메뉴 건너뛰기




Volumn 145, Issue 6, 1999, Pages 1199-1208

A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae

Author keywords

Cytoskeleton; Mitochondria; Organelle inheritance; Ubiquitin; Yeast

Indexed keywords

ARGININE; INTERMEDIATE FILAMENT PROTEIN; LYSINE; UBIQUITIN; UBIQUITIN PROTEIN LIGASE;

EID: 0033553857     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.145.6.1199     Document Type: Article
Times cited : (161)

References (51)
  • 1
    • 0024533657 scopus 로고
    • Dominant suppressors of yeast actin mutations that are reciprocally suppressed
    • Adams, A.E.M., and D. Botstein. 1989. Dominant suppressors of yeast actin mutations that are reciprocally suppressed. Genetics. 121:675-683.
    • (1989) Genetics. , vol.121 , pp. 675-683
    • Adams, A.E.M.1    Botstein, D.2
  • 2
    • 0024584813 scopus 로고
    • A yeast actin-binding protein is encoded by SAC6, a gene found by suppression of an actin mutation
    • Adams, A.E.M., D. Botstein, and D.G. Drubin. 1989. A yeast actin-binding protein is encoded by SAC6, a gene found by suppression of an actin mutation. Science. 243:231-233.
    • (1989) Science. , vol.243 , pp. 231-233
    • Adams, A.E.M.1    Botstein, D.2    Drubin, D.G.3
  • 4
    • 0028073188 scopus 로고
    • Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitinated chain
    • Arnason, T., and M.J. Ellison. 1994. Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitinated chain. Mol. Cell. Biol. 14:7876-7883.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7876-7883
    • Arnason, T.1    Ellison, M.J.2
  • 6
    • 0030468155 scopus 로고    scopus 로고
    • Mitochondrial distribution and inheritance
    • Berger, K.H., and M.P. Yaffe. 1996. Mitochondrial distribution and inheritance. Experientia. 52:1111-1116.
    • (1996) Experientia. , vol.52 , pp. 1111-1116
    • Berger, K.H.1    Yaffe, M.P.2
  • 7
    • 0031860890 scopus 로고    scopus 로고
    • Prohibitin family members interact genetically with mitochondrial inheritance components in Saccharomyces cerevisiae
    • Berger, K.H., and M.P. Yaffe. 1998. Prohibitin family members interact genetically with mitochondrial inheritance components in Saccharomyces cerevisiae. Mol. Cell. Biol. 18:4043-4052.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4043-4052
    • Berger, K.H.1    Yaffe, M.P.2
  • 8
    • 0031059722 scopus 로고    scopus 로고
    • Mdm12p, a component required for mitochondrial inheritance that is conserved between budding and fission yeast
    • Berger, K.H., L.F. Sogo, and M.P. Yaffe. 1997. Mdm12p, a component required for mitochondrial inheritance that is conserved between budding and fission yeast. J. Cell Biol. 136:545-553.
    • (1997) J. Cell Biol. , vol.136 , pp. 545-553
    • Berger, K.H.1    Sogo, L.F.2    Yaffe, M.P.3
  • 9
    • 0018564346 scopus 로고
    • Transformation in yeast: Development of a hybrid vector and isolation of the CAN1 gene
    • Broach, J.R., J.N. Strathern, and J.B. Hicks. 1979. Transformation in yeast: development of a hybrid vector and isolation of the CAN1 gene. Gene. 8:121-133.
    • (1979) Gene. , vol.8 , pp. 121-133
    • Broach, J.R.1    Strathern, J.N.2    Hicks, J.B.3
  • 10
    • 0031128320 scopus 로고    scopus 로고
    • ER-associated and proteosome-mediated protein degradation: How two topologically restricted events came together
    • Brodsky, J.L., and A.A. McCracken. 1997. ER-associated and proteosome-mediated protein degradation: how two topologically restricted events came together. Trends Cell Biol. 7:151-156.
    • (1997) Trends Cell Biol. , vol.7 , pp. 151-156
    • Brodsky, J.L.1    McCracken, A.A.2
  • 11
    • 0028129071 scopus 로고
    • MMMI encodes a mitochondrial outer membrane protein essential for establishing and maintaining the structure of yeast mitochondria
    • Burgess, S.M., M. Delannoy, and R.E. Jensen. 1994. MMMI encodes a mitochondrial outer membrane protein essential for establishing and maintaining the structure of yeast mitochondria. J. Cell Biol. 126:1375-1391.
    • (1994) J. Cell Biol. , vol.126 , pp. 1375-1391
    • Burgess, S.M.1    Delannoy, M.2    Jensen, R.E.3
  • 12
    • 0028110821 scopus 로고
    • The Pichia pastoris PAS4 gene encodes a ubiquitin-conjugating enzyme required for peroxisome assembly
    • Crane, D.I., J.E. Kalish, and S.J. Gould. 1994. The Pichia pastoris PAS4 gene encodes a ubiquitin-conjugating enzyme required for peroxisome assembly. J. Biol. Chem. 269:21835-21844.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21835-21844
    • Crane, D.I.1    Kalish, J.E.2    Gould, S.J.3
  • 13
    • 0025838227 scopus 로고
    • Epitope-tagged ubiquitin. A new probe for analyzing ubiquitin function
    • Ellison, M.J., and M. Hochstrasser. 1991. Epitope-tagged ubiquitin. A new probe for analyzing ubiquitin function. J. Biol. chem. 266:21150-21157.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21150-21157
    • Ellison, M.J.1    Hochstrasser, M.2
  • 14
    • 0030833816 scopus 로고    scopus 로고
    • Mutational analysis of Mdm1p function in nuclear and mitochondrial inheritance
    • Fisk, H.A., and M.P. Yaffe. 1997. Mutational analysis of Mdm1p function in nuclear and mitochondrial inheritance. J. Cell Biol. 138:485-494.
    • (1997) J. Cell Biol. , vol.138 , pp. 485-494
    • Fisk, H.A.1    Yaffe, M.P.2
  • 15
    • 0030881952 scopus 로고    scopus 로고
    • Ubiquitin Lys63 is involved in ubiquitination of a yeast plasma membrane protein
    • Gatan, J.M., and R. Haguenauer-Tsapis. 1997. Ubiquitin Lys63 is involved in ubiquitination of a yeast plasma membrane protein. EMBO (Eur. Mol. Biol. Org.) J. 16:5847-5854.
    • (1997) EMBO (Eur. Mol. Biol. Org.) J. , vol.16 , pp. 5847-5854
    • Gatan, J.M.1    Haguenauer-Tsapis, R.2
  • 16
    • 15844424064 scopus 로고    scopus 로고
    • Ubiquitination mediated by the Npilp/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease
    • Galan, J.M., V. Moreau, B. Andre, C. Volland, and R. Haguennauer-Tsapis. 1996. Ubiquitination mediated by the Npilp/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease. J. Biol. Chem. 271: 10946-10952.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10946-10952
    • Galan, J.M.1    Moreau, V.2    Andre, B.3    Volland, C.4    Haguennauer-Tsapis, R.5
  • 17
    • 0030660267 scopus 로고    scopus 로고
    • Ubiquitin-mediated regulation of 3-hydroxy-3-methylglutaryl-CoA reductase
    • Hampton, R.Y., and H. Bhakta. 1997. Ubiquitin-mediated regulation of 3-hydroxy-3-methylglutaryl-CoA reductase. Proc. Natl. Acad. Sci. USA. 94: 12944-12948.
    • (1997) Proc. Natl. Acad. Sci. USA. , vol.94 , pp. 12944-12948
    • Hampton, R.Y.1    Bhakta, H.2
  • 18
    • 0030951615 scopus 로고    scopus 로고
    • The yeast gene, MDM20, is necessary for mitochondrial inheritance and organization of the actin cytoskeleton. J
    • Hermann, G.J., E.J. King, and J.M. Shaw. 1997. The yeast gene, MDM20, is necessary for mitochondrial inheritance and organization of the actin cytoskeleton. J. Cell Biol. 137:141-153.
    • (1997) Cell Biol. , vol.137 , pp. 141-153
    • Hermann, G.J.1    King, E.J.2    Shaw, J.M.3
  • 19
    • 0030054178 scopus 로고    scopus 로고
    • Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis
    • Hicke, L., and H. Riezman. 1996. Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell. 84:277-287.
    • (1996) Cell. , vol.84 , pp. 277-287
    • Hicke, L.1    Riezman, H.2
  • 20
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser, M. 1996. Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30:405-439.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 21
  • 22
    • 0028907874 scopus 로고
    • A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase
    • Huibregtse, J., M. Scheffner, S. Beaudenon, and P.M. Howley. 1995. A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc. Natl. Acad. Sci. USA. 92:2563-2567.
    • (1995) Proc. Natl. Acad. Sci. USA. , vol.92 , pp. 2563-2567
    • Huibregtse, J.1    Scheffner, M.2    Beaudenon, S.3    Howley, P.M.4
  • 23
    • 0025932933 scopus 로고
    • A cellular protein mediates association of p53 with the E6 oncoprotein of human papillomavirus types 16 or 18
    • Huibregtse, J.M., M. Scheffner, and P.M. Howley. 1991. A cellular protein mediates association of p53 with the E6 oncoprotein of human papillomavirus types 16 or 18. EMBO (Eur. Mol. Biol. Org.) J. 10:4129-4135.
    • (1991) EMBO (Eur. Mol. Biol. Org.) J. , vol.10 , pp. 4129-4135
    • Huibregtse, J.M.1    Scheffner, M.2    Howley, P.M.3
  • 24
    • 0030888109 scopus 로고    scopus 로고
    • The large subunit of RNA polymerase II is a substrate of the Rsp5 ubiquitin-protein ligase
    • Huibregtse, J.M., J.C. Yang, and S.L. Beaudenon. 1997. The large subunit of RNA polymerase II is a substrate of the Rsp5 ubiquitin-protein ligase. Proc. Natl. Acad. Sci. USA. 94:3656-3661.
    • (1997) Proc. Natl. Acad. Sci. USA. , vol.94 , pp. 3656-3661
    • Huibregtse, J.M.1    Yang, J.C.2    Beaudenon, S.L.3
  • 25
    • 0029953663 scopus 로고    scopus 로고
    • Yeast RSP5 and its human homolog hRPF1 potentiate hormone-dependent activation of transcription by human progesterone and glucocorticoid receptors
    • Imhof, M.O., and D.P. McDonnell. 1996. Yeast RSP5 and its human homolog hRPF1 potentiate hormone-dependent activation of transcription by human progesterone and glucocorticoid receptors. Mol. Cell. Biol. 16:2594-2605.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2594-2605
    • Imhof, M.O.1    McDonnell, D.P.2
  • 27
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
    • Mahajan, R., C. Delphin, T. Guan, L. Gerace, and F. Melchior. 1997. A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell. 88:97-107.
    • (1997) Cell. , vol.88 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 28
    • 0001836496 scopus 로고
    • Production of single-stranded DNA by asymmetric PCR
    • M.A. Innis, D.H. Gelfand, J.J. Sninsky, and T.J. White, editors. Academic Press, San Diego, CA
    • McCabe, P.C. 1990. Production of single-stranded DNA by asymmetric PCR. In PCR Protocols. M.A. Innis, D.H. Gelfand, J.J. Sninsky, and T.J. White, editors. Academic Press, San Diego, CA. 76-83.
    • (1990) PCR Protocols , pp. 76-83
    • McCabe, P.C.1
  • 29
    • 0026690840 scopus 로고
    • Nuclear and mitochondrial inheritance in yeast depends on novel cytoplasmic structures defined by the MDM1 protein
    • McConnell, S.J., and M.P. Yaffe. 1992. Nuclear and mitochondrial inheritance in yeast depends on novel cytoplasmic structures defined by the MDM1 protein. J. Cell Biol. 118:385-395.
    • (1992) J. Cell Biol. , vol.118 , pp. 385-395
    • McConnell, S.J.1    Yaffe, A.P.2
  • 30
    • 0027286647 scopus 로고
    • Intermediate filament formation by a yeast protein essential for organelle inheritance
    • McConnell, S.J., and M.P. Yaffe. 1993. Intermediate filament formation by a yeast protein essential for organelle inheritance. Science. 260:687-689.
    • (1993) Science. , vol.260 , pp. 687-689
    • McConnell, S.J.1    Yaffe, M.P.2
  • 31
    • 0025076787 scopus 로고
    • Temperature-sensitive yeast mutants defective in mitochondrial inheritance
    • McConnell, S.J., L.C. Stewart, A. Talin, and M.P. Yaffe. 1990. Temperature-sensitive yeast mutants defective in mitochondrial inheritance. J. Cell Biol. 111:967-976.
    • (1990) J. Cell Biol. , vol.111 , pp. 967-976
    • McConnell, S.J.1    Stewart, L.C.2    Talin, A.3    Yaffe, M.P.4
  • 32
    • 0029892928 scopus 로고    scopus 로고
    • BRO1, a novel gene that interacts with components of the pkc1p-mitogen-activated protein kinase pathway in Saccharomyces cerevisiae
    • Nickas, M.E., and M.P. Yaffe. 1996. BRO1, a novel gene that interacts with components of the pkc1p-mitogen-activated protein kinase pathway in Saccharomyces cerevisiae. Mol. Cell. Biol. 16:2585-2593.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2585-2593
    • Nickas, M.E.1    Yaffe, M.P.2
  • 34
    • 0021005926 scopus 로고
    • Membrane biogeneis: An overview
    • Palade, G. 1983. Membrane biogeneis: an overview. Methods Enzymol. 96:29-40.
    • (1983) Methods Enzymol. , vol.96 , pp. 29-40
    • Palade, G.1
  • 35
    • 0030772933 scopus 로고    scopus 로고
    • Targeting of substrates to the 26s proteosome
    • Pickart, C.M. 1997. Targeting of substrates to the 26S proteosome. FASEB (Fed. Am. Soc. Exp. Biol.) J. 11:1055-1066.
    • (1997) FASEB (Fed. Am. Soc. Exp. Biol.) J. , vol.11 , pp. 1055-1066
    • Pickart, C.M.1
  • 36
    • 0025975312 scopus 로고
    • Cloning genes by complementation
    • Rose, M.D., and J.R. Broach. 1991. Cloning genes by complementation. Methods Enzymol. 194:195-230.
    • (1991) Methods Enzymol. , vol.194 , pp. 195-230
    • Rose, M.D.1    Broach, J.R.2
  • 37
    • 0023545322 scopus 로고
    • A Saccharomyces cerevisiae genomic plasmid bank based on a centromere-containing shuttle vector
    • Rose, M.D., P. Novick, J.H. Thomas, D. Botstein, and G.R. Fink. 1987. A Saccharomyces cerevisiae genomic plasmid bank based on a centromere-containing shuttle vector. Gene. 60:237-243.
    • (1987) Gene. , vol.60 , pp. 237-243
    • Rose, M.D.1    Novick, P.2    Thomas, J.H.3    Botstein, D.4    Fink, G.R.5
  • 39
    • 0025164762 scopus 로고
    • Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins
    • Seufert, W., and S. Jentsch. 1990. Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins. EMBO (Eur. Mol. Biol. Org.) J. 9:543-550.
    • (1990) EMBO (Eur. Mol. Biol. Org.) J. , vol.9 , pp. 543-550
    • Seufert, W.1    Jentsch, S.2
  • 40
    • 0025632969 scopus 로고
    • UBC1 encodes a novel member of an essential subfamily of yeast ubiquitin-conjugating enzymes involved in protein degradation
    • Seufert, W., J.P. McGrath, and S. Jentsch. 1990. UBC1 encodes a novel member of an essential subfamily of yeast ubiquitin-conjugating enzymes involved in protein degradation. EMBO (Eur. Mol. Biol. Org.) J. 9:4535-4541.
    • (1990) EMBO (Eur. Mol. Biol. Org.) J. , vol.9 , pp. 4535-4541
    • Seufert, W.1    McGrath, J.P.2    Jentsch, S.3
  • 41
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R.S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics. 122:19-27.
    • (1989) Genetics. , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 42
    • 0026342691 scopus 로고
    • A mutation in the yeast heat-shock factor gene causes temperature-sensitive defects in both mitochondrial protein import and the cell cycle
    • Smith, B.J., and M.P. Yaffe. 1991. A mutation in the yeast heat-shock factor gene causes temperature-sensitive defects in both mitochondrial protein import and the cell cycle. Mol. Cell. Biol. 11:2647-2655.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2647-2655
    • Smith, B.J.1    Yaffe, M.P.2
  • 43
    • 0028024592 scopus 로고
    • Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane
    • Sogo, L.F., and M.P. Yaffe. 1994. Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane. J. Cell Biol. 126:1361-1373.
    • (1994) J. Cell Biol. , vol.126 , pp. 1361-1373
    • Sogo, L.F.1    Yaffe, M.P.2
  • 44
    • 0031867271 scopus 로고    scopus 로고
    • Nitrogen-regulated ubiquitination of the Gap1 permease of Saccharomyces cerevisiae
    • Springael, J.Y., and B. Andre. 1998. Nitrogen-regulated ubiquitination of the Gap1 permease of Saccharomyces cerevisiae. Mol. Biol. Cell. 9:1253-1263.
    • (1998) Mol. Biol. Cell. , vol.9 , pp. 1253-1263
    • Springael, J.Y.1    Andre, B.2
  • 45
    • 0001070587 scopus 로고
    • Mitochondrial structure
    • J.N. Strathern, E.W. Jones, and J.R. Broach, editors. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • Stevens, B. 1981. Mitochondrial structure. In The Molecular Biology of the Yeast Saccharomyces cerevisiae. Vol. 1. J.N. Strathern, E.W. Jones, and J.R. Broach, editors. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY. 471-504.
    • (1981) The Molecular Biology of the Yeast Saccharomyces Cerevisiae , vol.1 , pp. 471-504
    • Stevens, B.1
  • 46
    • 0026782393 scopus 로고
    • The Pas2 protein essential for peroxisome biogenesis is related to ubiquitin-conjugating enzymes
    • Wiebel, F.F., and W.-H. Kunau. 1992. The Pas2 protein essential for peroxisome biogenesis is related to ubiquitin-conjugating enzymes. Nature. 359: 73-76.
    • (1992) Nature. , vol.359 , pp. 73-76
    • Wiebel, F.F.1    Kunau, W.-H.2
  • 47
    • 0016588190 scopus 로고
    • The use of fluorescent DNA-binding agent for detecting and separating yeast mitochondrial DNA
    • Williamson, D.H., and D.J. Fennell. 1975. The use of fluorescent DNA-binding agent for detecting and separating yeast mitochondrial DNA. Methods Cell Biol. 12:335-351.
    • (1975) Methods Cell Biol. , vol.12 , pp. 335-351
    • Williamson, D.H.1    Fennell, D.J.2
  • 48
    • 0030006865 scopus 로고    scopus 로고
    • Bull, a new protein that binds to the Rsp5 ubiquitin ligase in Saccharomyces cerevisiae
    • Yashiroda, H., T. Oguchi, Y. Yasuda, A. Toh-E, and Y. Kikuchi. 1996. Bull, a new protein that binds to the Rsp5 ubiquitin ligase in Saccharomyces cerevisiae. Mol. Cell. Biol. 16:3255-3263.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3255-3263
    • Yashiroda, H.1    Oguchi, T.2    Yasuda, Y.3    Toh-E, A.4    Kikuchi, Y.5
  • 49
    • 0024416864 scopus 로고
    • Ubiquitin is involved in the in vitro insertion of monoamino oxidase B into mitochondrial outer membranes
    • Zhuang, Z., and R.B. McCauley. 1989. Ubiquitin is involved in the in vitro insertion of monoamino oxidase B into mitochondrial outer membranes. J. Biol. Chem. 264:14594-14596.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14594-14596
    • Zhuang, Z.1    McCauley, R.B.2
  • 50
    • 0028791882 scopus 로고
    • Mutations altering the mitochondrial-cyloplasmic distribution of Mod5p implicate the actin cytoskeleton and mRNA 3′ ends and/or protein synthesis in mitochondrial delivery
    • Zoladek, T., G. Vaduva, L.A. Hunter, M. Boguta, B.D. Go, N.C. Martin, and A.K. Hopper. 1995. Mutations altering the mitochondrial-cyloplasmic distribution of Mod5p implicate the actin cytoskeleton and mRNA 3′ ends and/or protein synthesis in mitochondrial delivery. Mol. Cell. Biol. 15:6884-6894.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6884-6894
    • Zoladek, T.1    Vaduva, G.2    Hunter, L.A.3    Boguta, M.4    Go, B.D.5    Martin, N.C.6    Hopper, A.K.7
  • 51
    • 1842374437 scopus 로고    scopus 로고
    • MDP1, a Saccharomyces cerevisiae gene involved in mitochondrial/cytoplasmic protein distribution, is identical to the ubiquitin-protein ligase gene RSP5
    • Zoladek, T., A. Tobiasz, G. Vaduva, M. Boguta, N.C. Martin, and A.K. Hopper. 1997. MDP1, a Saccharomyces cerevisiae gene involved in mitochondrial/cytoplasmic protein distribution, is identical to the ubiquitin-protein ligase gene RSP5. Genetics. 145:595-603.
    • (1997) Genetics. , vol.145 , pp. 595-603
    • Zoladek, T.1    Tobiasz, A.2    Vaduva, G.3    Boguta, M.4    Martin, N.C.5    Hopper, A.K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.