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Volumn 19, Issue 3, 2008, Pages 1022-1031

Dissection of the carboxyl-terminal domain of the proteasomal subunit Rpn11 in maintenance of mitochondrial structure and function

Author keywords

[No Author keywords available]

Indexed keywords

MITOCHONDRIAL PROTEIN; PROTEIN RPN11; UNCLASSIFIED DRUG;

EID: 41649083740     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E07-07-0717     Document Type: Article
Times cited : (35)

References (40)
  • 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
    • 0027535182 scopus 로고
    • Patterns of mitochondrial sorting in yeast zygotes
    • Azpiroz, R., and Butow, R. A. (1993). Patterns of mitochondrial sorting in yeast zygotes. Mol. Biol. Cell 4, 21-36.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 21-36
    • Azpiroz, R.1    Butow, R.A.2
  • 3
    • 0034966332 scopus 로고    scopus 로고
    • Mitochondrial inheritance in budding yeast
    • Boldogh, I. R., Yang, H. C., and Pon, L. A. (2001). Mitochondrial inheritance in budding yeast. Traffic 2, 368-374.
    • (2001) Traffic , vol.2 , pp. 368-374
    • Boldogh, I.R.1    Yang, H.C.2    Pon, L.A.3
  • 4
    • 23644435760 scopus 로고    scopus 로고
    • Mitochondrial movement and inheritance in budding yeast
    • Boldogh, I. R., Fehrenbacher, K. L., Yang, H. C., and Pon, L. A. (2005). Mitochondrial movement and inheritance in budding yeast. Gene 354, 28-36.
    • (2005) Gene , vol.354 , pp. 28-36
    • Boldogh, I.R.1    Fehrenbacher, K.L.2    Yang, H.C.3    Pon, L.A.4
  • 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
    • 1842665662 scopus 로고    scopus 로고
    • Mitochondrial signaling: The retrograde response
    • Butow, R. A., and Avadhani, N. G. (2004). Mitochondrial signaling: the retrograde response. Mol. Cell 14, 1-15.
    • (2004) Mol. Cell , vol.14 , pp. 1-15
    • Butow, R.A.1    Avadhani, N.G.2
  • 7
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: Critical control points
    • Danial, N. N., and Korsmeyer, S. J. (2004). Cell death: critical control points. Cell 116, 205-219.
    • (2004) Cell , vol.116 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 8
    • 35448960851 scopus 로고    scopus 로고
    • Functions and dysfunctions of mitochondrial dynamics
    • Detmer, S. A., and Chan, D. C. (2007). Functions and dysfunctions of mitochondrial dynamics. Nat. Rev. Mol. Cell Biol. 8, 870-879.
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 870-879
    • Detmer, S.A.1    Chan, D.C.2
  • 10
    • 12144280303 scopus 로고    scopus 로고
    • Mdm31 and Mdm32 are inner membrane proteins required for maintenance of mitochondrial shape and stability of mitochondrial DNA nucleoids in yeast
    • Dimmer, K. S., Jakobs, S., Vogel, F., Altmann, K., and Westermann, B. (2005). Mdm31 and Mdm32 are inner membrane proteins required for maintenance of mitochondrial shape and stability of mitochondrial DNA nucleoids in yeast. J. Cell Biol. 168, 103-115.
    • (2005) J. Cell Biol , vol.168 , pp. 103-115
    • Dimmer, K.S.1    Jakobs, S.2    Vogel, F.3    Altmann, K.4    Westermann, B.5
  • 11
    • 33748327051 scopus 로고    scopus 로고
    • Non-redundant roles of mitochondria-associated FBox proteins, Mfb1 and Mdm30, in maintenance of mitochondria morphology in yeast
    • Dürr, M., Escobar-Henriquez, M., Merz, S., Geimer, S., Langer, T., and Westermann, B. (2006). Non-redundant roles of mitochondria-associated FBox proteins, Mfb1 and Mdm30, in maintenance of mitochondria morphology in yeast. Mol. Biol. Cell 17, 3745-3755.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3745-3755
    • Dürr, M.1    Escobar-Henriquez, M.2    Merz, S.3    Geimer, S.4    Langer, T.5    Westermann, B.6
  • 12
    • 33747389446 scopus 로고    scopus 로고
    • Regulation of mitochondrial fusion by the F-box protein Mdm30 involves proteasome- independent turnover of Fzo1
    • Escobar-Henriques, M., Westermann, B., and Langer, T. (2006). Regulation of mitochondrial fusion by the F-box protein Mdm30 involves proteasome- independent turnover of Fzo1. 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
    • 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
  • 14
    • 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
  • 15
    • 0037126632 scopus 로고    scopus 로고
    • Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome
    • Fu, H., Reis, N., Lee, Y., Glickman, M. H., and Vierstra, R. D. (2001). Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome. EMBO J. 20, 7096-7107.
    • (2001) EMBO J , vol.20 , pp. 7096-7107
    • Fu, H.1    Reis, N.2    Lee, Y.3    Glickman, M.H.4    Vierstra, R.D.5
  • 17
    • 34250204271 scopus 로고    scopus 로고
    • The machines that divide and fuse mitochondria
    • Hoppins, S., Lackner, L., and 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
  • 18
    • 34347398050 scopus 로고    scopus 로고
    • The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division
    • Karbowski, M., Neutzner, A., and Youle, R. J. (2007). The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division. J. Cell Biol. 178, 71-84.
    • (2007) J. Cell Biol , vol.178 , pp. 71-84
    • Karbowski, M.1    Neutzner, A.2    Youle, R.J.3
  • 19
    • 0032203713 scopus 로고    scopus 로고
    • Arabidopsis homologs of a c-Jun coactivator are present both in monomeric form and in the COP9 complex, and their abundance is differentially affected by the pleiotropic cop/det/fus mutations
    • Kwok, S. F., Solano, R., Tsuge, T., Chamovitz, D. A., Ecker, J. R., Matsui, M., and Deng, X. W. (1998). Arabidopsis homologs of a c-Jun coactivator are present both in monomeric form and in the COP9 complex, and their abundance is differentially affected by the pleiotropic cop/det/fus mutations. Plant Cell 10, 1779-1790.
    • (1998) Plant Cell , vol.10 , pp. 1779-1790
    • Kwok, S.F.1    Solano, R.2    Tsuge, T.3    Chamovitz, D.A.4    Ecker, J.R.5    Matsui, M.6    Deng, X.W.7
  • 20
    • 0037910318 scopus 로고    scopus 로고
    • Constriction and Dnm1p recruitment are distinct processes in mitochondrial fission
    • Legesse-Miller, A., Massol, R. H., and Kirchhausen, T. (2003). Constriction and Dnm1p recruitment are distinct processes in mitochondrial fission. Mol. Biol. Cell 14, 1953-1963.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1953-1963
    • Legesse-Miller, A.1    Massol, R.H.2    Kirchhausen, T.3
  • 21
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M. S., McKenzie, A., 3rd, Demarini, D. J., Shah, N. G., Wach, A., Brachat, A., Philippsen, P., and Pringle, J. R. (1998). Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14, 953-961.
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie 3rd, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 22
    • 41649099377 scopus 로고    scopus 로고
    • MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function
    • Maytal-Kivity, V., Reis, N., Hofmann, K., and Glickman, M. H. (2002). MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function. BMC Biochem. 20, 3-28.
    • (2002) BMC Biochem , vol.20 , pp. 3-28
    • Maytal-Kivity, V.1    Reis, N.2    Hofmann, K.3    Glickman, M.H.4
  • 23
    • 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
  • 24
    • 33749253910 scopus 로고    scopus 로고
    • MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change mitochondrial morphology
    • Nakamura, N., Kimura, Y., Tokuda, M., Honda, S., and Hirose, S. (2006). MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change mitochondrial morphology. EMBO Rep. 7, 1019-1022.
    • (2006) EMBO Rep , vol.7 , pp. 1019-1022
    • Nakamura, N.1    Kimura, Y.2    Tokuda, M.3    Honda, S.4    Hirose, S.5
  • 25
    • 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
  • 26
    • 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
  • 27
    • 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
  • 28
    • 0031709394 scopus 로고    scopus 로고
    • A mutation in a novel yeast proteasomal gene, RPN11/MPR1, produces a 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 a 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
  • 29
    • 0037029053 scopus 로고    scopus 로고
    • Mitochondrial effects of the pleiotropic proteasomal mutation mpr1/rpn11, uncoupling from cell cycle defects in extragenic revertants
    • Rinaldi, T., Ricordy, R., Bolotin-Fukuhara, M., and Frontali, L. (2002). Mitochondrial effects of the pleiotropic proteasomal mutation mpr1/rpn11, uncoupling from cell cycle defects in extragenic revertants. Gene 286, 43-51.
    • (2002) Gene , vol.286 , pp. 43-51
    • Rinaldi, T.1    Ricordy, R.2    Bolotin-Fukuhara, M.3    Frontali, L.4
  • 30
    • 3142723187 scopus 로고    scopus 로고
    • Participation of the proteasomal lid subunit Rpn11 in mitochondrial morphology and function is mapped to a distinct C-terminal domain
    • Rinaldi, T., Pick, E., Gambadoro, A., Zilli, S., Maytal-Kivity, V., Frontali, L., and Glickman, M. H. (2004). Participation of the proteasomal lid subunit Rpn11 in mitochondrial morphology and function is mapped to a distinct C-terminal domain. Biochem. J. 381, 275-285.
    • (2004) Biochem. J , vol.381 , pp. 275-285
    • Rinaldi, T.1    Pick, E.2    Gambadoro, A.3    Zilli, S.4    Maytal-Kivity, V.5    Frontali, L.6    Glickman, M.H.7
  • 31
    • 0028284879 scopus 로고
    • Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding
    • Rowley, N., Prip-Buus, C., Westermann, B., Brown, C., Schwarz, E., Barrell, B., and Neupert, W. (1994). Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding. Cell 77, 249-259.
    • (1994) Cell , vol.77 , pp. 249-259
    • Rowley, N.1    Prip-Buus, C.2    Westermann, B.3    Brown, C.4    Schwarz, E.5    Barrell, B.6    Neupert, W.7
  • 32
    • 33747347236 scopus 로고    scopus 로고
    • Structural organization of the 19S proteasome lid: Insights from MS of intact complexes
    • Sharon, M., Taverner, T., Ambroggio, X. I., Deshaies, R. J., and Robinson, C. V. (2006). Structural organization of the 19S proteasome lid: insights from MS of intact complexes. PLoS Biol. 4, 1314-1323.
    • (2006) PLoS Biol , vol.4 , pp. 1314-1323
    • Sharon, M.1    Taverner, T.2    Ambroggio, X.I.3    Deshaies, R.J.4    Robinson, C.V.5
  • 33
    • 0036536714 scopus 로고    scopus 로고
    • Mitochondrial dynamics and division in budding yeast
    • Shaw, J. M., and Nunnari, J. (2002). Mitochondrial dynamics and division in budding yeast. Trends Cell Biol. 12, 178-184.
    • (2002) Trends Cell Biol , vol.12 , pp. 178-184
    • Shaw, J.M.1    Nunnari, J.2
  • 34
    • 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. Cytoskelet. 37, 199-210.
    • (1997) Cell Motil. Cytoskelet , vol.37 , pp. 199-210
    • Simon, V.R.1    Karmon, S.L.2    Pon, L.A.3
  • 35
  • 36
    • 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
  • 37
    • 0030040690 scopus 로고    scopus 로고
    • Organelle inheritance
    • Warren, G., and Wickner, W. (1996). Organelle inheritance. Cell 84, 395-400.
    • (1996) Cell , vol.84 , pp. 395-400
    • Warren, G.1    Wickner, W.2
  • 38
    • 0037179694 scopus 로고    scopus 로고
    • A cryptic protease couples deubiquitination and degradation by the proteasome
    • Yao, T., and Cohen, R. E. (2002). A cryptic protease couples deubiquitination and degradation by the proteasome. Nature 419, 403-407.
    • (2002) Nature , vol.419 , pp. 403-407
    • Yao, T.1    Cohen, R.E.2
  • 39
    • 1442309968 scopus 로고    scopus 로고
    • Mmm2p, a mitochondrial outer membrane protein required for yeast mitochondrial shape and maintenance of mtDNA nucleoids
    • Youngman, M. J., Hobbs, A. E., Burgess, S. M., Srinivasan, M., and Jensen, R. E. (2004). Mmm2p, a mitochondrial outer membrane protein required for yeast mitochondrial shape and maintenance of mtDNA nucleoids. J. Cell Biol. 164(5), 677-88.
    • (2004) J. Cell Biol , vol.164 , Issue.5 , pp. 677-688
    • Youngman, M.J.1    Hobbs, A.E.2    Burgess, S.M.3    Srinivasan, M.4    Jensen, R.E.5
  • 40
    • 33747613595 scopus 로고    scopus 로고
    • A novel mitochondrial ubiquitin ligase plays a critical role in mitochondrial dynamics
    • Yonashiro, R. et al. (2006). A novel mitochondrial ubiquitin ligase plays a critical role in mitochondrial dynamics. EMBO J. 25, 3618-3626.
    • (2006) EMBO J , vol.25 , pp. 3618-3626
    • Yonashiro, R.1


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