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Volumn 2, Issue 4, 2012, Pages 738-747

Confinement to Organelle-Associated Inclusion Structures Mediates Asymmetric Inheritance of Aggregated Protein in Budding Yeast

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 104;

EID: 84868149498     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2012.08.024     Document Type: Article
Times cited : (160)

References (28)
  • 1
    • 0242585476 scopus 로고    scopus 로고
    • Asymmetric inheritance of oxidatively damaged proteins during cytokinesis
    • Aguilaniu H., Gustafsson L., Rigoulet M., Nyström T. Asymmetric inheritance of oxidatively damaged proteins during cytokinesis. Science 2003, 299:1751-1753.
    • (2003) Science , vol.299 , pp. 1751-1753
    • Aguilaniu, H.1    Gustafsson, L.2    Rigoulet, M.3    Nyström, T.4
  • 2
    • 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., Boeke J.D. Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast 1998, 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
  • 5
    • 34547410267 scopus 로고    scopus 로고
    • Sir2p-dependent protein segregation gives rise to a superior reactive oxygen species management in the progeny of Saccharomyces cerevisiae
    • Erjavec N., Nyström T. Sir2p-dependent protein segregation gives rise to a superior reactive oxygen species management in the progeny of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 2007, 104:10877-10881.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 10877-10881
    • Erjavec, N.1    Nyström, T.2
  • 6
    • 34948846000 scopus 로고    scopus 로고
    • Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregation-remodeling factor Hsp104p
    • Erjavec N., Larsson L., Grantham J., Nyström T. Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregation-remodeling factor Hsp104p. Genes Dev. 2007, 21:2410-2421.
    • (2007) Genes Dev. , vol.21 , pp. 2410-2421
    • Erjavec, N.1    Larsson, L.2    Grantham, J.3    Nyström, T.4
  • 7
    • 79955703186 scopus 로고    scopus 로고
    • Phosphoinositide [PI(3,5)P2] lipid-dependent regulation of the general transcriptional regulator Tup1
    • Han B.K., Emr S.D. Phosphoinositide [PI(3,5)P2] lipid-dependent regulation of the general transcriptional regulator Tup1. Genes Dev. 2011, 25:984-995.
    • (2011) Genes Dev. , vol.25 , pp. 984-995
    • Han, B.K.1    Emr, S.D.2
  • 8
    • 56949107726 scopus 로고    scopus 로고
    • A mother's sacrifice: what is she keeping for herself?
    • Henderson K.A., Gottschling D.E. A mother's sacrifice: what is she keeping for herself?. Curr. Opin. Cell Biol. 2008, 20:723-728.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 723-728
    • Henderson, K.A.1    Gottschling, D.E.2
  • 10
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • Kaganovich D., Kopito R., Frydman J. Misfolded proteins partition between two distinct quality control compartments. Nature 2008, 454:1088-1095.
    • (2008) Nature , vol.454 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 11
    • 74549184412 scopus 로고    scopus 로고
    • The polarisome is required for segregation and retrograde transport of protein aggregates
    • Liu B., Larsson L., Caballero A., Hao X., Oling D., Grantham J., Nyström T. The polarisome is required for segregation and retrograde transport of protein aggregates. Cell 2010, 140:257-267.
    • (2010) Cell , vol.140 , pp. 257-267
    • Liu, B.1    Larsson, L.2    Caballero, A.3    Hao, X.4    Oling, D.5    Grantham, J.6    Nyström, T.7
  • 13
    • 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., Demarini D.J., Shah N.G., Wach A., Brachat A., Philippsen P., Pringle J.R. Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 1998, 14:953-961.
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 14
    • 79251494142 scopus 로고    scopus 로고
    • Spatial protein quality control and the evolution of lineage-specific ageing
    • Nyström T. Spatial protein quality control and the evolution of lineage-specific ageing. Philos. Trans. R. Soc. Lond. B Biol. Sci. 2011, 366:71-75.
    • (2011) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.366 , pp. 71-75
    • Nyström, T.1
  • 17
    • 3142677196 scopus 로고    scopus 로고
    • Cargo proteins facilitate the formation of transport vesicles in the cytoplasm to vacuole targeting pathway
    • Shintani T., Klionsky D.J. Cargo proteins facilitate the formation of transport vesicles in the cytoplasm to vacuole targeting pathway. J. Biol. Chem. 2004, 279:29889-29894.
    • (2004) J. Biol. Chem. , vol.279 , pp. 29889-29894
    • Shintani, T.1    Klionsky, D.J.2
  • 18
    • 2942722444 scopus 로고    scopus 로고
    • Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers
    • Shorter J., Lindquist S. Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science 2004, 304:1793-1797.
    • (2004) Science , vol.304 , pp. 1793-1797
    • Shorter, J.1    Lindquist, S.2
  • 19
    • 33746405081 scopus 로고    scopus 로고
    • Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities
    • Shorter J., Lindquist S. Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities. Mol. Cell 2006, 23:425-438.
    • (2006) Mol. Cell , vol.23 , pp. 425-438
    • Shorter, J.1    Lindquist, S.2
  • 20
    • 81355149538 scopus 로고    scopus 로고
    • Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae
    • Specht S., Miller S.B., Mogk A., Bukau B. Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae. J. Cell Biol. 2011, 195:617-629.
    • (2011) J. Cell Biol. , vol.195 , pp. 617-629
    • Specht, S.1    Miller, S.B.2    Mogk, A.3    Bukau, B.4
  • 21
    • 66749115386 scopus 로고    scopus 로고
    • Amyloid deposits: protection against toxic protein species?
    • Treusch S., Cyr D.M., Lindquist S. Amyloid deposits: protection against toxic protein species?. Cell Cycle 2009, 8:1668-1674.
    • (2009) Cell Cycle , vol.8 , pp. 1668-1674
    • Treusch, S.1    Cyr, D.M.2    Lindquist, S.3
  • 22
    • 77958487260 scopus 로고    scopus 로고
    • Cellular strategies for controlling protein aggregation
    • Tyedmers J., Mogk A., Bukau B. Cellular strategies for controlling protein aggregation. Nat. Rev. Mol. Cell Biol. 2010, 11:777-788.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 777-788
    • Tyedmers, J.1    Mogk, A.2    Bukau, B.3
  • 23
    • 77952711519 scopus 로고    scopus 로고
    • Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentation
    • Tyedmers J., Treusch S., Dong J., McCaffery J.M., Bevis B., Lindquist S. Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentation. Proc. Natl. Acad. Sci. USA 2010, 107:8633-8638.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 8633-8638
    • Tyedmers, J.1    Treusch, S.2    Dong, J.3    McCaffery, J.M.4    Bevis, B.5    Lindquist, S.6
  • 24
    • 0026737363 scopus 로고
    • Systematic mutational analysis of the yeast ACT1 gene
    • Wertman K.F., Drubin D.G., Botstein D. Systematic mutational analysis of the yeast ACT1 gene. Genetics 1992, 132:337-350.
    • (1992) Genetics , vol.132 , pp. 337-350
    • Wertman, K.F.1    Drubin, D.G.2    Botstein, D.3
  • 25
    • 84864387363 scopus 로고    scopus 로고
    • Chaperone networks in protein disaggregation and prion propagation
    • Winkler J., Tyedmers J., Bukau B., Mogk A. Chaperone networks in protein disaggregation and prion propagation. J. Struct. Biol. 2012, 179:152-160.
    • (2012) J. Struct. Biol. , vol.179 , pp. 152-160
    • Winkler, J.1    Tyedmers, J.2    Bukau, B.3    Mogk, A.4
  • 27
    • 84864019027 scopus 로고    scopus 로고
    • Molecular phenotyping of aging in single yeast cells using a novel microfluidic device
    • Xie Z., Zhang Y., Zou K., Brandman O., Luo C., Ouyang Q., Li H. Molecular phenotyping of aging in single yeast cells using a novel microfluidic device. Aging Cell 2012, 11:599-606.
    • (2012) Aging Cell , vol.11 , pp. 599-606
    • Xie, Z.1    Zhang, Y.2    Zou, K.3    Brandman, O.4    Luo, C.5    Ouyang, Q.6    Li, H.7
  • 28
    • 81855227611 scopus 로고    scopus 로고
    • Motility and segregation of Hsp104-associated protein aggregates in budding yeast
    • Zhou C., Slaughter B.D., Unruh J.R., Eldakak A., Rubinstein B., Li R. Motility and segregation of Hsp104-associated protein aggregates in budding yeast. Cell 2011, 147:1186-1196.
    • (2011) Cell , vol.147 , pp. 1186-1196
    • Zhou, C.1    Slaughter, B.D.2    Unruh, J.R.3    Eldakak, A.4    Rubinstein, B.5    Li, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.