710081 scopus 로고    scopus 로고
    • Alternative topogenesis of Mgm1 and mitochondrial morphology depend on ATP and a functional import motor
    • Herlan, M., Bornhövd, C., Hell, K., Neupert, W., and Reichert, A. S. (2004). Alternative topogenesis of Mgm1 and mitochondrial morphology depend on ATP and a functional import motor. J. Cell Biol. 165, 167-173.
    • (2004) J. Cell Biol. , vol.165 , pp. 167-173
    • Herlan, M.1    Bornhövd, C.2    Hell, K.3    Neupert, W.4    Reichert, A.S.5
  • 23
    • 0042526632 scopus 로고    scopus 로고
    • Processing of Mgm1 by the rhomboid-type protease Pcp1 is required for maintenance of mitochondrial morphology and of mitochondrial DNA
    • Herlan, M., Vogel, F., Bornhövd, C., Neupert, W., and Reichert, A. S. (2003). Processing of Mgm1 by the rhomboid-type protease Pcp1 is required for maintenance of mitochondrial morphology and of mitochondrial DNA. J. Biol. Chem. 278, 27781-27788.
    • (2003) J. Biol. Chem. , vol.278 , pp. 27781-27788
    • Herlan, M.1    Vogel, F.2    Bornhövd, C.3    Neupert, W.4    Reichert, A.S.5
  • 25
    • 0037050004 scopus 로고    scopus 로고
    • Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
    • Ho, Y., et al. (2002). Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 415, 180-183.
    • (2002) Nature , vol.415 , pp. 180-183
    • Ho, Y.1
  • 27
    • 13944278072 scopus 로고    scopus 로고
    • DRP-1-mediated mitochondrial fragmentation during EGL-1-induced cell death in C. elegans
    • Jagasia, R., Grote, P., Westermann, B., and Conradt, B. (2005). DRP-1-mediated mitochondrial fragmentation during EGL-1-induced cell death in C. elegans. Nature 433, 754-760.
    • (2005) Nature , vol.433 , pp. 754-760
    • Jagasia, R.1    Grote, P.2    Westermann, B.3    Conradt, B.4
  • 28
    • 0037768628 scopus 로고    scopus 로고
    • Spatial and temporal dynamics of budding yeast mitochondria lacking the division component Fis1p
    • Jakobs, S., Martini, N., Schauss, A. C., Egner, A., Westermann, B., and Hell, S. W. (2003). Spatial and temporal dynamics of budding yeast mitochondria lacking the division component Fis1p. J. Cell Sci. 116, 2005-2014.
    • (2003) J. Cell Sci. , vol.116 , pp. 2005-2014
    • Jakobs, S.1    Martini, N.2    Schauss, A.C.3    Egner, A.4    Westermann, B.5    Hell, S.W.6
  • 29
    • 0042564753 scopus 로고    scopus 로고
    • The yeast deubiquitinating enzyme Ubp16 is anchored to the outer mitochondrial membrane
    • Kinner, A., and Kölling, R. (2003). The yeast deubiquitinating enzyme Ubp16 is anchored to the outer mitochondrial membrane. FEBS Lett. 549, 135-140.
    • (2003) FEBS Lett. , vol.549 , pp. 135-140
    • Kinner, A.1    Kölling, R.2
  • 30
    • 33748316457 scopus 로고    scopus 로고
    • The novel F-box protein Mfb1p regulates mitochondrial connectivity and exhibits asymmetric localization in yeast
    • Kondo-Okamoto, N., Ohkuni, K., Kitagawa, K., McCaffery, J. M., Shaw, J. M., and Okamoto, K. (2006). The novel F-box protein Mfb1p regulates mitochondrial connectivity and exhibits asymmetric localization in yeast. Mol. Biol. Cell 17, 3756-3767.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3756-3767
    • Kondo-Okamoto, N.1    Ohkuni, K.2    Kitagawa, K.3    McCaffery, J.M.4    Shaw, J.M.5    Okamoto, K.6
  • 31
  • 32
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • Kremer, J. R., Mastronarde, D. N., and McIntosh, J. R. (1996). Computer visualization of three-dimensional image data using IMOD. J. Struct. Biol. 116, 71-76.
    • (1996) J. Struct. Biol. , vol.116 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 33
    • 1042268088 scopus 로고    scopus 로고
    • Functional interaction of 13 yeast SCF complexes with a set of yeast E2 enzymes in vitro
    • Kus, B. M., Caldon, C. E., Andorn-Broza, R., and Edwards, A. M. (2004). Functional interaction of 13 yeast SCF complexes with a set of yeast E2 enzymes in vitro. Proteins 54, 455-467.
    • (2004) Proteins , vol.54 , pp. 455-467
    • Kus, B.M.1    Caldon, C.E.2    Andorn-Broza, R.3    Edwards, A.M.4
  • 34
    • 14744294785 scopus 로고    scopus 로고
    • Iron-sulfur-protein biogenesis in eukaryotes
    • Lill, R., and Mühlenhoff, U. (2005). Iron-sulfur-protein biogenesis in eukaryotes. Trends Biochem. Sci. 30, 133-141.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 133-141
    • Lill, R.1    Mühlenhoff, U.2
  • 35
    • 0038700756 scopus 로고    scopus 로고
    • Mitochondrial membrane remodelling regulated by a conserved rhomboid protease
    • McQuibban, G. A., Saurya, S., and Freeman, M. (2003). Mitochondrial membrane remodelling regulated by a conserved rhomboid protease. Nature 423, 537-541.
    • (2003) Nature , vol.423 , pp. 537-541
    • McQuibban, G.A.1    Saurya, S.2    Freeman, M.3
  • 36
    • 0021285523 scopus 로고
    • Fluorescence microscopic studies of mitochondrial nucleoids during meiosis and sporulation in the yeast, Saccharomyces cerevisiae
    • Miyakawa, I., Aoi, H., Sando, N., and Kuroiwa, T. (1984). Fluorescence microscopic studies of mitochondrial nucleoids during meiosis and sporulation in the yeast, Saccharomyces cerevisiae. J. Cell Sci. 66, 21-38.
    • (1984) J. Cell Sci. , vol.66 , pp. 21-38
    • Miyakawa, I.1    Aoi, H.2    Sando, N.3    Kuroiwa, T.4
  • 37
    • 3142536716 scopus 로고    scopus 로고
    • Exploration of essential gene functions via titratable promoter alleles
    • Mnaimneh, S., et al. (2004). Exploration of essential gene functions via titratable promoter alleles. Cell 118, 31-44.
    • (2004) Cell , vol.118 , pp. 31-44
    • Mnaimneh, S.1
  • 38
    • 0034676096 scopus 로고    scopus 로고
    • Dnm1p GTPase-mediated mitochondrial fusion is a multi-step process requiring the novel integral membrane component Fis1p
    • Mozdy, A., McCaffery, J. M., and Shaw, J. M. (2000). Dnm1p GTPase-mediated mitochondrial fusion is a multi-step process requiring the novel integral membrane component Fis1p. J. Cell Biol. 151, 367-379.
    • (2000) J. Cell Biol. , vol.151 , pp. 367-379
    • Mozdy, A.1    McCaffery, J.M.2    Shaw, J.M.3
  • 39
    • 0038024175 scopus 로고    scopus 로고
    • A fuzzy mitochondrial fusion apparatus comes into focus
    • Mozdy, A. D., and Shaw, J. M. (2003). A fuzzy mitochondrial fusion apparatus comes into focus. Nat. Rev. Mol. Cell Biol. 4, 468-478.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 468-478
    • Mozdy, A.D.1    Shaw, J.M.2
  • 40
    • 17644386183 scopus 로고    scopus 로고
    • The F box protein Dsg1/Mdm30 is a transcriptional coactivator that stimulates Gal4 turnover and cotranscriptional mRNA processing
    • Muratani, M., Kung, C., Shokat, K. M., and Tansey, W. P. (2005). The F box protein Dsg1/Mdm30 is a transcriptional coactivator that stimulates Gal4 turnover and cotranscriptional mRNA processing. Cell 120, 887-899.
    • (2005) Cell , vol.120 , pp. 887-899
    • Muratani, M.1    Kung, C.2    Shokat, K.M.3    Tansey, W.P.4
  • 41
    • 21444442598 scopus 로고    scopus 로고
    • Instability of the mitofusin Fzo1 regulates mitochondrial morphology during the mating response of the yeast Saccharomyces cerevisiae
    • Neutzner, A., and Youle, R. J. (2005). Instability of the mitofusin Fzo1 regulates mitochondrial morphology during the mating response of the yeast Saccharomyces cerevisiae. J. Biol. Chem. 280, 18598-18603.
    • (2005) J. Biol. Chem. , vol.280 , pp. 18598-18603
    • Neutzner, A.1    Youle, R.J.2
  • 42
    • 0030841103 scopus 로고    scopus 로고
    • Mitochondrial transmission during mating in Saccharomyces cerevisiae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA
    • Nunnari, J., Marshall, W. F., Straight, A., Murray, A., Sedat, J. W., and Walter, P. (1997). Mitochondrial transmission during mating in Saccharomyces cerevisiae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA. Mol. Biol. Cell 8, 1233-1242.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1233-1242
    • Nunnari, J.1    Marshall, W.F.2    Straight, A.3    Murray, A.4    Sedat, J.W.5    Walter, P.6
  • 43
    • 0031823213 scopus 로고    scopus 로고
    • The sorting of mitochondrial DNA and mitochondrial proteins in zygotes: Preferential transmission of mitochondrial DNA to the medial bud
    • Okamoto, K., Perlman, P. S., and Butow, R. A. (1998). The sorting of mitochondrial DNA and mitochondrial proteins in zygotes: preferential transmission of mitochondrial DNA to the medial bud. J. Cell Biol. 142, 613-623.
    • (1998) J. Cell Biol. , vol.142 , pp. 613-623
    • Okamoto, K.1    Perlman, P.S.2    Butow, R.A.3
  • 44
    • 27544466847 scopus 로고    scopus 로고
    • Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes
    • Okamoto, K., and Shaw, J. M. (2005). Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes. Annu. Rev. Genet. 39, 503-536.
    • (2005) Annu. Rev. Genet. , vol.39 , pp. 503-536
    • Okamoto, K.1    Shaw, J.M.2
  • 45
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • Petroski, M. D., and Deshaies, R. J. (2005). Function and regulation of cullin-RING ubiquitin ligases. Nat. Rev. Mol. Cell Biol. 6, 9-20.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 46
    • 0032493625 scopus 로고    scopus 로고
    • Fzo1p is a mitochondrial outer membrane protein essential for the biogenesis of functional mitochondria in Saccharomyces cerevisiae
    • Rapaport, D., Brunner, M., Neupert, W., and Westermann, B. (1998). Fzo1p is a mitochondrial outer membrane protein essential for the biogenesis of functional mitochondria in Saccharomyces cerevisiae. J. Biol. Chem. 273, 20150-20155.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20150-20155
    • Rapaport, D.1    Brunner, M.2    Neupert, W.3    Westermann, B.4
  • 47
    • 0031709394 scopus 로고    scopus 로고
    • A mutation in a novel yeast proteasomal gene, RPN11/MPR1, produces cell cycle arrest, overreplication of nuclear and mitochondrial DNA, and an altered mitochondrial morphology
    • Rinaldi, T., Ricci, C., Porro, D., Bolotin-Fukuhara, M., and Frontali, L. (1998). A mutation in a novel yeast proteasomal gene, RPN11/MPR1, produces cell cycle arrest, overreplication of nuclear and mitochondrial DNA, and an altered mitochondrial morphology. Mol. Biol. Cell 9, 2917-2931.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2917-2931
    • Rinaldi, T.1    Ricci, C.2    Porro, D.3    Bolotin-Fukuhara, M.4    Frontali, L.5
  • 48
    • 0037089084 scopus 로고    scopus 로고
    • Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo
    • Rojo, M., Legros, F., Chateau, D., and Lombes, A. (2002). Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo. J. Cell Sci. 115, 1663-1674.
    • (2002) J. Cell Sci. , vol.115 , pp. 1663-1674
    • Rojo, M.1    Legros, F.2    Chateau, D.3    Lombes, A.4
  • 49
    • 0038783254 scopus 로고    scopus 로고
    • Mitofusin-1 protein is a generally expressed mediator of mitochondrial fusion in mammalian cells
    • Santel, A., Frank, S., Gaume, B., Herrler, M., Youle, R. J., and Fuller, M. T. (2003). Mitofusin-1 protein is a generally expressed mediator of mitochondrial fusion in mammalian cells. J. Cell Sci. 116, 2763-2774.
    • (2003) J. Cell Sci. , vol.116 , pp. 2763-2774
    • Santel, A.1    Frank, S.2    Gaume, B.3    Herrler, M.4    Youle, R.J.5    Fuller, M.T.6
  • 50
    • 0003118424 scopus 로고    scopus 로고
    • A century of mitochondrial research: Achievements and perspectives
    • Scheffler, I. E. (2000). A century of mitochondrial research: achievements and perspectives. Mitochondrion 1, 3-31.
    • (2000) Mitochondrion , vol.1 , pp. 3-31
    • Scheffler, I.E.1
  • 51
    • 0041765777 scopus 로고    scopus 로고
    • Staying in aerobic shape: How the structural integrity of mitochondria and mitochondrial DNA is maintained
    • Scott, S. V., Cassidy-Stone, A., Meeusen, S. L., and Nunnari, J. (2003). Staying in aerobic shape: how the structural integrity of mitochondria and mitochondrial DNA is maintained. Curr. Opin. Cell Biol. 15, 482-488.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 482-488
    • Scott, S.V.1    Cassidy-Stone, A.2    Meeusen, S.L.3    Nunnari, J.4
  • 52
    • 0033571410 scopus 로고    scopus 로고
    • Division versus fusion: Dnm1p and Fzo1p antagonistically regulate mitochondrial shape
    • Sesaki, H., and Jensen, R. E. (1999). Division versus fusion: Dnm1p and Fzo1p antagonistically regulate mitochondrial shape. J. Cell Biol. 147, 699-706.
    • (1999) J. Cell Biol. , vol.147 , pp. 699-706
    • Sesaki, H.1    Jensen, R.E.2
  • 53
    • 0035911963 scopus 로고    scopus 로고
    • UGO1 encodes an outer membrane protein required for mitochondrial fusion
    • Sesaki, H., and Jensen, R. E. (2001). UGO1 encodes an outer membrane protein required for mitochondrial fusion. J. Cell Biol. 152, 1123-1134.
    • (2001) J. Cell Biol. , vol.152 , pp. 1123-1134
    • Sesaki, H.1    Jensen, R.E.2
  • 54
    • 3142546895 scopus 로고    scopus 로고
    • Ugo1p links the Fzo1p and Mgm1p GTPases for mitochondrial fusion
    • Sesaki, H., and Jensen, R. E. (2004). Ugo1p links the Fzo1p and Mgm1p GTPases for mitochondrial fusion. J. Biol. Chem. 279, 28298-28303.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28298-28303
    • Sesaki, H.1    Jensen, R.E.2
  • 55
    • 0043095416 scopus 로고    scopus 로고
    • Cells lacking Pcp1p/Ugo2p, a rhomboid-like protease required for Mgm1p processing, lose mtDNA and mitochondrial structure in a Dnm1p-dependent manner, but remain competent for mitochondrial fusion
    • Sesaki, H., Southard, S. M., Hobbs, A. E., and Jensen, R. E. (2003). Cells lacking Pcp1p/Ugo2p, a rhomboid-like protease required for Mgm1p processing, lose mtDNA and mitochondrial structure in a Dnm1p-dependent manner, but remain competent for mitochondrial fusion. Biochem. Biophys. Res. Commun. 308, 276-283.
    • (2003) Biochem. Biophys. Res. Commun. , vol.308 , pp. 276-283
    • Sesaki, H.1    Southard, S.M.2    Hobbs, A.E.3    Jensen, R.E.4
  • 56
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Sherman, F. (1991). Getting started with yeast. Methods Enzymol. 194, 3-21.
    • (1991) Methods Enzymol. , vol.194 , pp. 3-21
    • Sherman, F.1
  • 57
    • 0025978950 scopus 로고
    • Micromanipulation and dissection of asci
    • Sherman, F., and Hicks, J. (1991). Micromanipulation and dissection of asci. Methods Enzymol. 194, 21-37.
    • (1991) Methods Enzymol. , vol.194 , pp. 21-37
    • Sherman, F.1    Hicks, J.2
  • 58
    • 0345687191 scopus 로고    scopus 로고
    • The proteome of Saccharomyces cerevisiae mitochondria
    • Sickmann, A., et al. (2003). The proteome of Saccharomyces cerevisiae mitochondria. Proc. Natl. Acad. Sci. USA 100, 13207-13212.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13207-13212
    • Sickmann, A.1
  • 59
    • 0030854830 scopus 로고    scopus 로고
    • Mitochondrial inheritance: Cell cycle and actin cable dependence of polarized mitochondrial movements in Saccharomyces cerevisiae
    • Simon, V. R., Karmon, S. L., and Pon, L. A. (1997). Mitochondrial inheritance: cell cycle and actin cable dependence of polarized mitochondrial movements in Saccharomyces cerevisiae. Cell Motil. Cytoskeleton 37, 199-210.
    • (1997) Cell Motil. Cytoskeleton , vol.37 , pp. 199-210
    • Simon, V.R.1    Karmon, S.L.2    Pon, L.A.3
  • 60
    • 0014444144 scopus 로고
    • A low-viscosity epoxy resin embedding medium for electron microscopy
    • Spurr, A. R. (1969). A low-viscosity epoxy resin embedding medium for electron microscopy. J. Ultrastruct. Res. 26, 31-43.
    • (1969) J. Ultrastruct. Res. , vol.26 , pp. 31-43
    • Spurr, A.R.1
  • 61
    • 0001070587 scopus 로고
    • Mitochondrial structure
    • ed. E. W. Strathern, E. W. Jones, and J. R. Broach, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Stevens, B. (1981). Mitochondrial structure. In: The Molecular Biology of the Yeast Saccharomyces: Life Cycle and Inheritance, ed. E. W. Strathern, E. W. Jones, and J. R. Broach, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, 471-504.
    • (1981) The Molecular Biology of the Yeast Saccharomyces: Life Cycle and Inheritance , pp. 471-504
    • Stevens, B.1
  • 62
    • 33748306502 scopus 로고    scopus 로고
    • Studying proteolysis within mitochondria
    • in press
    • Tatsuta, T., and Langer, T. (2006). Studying proteolysis within mitochondria. Curr. Topics Gen. (in press).
    • (2006) Curr. Topics Gen.
    • Tatsuta, T.1    Langer, T.2
  • 63
    • 0034628508 scopus 로고    scopus 로고
    • A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae
    • Uetz, P., et al. (2000). A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature 403, 601-603.
    • (2000) Nature , vol.403 , pp. 601-603
    • Uetz, P.1
  • 65
    • 0036308235 scopus 로고    scopus 로고
    • Merging mitochondria matters. Cellular role and molecular machinery of mitochondrial fusion
    • Westermann, B. (2002). Merging mitochondria matters. Cellular role and molecular machinery of mitochondrial fusion. EMBO Rep. 3, 527-531.
    • (2002) EMBO Rep. , vol.3 , pp. 527-531
    • Westermann, B.1
  • 66
    • 0033672549 scopus 로고    scopus 로고
    • Mitochondria-targeted green fluorescent proteins: Convenient tools for the study of organelle biogenesis in Saccharomyces cerevisiae
    • Westermann, B., and Neupert, W. (2000). Mitochondria-targeted green fluorescent proteins: convenient tools for the study of organelle biogenesis in Saccharomyces cerevisiae. Yeast 16, 1421-1427.
    • (2000) Yeast , vol.16 , pp. 1421-1427
    • Westermann, B.1    Neupert, W.2
  • 67
    • 9644273891 scopus 로고    scopus 로고
    • A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin
    • Willems, A. R., Schwab, M., and Tyers, M. (2004). A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin. Biochim. Biophys. Acta 1695, 133-170.
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 133-170
    • Willems, A.R.1    Schwab, M.2    Tyers, M.3
  • 68
    • 0034676095 scopus 로고    scopus 로고
    • The dynamin-related GTPase, Mgm1p, is an intermembrane space protein required for maintenance of fusion competent mitochondria
    • Wong, E. D., Wagner, J. A., Gorsich, S. W., McCaffery, J. M., Shaw, J. M., and Nunnari, J. (2000). The dynamin-related GTPase, Mgm1p, is an intermembrane space protein required for maintenance of fusion competent mitochondria. J. Cell Biol. 151, 341-352.
    • (2000) J. Cell Biol. , vol.151 , pp. 341-352
    • Wong, E.D.1    Wagner, J.A.2    Gorsich, S.W.3    McCaffery, J.M.4    Shaw, J.M.5    Nunnari, J.6
  • 69
    • 0037415638 scopus 로고    scopus 로고
    • The intramitochondrial dynamin-related GTPase, Mgm1p, is a component of a protein complex that mediates mitochondrial fusion
    • Wong, E. D., Wagner, J. A., Scott, S. V., Okreglak, V., Holewinske, T. J., Cassidy-Stone, A., and Nunnari, J. (2003). The intramitochondrial dynamin-related GTPase, Mgm1p, is a component of a protein complex that mediates mitochondrial fusion. J. Cell Biol. 160, 303-311.
    • (2003) J. Cell Biol. , vol.160 , pp. 303-311
    • Wong, E.D.1    Wagner, J.A.2    Scott, S.V.3    Okreglak, V.4    Holewinske, T.J.5    Cassidy-Stone, A.6    Nunnari, J.7
  • 70
    • 0033525615 scopus 로고    scopus 로고
    • The machinery of mitochondrial inheritance and behavior
    • Yaffe, M. P. (1999). The machinery of mitochondrial inheritance and behavior. Science 283, 1493-1497.
    • (1999) Science , vol.283 , pp. 1493-1497
    • Yaffe, M.P.1
  • 71
    • 0033533697 scopus 로고    scopus 로고
    • A retention mechanism for distribution of mitochondria during cell division in budding yeast
    • Yang, H. C., Palazzo, A., Swayne, T. C., and Pon, L. A. (1999). A retention mechanism for distribution of mitochondria during cell division in budding yeast. Curr. Biol. 9, 1111-1114.
    • (1999) Curr. Biol. , vol.9 , pp. 1111-1114
    • Yang, H.C.1    Palazzo, A.2    Swayne, T.C.3    Pon, L.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.