메뉴 건너뛰기




Volumn 18, Issue 1, 2007, Pages 153-165

The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome system

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CARBOXYPEPTIDASE C; CARBOXYPEPTIDASE YSCY; CHAPERONE; CYTOPLASM PROTEIN; ENZYME; GREEN FLUORESCENT PROTEIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 104; HEAT SHOCK PROTEIN 26; HEAT SHOCK PROTEIN 42; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; MISFOLDED PROTEIN; MUTANT PROTEIN; ORNITHINE DECARBOXYLASE; PROTEASOME; PROTEIN; PROTEIN SSA1P; PROTEIN UBC4P; PROTEIN UBC5P; PROTEIN YDJ1P; SIGNAL PEPTIDE; UBIQUITIN; UBIQUITIN CONJUGATING ENZYME; UNCLASSIFIED DRUG;

EID: 33846107847     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E06-04-0338     Document Type: Article
Times cited : (136)

References (92)
  • 1
    • 23744457478 scopus 로고    scopus 로고
    • Versatility of the endoplasmic reticulum protein folding factory
    • Anken, E., Braakman, I., and Craig, E. (2005). Versatility of the endoplasmic reticulum protein folding factory. Crit. Rev. Biochem. Mol. Biol. 40, 191-228.
    • (2005) Crit. Rev. Biochem. Mol. Biol , vol.40 , pp. 191-228
    • Anken, E.1    Braakman, I.2    Craig, E.3
  • 4
    • 0029954823 scopus 로고    scopus 로고
    • Functional interaction of cytosolic hsp70 and a DnaJ-related protein, Ydj1p, in protein translocation in vivo
    • Becker, J., Walter, W., Yan, W., and Craig, E. A. (1996). Functional interaction of cytosolic hsp70 and a DnaJ-related protein, Ydj1p, in protein translocation in vivo. Mol. Cell Biol. 16, 4378-4386.
    • (1996) Mol. Cell Biol , vol.16 , pp. 4378-4386
    • Becker, J.1    Walter, W.2    Yan, W.3    Craig, E.A.4
  • 5
    • 0033208984 scopus 로고    scopus 로고
    • ER protein quality control and proteasome-mediated protein degradation
    • Brodsky, J. L., and McCracken, A. A. (1999). ER protein quality control and proteasome-mediated protein degradation. Semin. Cell Dev. Biol. 10, 507-513.
    • (1999) Semin. Cell Dev. Biol , vol.10 , pp. 507-513
    • Brodsky, J.L.1    McCracken, A.A.2
  • 6
    • 0033525198 scopus 로고    scopus 로고
    • The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct
    • Brodsky, J. L., Werner, E. D., Dubas, M. K., Goeckeler, J. L., Kruse, K. B., and McCracken, A. A. (1999). The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct. J. Biol. Chem. 274, 3453-3460.
    • (1999) J. Biol. Chem , vol.274 , pp. 3453-3460
    • Brodsky, J.L.1    Werner, E.D.2    Dubas, M.K.3    Goeckeler, J.L.4    Kruse, K.B.5    McCracken, A.A.6
  • 7
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukan, B., Weissman, J., and Horwich, A. (2006). Molecular chaperones and protein quality control. Cell 125, 443-451.
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukan, B.1    Weissman, J.2    Horwich, A.3
  • 8
    • 0027102871 scopus 로고
    • YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism
    • Caplan, A. J., Cyr, D. M., and Douglas, M. G. (1992). YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Cell 71, 1143-1155.
    • (1992) Cell , vol.71 , pp. 1143-1155
    • Caplan, A.J.1    Cyr, D.M.2    Douglas, M.G.3
  • 9
    • 21244466032 scopus 로고    scopus 로고
    • A chaperone pathway in protein disaggregation, Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104
    • Cashikar, A. G., Duennwald, M., and Lindquist, S. L. (2005). A chaperone pathway in protein disaggregation, Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104. J. Biol. Chem. 280, 23869-23875.
    • (2005) J. Biol. Chem , vol.280 , pp. 23869-23875
    • Cashikar, A.G.1    Duennwald, M.2    Lindquist, S.L.3
  • 10
    • 0031945665 scopus 로고    scopus 로고
    • Structure, function and evolution of DnaJ: Conservation and adaptation of chaperone function
    • Cheetham, M. E., and Caplan, A. J. (1998). Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function. Cell Stress Chaperones 3, 28-36.
    • (1998) Cell Stress Chaperones , vol.3 , pp. 28-36
    • Cheetham, M.E.1    Caplan, A.J.2
  • 11
    • 0025804582 scopus 로고
    • Regulated import and degradation of a cytosolic protein in the yeast vacuole
    • Chiang, H. L., and Schekman, R. (1991). Regulated import and degradation of a cytosolic protein in the yeast vacuole. Nature 350, 313-318.
    • (1991) Nature , vol.350 , pp. 313-318
    • Chiang, H.L.1    Schekman, R.2
  • 13
    • 0036629253 scopus 로고    scopus 로고
    • Protein quality control: U-box-containing E3 ubiquitin ligases join the fold
    • Cyr, D. M., Hohfeld, J., and Patterson, C. (2002). Protein quality control: U-box-containing E3 ubiquitin ligases join the fold. Trends Biochem. Sci. 27, 368-375.
    • (2002) Trends Biochem. Sci , vol.27 , pp. 368-375
    • Cyr, D.M.1    Hohfeld, J.2    Patterson, C.3
  • 15
    • 0035899897 scopus 로고    scopus 로고
    • Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/ proteasome coupling
    • Demand, J., Alberti, S., Patterson, C., and Hohfeld, J. (2001). Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/ proteasome coupling. Curr. Biol. 11, 1569-1577.
    • (2001) Curr. Biol , vol.11 , pp. 1569-1577
    • Demand, J.1    Alberti, S.2    Patterson, C.3    Hohfeld, J.4
  • 16
    • 11444271010 scopus 로고    scopus 로고
    • Chaperone-assisted folding of newly synthesized proteins in the cytosol
    • Deuerling, E., and Bukau, B. (2004). Chaperone-assisted folding of newly synthesized proteins in the cytosol. Crit. Rev. Biochem. Mol. Biol. 39, 261-277.
    • (2004) Crit. Rev. Biochem. Mol. Biol , vol.39 , pp. 261-277
    • Deuerling, E.1    Bukau, B.2
  • 17
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C. M. (2003). Protein folding and misfolding. Nature 426, 884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 18
    • 23144449583 scopus 로고    scopus 로고
    • Delivery of ubiquitinated substrates to protein-unfolding machines
    • Elsasser, S., and Finley, D. (2005). Delivery of ubiquitinated substrates to protein-unfolding machines. Nat. Cell Biol. 7, 742-749.
    • (2005) Nat. Cell Biol , vol.7 , pp. 742-749
    • Elsasser, S.1    Finley, D.2
  • 19
    • 0028010544 scopus 로고
    • 2.8-A structure of yeast serine carboxypeptidase
    • Endrizzi, J. A., Breddam, K., and Remington, S. J. (1994). 2.8-A structure of yeast serine carboxypeptidase. Biochemistry 33, 11106-11120.
    • (1994) Biochemistry , vol.33 , pp. 11106-11120
    • Endrizzi, J.A.1    Breddam, K.2    Remington, S.J.3
  • 20
    • 9644280977 scopus 로고    scopus 로고
    • Cooperation of molecular chaperones with the ubiquitin/proteasome system
    • Esser, C., Alberti, S., and Hohfeld, J. (2004). Cooperation of molecular chaperones with the ubiquitin/proteasome system. Biochim. Biophys. Acta 1695, 171-188.
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 171-188
    • Esser, C.1    Alberti, S.2    Hohfeld, J.3
  • 21
    • 1242269219 scopus 로고    scopus 로고
    • Mechanisms for regulation of Hsp70 function by Hsp40
    • Fan, C. Y., Lee, S., and Cyr, D. M. (2003). Mechanisms for regulation of Hsp70 function by Hsp40. Cell Stress Chaperones 8, 309-316.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 309-316
    • Fan, C.Y.1    Lee, S.2    Cyr, D.M.3
  • 22
    • 0027137885 scopus 로고
    • Analysis of two mutated vacuolar proteins reveals a degradation pathway in the endoplasmic reticulum or a related compartment of yeast
    • Finger, A., Knop, M., and Wolf, D. H. (1993). Analysis of two mutated vacuolar proteins reveals a degradation pathway in the endoplasmic reticulum or a related compartment of yeast. Eur. J. Biochem. 218, 565-574.
    • (1993) Eur. J. Biochem , vol.218 , pp. 565-574
    • Finger, A.1    Knop, M.2    Wolf, D.H.3
  • 23
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • Frydman, J. (2001). Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu. Rev. Biochem. 70, 603-647.
    • (2001) Annu. Rev. Biochem , vol.70 , pp. 603-647
    • Frydman, J.1
  • 24
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp 40, a novel chaperone system that rescues previously aggregated proteins
    • Glover, J. R., and Lindquist, S. (1998), Hsp104, Hsp70, and Hsp 40, a novel chaperone system that rescues previously aggregated proteins. Cell 94, 73-82.
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 25
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg, A. L. (2003). Protein degradation and protection against misfolded or damaged proteins. Nature 426, 895-899.
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 27
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F. U. (1996). Molecular chaperones in cellular protein folding. Nature 381, 571-579.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 28
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F. U., and Hayer-Hartl, M. (2002). Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 29
    • 4544290828 scopus 로고    scopus 로고
    • Protein degradation: Recognition of ubiquitinylated substrates
    • Hartmann-Petersen, R., and Gordon, C. (2004). Protein degradation: recognition of ubiquitinylated substrates. Curr. Biol. 14, R754-R756.
    • (2004) Curr. Biol , vol.14
    • Hartmann-Petersen, R.1    Gordon, C.2
  • 30
    • 1442289304 scopus 로고    scopus 로고
    • Hsp42 is the general small heat shuck protein in the cytosol of Saccharomyces cerevisiae
    • Haslbeck, M., Braun, N., Stromer, T., Richter, B., Model, N., Weinkauf, S., and Buchner, J. (2004). Hsp42 is the general small heat shuck protein in the cytosol of Saccharomyces cerevisiae. EMBO J. 23, 638-649.
    • (2004) EMBO J , vol.23 , pp. 638-649
    • Haslbeck, M.1    Braun, N.2    Stromer, T.3    Richter, B.4    Model, N.5    Weinkauf, S.6    Buchner, J.7
  • 32
    • 0025980627 scopus 로고
    • Proteinase yscE, the yeast proteasome/multicatalytic- multifunctional proteinase; mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival
    • Heinemeyer, W., Kleinschmidt, J. A., Saidowsky, J., Escher, C., and Wolf, D. H. (1991). Proteinase yscE, the yeast proteasome/multicatalytic- multifunctional proteinase; mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival. EMBO J. 10, 555-562.
    • (1991) EMBO J , vol.10 , pp. 555-562
    • Heinemeyer, W.1    Kleinschmidt, J.A.2    Saidowsky, J.3    Escher, C.4    Wolf, D.H.5
  • 34
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquiuin-proteasome pathway
    • Hiller, M. M., Finger, A., Schweizer, M., and Wolf, D. H. (1996). ER degradation of a misfolded luminal protein by the cytosolic ubiquiuin-proteasome pathway. Science 273, 1725-1728.
    • (1996) Science , vol.273 , pp. 1725-1728
    • Hiller, M.M.1    Finger, A.2    Schweizer, M.3    Wolf, D.H.4
  • 35
    • 9644300910 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated protein degradation-one model fits all?
    • Hirsch, C., Jarosch, E., Sommer, T., and Wolf, D. H. (2004). Endoplasmic reticulum-associated protein degradation-one model fits all? Biochim. Biophys. Acta 1695, 215-223.
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 215-223
    • Hirsch, C.1    Jarosch, E.2    Sommer, T.3    Wolf, D.H.4
  • 36
    • 0029870836 scopus 로고    scopus 로고
    • Protein degradation or regulation: Ub the judge
    • Hochstrasser, M. (1996). Protein degradation or regulation: Ub the judge. Cell 84, 813-815.
    • (1996) Cell , vol.84 , pp. 813-815
    • Hochstrasser, M.1
  • 37
    • 3242732010 scopus 로고    scopus 로고
    • Ubiquitin-free routes into the proteasome
    • Hoyt, M. A., and Coffino, P. (2004), Ubiquitin-free routes into the proteasome. Cell Mol. Life Sci. 61, 1596-1600.
    • (2004) Cell Mol. Life Sci , vol.61 , pp. 1596-1600
    • Hoyt, M.A.1    Coffino, P.2
  • 38
    • 0012919901 scopus 로고    scopus 로고
    • Ubiquitin-independent mechanisms of mouse ornithine decarboxylase degradation are conserved between mammalian and fungal cells
    • Hoyt, M. A., Zhang, M., and Coffino, P. (2003). Ubiquitin-independent mechanisms of mouse ornithine decarboxylase degradation are conserved between mammalian and fungal cells. J. Biol. Chem. 278, 12135-12143.
    • (2003) J. Biol. Chem , vol.278 , pp. 12135-12143
    • Hoyt, M.A.1    Zhang, M.2    Coffino, P.3
  • 39
    • 4444355303 scopus 로고    scopus 로고
    • Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multi-spanning membrane protein and a soluble luminal protein
    • Huyer, C., Piluek, W. F., Fansler, Z., Kreft, S. G., Hochstransser, M., Brodsky, J. L., and Michaelis, S. (2004). Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multi-spanning membrane protein and a soluble luminal protein. J. Biol. Chem. 279, 38369-38378.
    • (2004) J. Biol. Chem , vol.279 , pp. 38369-38378
    • Huyer, C.1    Piluek, W.F.2    Fansler, Z.3    Kreft, S.G.4    Hochstransser, M.5    Brodsky, J.L.6    Michaelis, S.7
  • 40
    • 0028260121 scopus 로고
    • Selective retention of secretory proteins in the yeast endoplasmic reticulum by treatment of cells with a reducing agent
    • Jamsa, E., Simonen, M., and Makarow, M. (1994). Selective retention of secretory proteins in the yeast endoplasmic reticulum by treatment of cells with a reducing agent. Yeast 10, 355-370.
    • (1994) Yeast , vol.10 , pp. 355-370
    • Jamsa, E.1    Simonen, M.2    Makarow, M.3
  • 42
    • 0035900793 scopus 로고    scopus 로고
    • CHIP is a U-box-dependent E3 ubiquitin ligase: Identification of Hsc70 as a target for ubiquitylation
    • Jiang, J., Ballinger, C. A., Wu, Y., Dai, Q., Cyr, D. M., Hohfeld, J., and Patterson, C. (2001). CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation. J. Biol. Chem. 276, 42938-42944.
    • (2001) J. Biol. Chem , vol.276 , pp. 42938-42944
    • Jiang, J.1    Ballinger, C.A.2    Wu, Y.3    Dai, Q.4    Cyr, D.M.5    Hohfeld, J.6    Patterson, C.7
  • 43
    • 0035911158 scopus 로고    scopus 로고
    • An essential role for the substrate-binding region of Hsp40s in Saccharomyces cerevisiae
    • Johnson, J. L. and Craig, E. A. (2001). An essential role for the substrate-binding region of Hsp40s in Saccharomyces cerevisiae. J. Cell Biol. 152, 851-856.
    • (2001) J. Cell Biol , vol.152 , pp. 851-856
    • Johnson, J.L.1    Craig, E.A.2
  • 44
    • 0035890265 scopus 로고    scopus 로고
    • Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53
    • King, F. W., Wawrzynow, A., Hohfeld, J., and Zylicz, M. (2001). Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53. EMBO J. 20, 6297-6305.
    • (2001) EMBO J , vol.20 , pp. 6297-6305
    • King, F.W.1    Wawrzynow, A.2    Hohfeld, J.3    Zylicz, M.4
  • 45
    • 3142587059 scopus 로고    scopus 로고
    • Protein folding and quality control in the endoplasmic reticulum
    • Kleizen, B., and Braakman, I. (2004). Protein folding and quality control in the endoplasmic reticulum. Curr. Opin. Cell Biol. 16, 343-349.
    • (2004) Curr. Opin. Cell Biol , vol.16 , pp. 343-349
    • Kleizen, B.1    Braakman, I.2
  • 46
    • 0030041781 scopus 로고    scopus 로고
    • Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast
    • Knop, M., Finger, A., Braun, T., Hellmuth, K., and Wolf, D. H. (1996). Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast. EMBO J. 15, 753-763.
    • (1996) EMBO J , vol.15 , pp. 753-763
    • Knop, M.1    Finger, A.2    Braun, T.3    Hellmuth, K.4    Wolf, D.H.5
  • 47
    • 0027373715 scopus 로고
    • Vacuolar/ lysosomal proteolysis: Proteases, substrates, mechanisms
    • Knop, M., Schiffer, H. H., Rupp, S., and Wolf, D. H. (1993). Vacuolar/ lysosomal proteolysis: proteases, substrates, mechanisms. Curr. Opin. Cell Biol. 5, 990-996.
    • (1993) Curr. Opin. Cell Biol , vol.5 , pp. 990-996
    • Knop, M.1    Schiffer, H.H.2    Rupp, S.3    Wolf, D.H.4
  • 48
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito, R. R. (2000). Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 10, 524-530.
    • (2000) Trends Cell Biol , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 49
    • 0037566901 scopus 로고    scopus 로고
    • For whom the bell tolls: Protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection
    • Kostova, Z., and Wolf, D. H. (2003). For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection. EMBO J. 22, 2309-2317.
    • (2003) EMBO J , vol.22 , pp. 2309-2317
    • Kostova, Z.1    Wolf, D.H.2
  • 50
    • 17844382159 scopus 로고    scopus 로고
    • Importance of carbohydrate positioning in the recognition of mutated CPY for ER-associated degradation
    • Kostova, Z., and Wolf, D. H. (2005). Importance of carbohydrate positioning in the recognition of mutated CPY for ER-associated degradation. J. Cell Sci. 118, 1485-1492.
    • (2005) J. Cell Sci , vol.118 , pp. 1485-1492
    • Kostova, Z.1    Wolf, D.H.2
  • 51
    • 0001389495 scopus 로고    scopus 로고
    • Involvement of the molecular chaperone Ydj1 in the ubiquitin-dependent degradation of short-lived and abnormal proteins in Saccharomyces cerevisiae
    • Lee, D. H., Sherman, M. Y., and Goldberg, A. L. (1996). Involvement of the molecular chaperone Ydj1 in the ubiquitin-dependent degradation of short-lived and abnormal proteins in Saccharomyces cerevisiae. Mol. Cell Biol. 16, 4773-4781.
    • (1996) Mol. Cell Biol , vol.16 , pp. 4773-4781
    • Lee, D.H.1    Sherman, M.Y.2    Goldberg, A.L.3
  • 52
    • 11144255136 scopus 로고    scopus 로고
    • The efficiency of protein compartmentalization into the secretory pathway
    • Levine, C. G., Mitra, D., Sharma, A., Smith, C. L., and Hegde, R. S. (2005). The efficiency of protein compartmentalization into the secretory pathway. Mol. Biol. Cell 16, 279-291.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 279-291
    • Levine, C.G.1    Mitra, D.2    Sharma, A.3    Smith, C.L.4    Hegde, R.S.5
  • 53
    • 0037449572 scopus 로고    scopus 로고
    • Endoproteolytic activity of the proteasome
    • Liu, C. W., Corboy, M. J., DeMartino, C. N., and Thomas, P. J. (2003). Endoproteolytic activity of the proteasome. Science 299, 408-411.
    • (2003) Science , vol.299 , pp. 408-411
    • Liu, C.W.1    Corboy, M.J.2    DeMartino, C.N.3    Thomas, P.J.4
  • 54
    • 3142657524 scopus 로고    scopus 로고
    • Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104
    • Lum, K., Tkach, J. M., Vierling, E., and Glover, J. R. (2004). Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104. J. Biol. Chem. 279, 29139-29146.
    • (2004) J. Biol. Chem , vol.279 , pp. 29139-29146
    • Lum, K.1    Tkach, J.M.2    Vierling, E.3    Glover, J.R.4
  • 55
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: Cellular functions and molecular mechanism
    • Mayer, M. P., and Bukau, B. (2005). Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol. Life Sci. 62, 670-684.
    • (2005) Cell Mol. Life Sci , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 56
    • 20444413061 scopus 로고    scopus 로고
    • Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways
    • McClellan, A. J., Scott, M. D., and Frydman, J. (2005a). Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways. Cell 121, 739-748.
    • (2005) Cell , vol.121 , pp. 739-748
    • McClellan, A.J.1    Scott, M.D.2    Frydman, J.3
  • 57
    • 23144443884 scopus 로고    scopus 로고
    • Protein quality control: Chaperones culling corrupt conformations
    • McClellan, A. J., Tam, S., Kaganovich, D., and Frydman, J. (2005b). Protein quality control: chaperones culling corrupt conformations. Nat. Cell Biol. 7, 736-741.
    • (2005) Nat. Cell Biol , vol.7 , pp. 736-741
    • McClellan, A.J.1    Tam, S.2    Kaganovich, D.3    Frydman, J.4
  • 58
    • 4444320698 scopus 로고    scopus 로고
    • A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation
    • Medicherla, B., Kostova, Z., Schaefer, A., and Wolf, D. H. (2004). A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation, EMBO Rep. 5, 692-697.
    • (2004) EMBO Rep , vol.5 , pp. 692-697
    • Medicherla, B.1    Kostova, Z.2    Schaefer, A.3    Wolf, D.H.4
  • 59
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • Muchowski, P. J., and Wacker, J. L. (2005). Modulation of neurodegeneration by molecular chaperones. Nat. Rev. Neurosci. 6, 11-22.
    • (2005) Nat. Rev. Neurosci , vol.6 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 60
    • 0035684430 scopus 로고    scopus 로고
    • CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein
    • Murata, S., Minami, Y., Minami, M., Chiba, T., and Tanaka, K. (2001). CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein. EMBO Rep. 2, 1133-1138.
    • (2001) EMBO Rep , vol.2 , pp. 1133-1138
    • Murata, S.1    Minami, Y.2    Minami, M.3    Chiba, T.4    Tanaka, K.5
  • 61
    • 0030667932 scopus 로고    scopus 로고
    • In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone
    • Nathan, D. F., Vos, M. H. and Lindquist, S. (1997). In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone. Proc. Natl. Acad. Sci. USA 94, 12949-12936.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12949-12936
    • Nathan, D.F.1    Vos, M.H.2    Lindquist, S.3
  • 62
    • 0035947773 scopus 로고    scopus 로고
    • Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation
    • Nishikawa, S. P., Fewell, S. W., Kato, Y., Brodsky, J. L., and Endo, T. (2001). Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation. J. Cell Biol. 153, 1061-1070.
    • (2001) J. Cell Biol , vol.153 , pp. 1061-1070
    • Nishikawa, S.P.1    Fewell, S.W.2    Kato, Y.3    Brodsky, J.L.4    Endo, T.5
  • 64
    • 0027996115 scopus 로고
    • Protein disaggregation mediated by heat-shock protein Hsp104
    • Parsell, D. A., Kowal, A. S., Singer, M. A., and Lindquist, S. (1994). Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372, 475-478.
    • (1994) Nature , vol.372 , pp. 475-478
    • Parsell, D.A.1    Kowal, A.S.2    Singer, M.A.3    Lindquist, S.4
  • 65
    • 0027135501 scopus 로고
    • The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • Parsell, D. A., and Lindquist, S. (1993). The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annu. Rev. Genet 27, 437-496.
    • (1993) Annu. Rev. Genet , vol.27 , pp. 437-496
    • Parsell, D.A.1    Lindquist, S.2
  • 66
    • 0035658334 scopus 로고    scopus 로고
    • Divergent functional properties of the ribosome-associated molecular chaperone Ssb compared with other Hsp70s
    • Pfund, C., Huang, P., Lopez-Hoyo, N., and Craig, E. A. (2001). Divergent functional properties of the ribosome-associated molecular chaperone Ssb compared with other Hsp70s. Mol. Biol. Cell 12, 3773-3782.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3773-3782
    • Pfund, C.1    Huang, P.2    Lopez-Hoyo, N.3    Craig, E.A.4
  • 67
  • 68
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart, C. M. (2001). Mechanisms underlying ubiquitination. Annu. Rev. Biochem, 70, 503-533.
    • (2001) Annu. Rev. Biochem , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 69
    • 1842409617 scopus 로고    scopus 로고
    • Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
    • Plemper, R. K., Bohmler, S., Bordallo, J., Sommer, T., and Wolf, D. H. (1997). Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 388, 891-895.
    • (1997) Nature , vol.388 , pp. 891-895
    • Plemper, R.K.1    Bohmler, S.2    Bordallo, J.3    Sommer, T.4    Wolf, D.H.5
  • 70
    • 32544437041 scopus 로고    scopus 로고
    • Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways
    • Ravid, T., Kreft, S. G., and Hochstrasser, M. (2006). Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways. EMBO J. 25, 533-543.
    • (2006) EMBO J , vol.25 , pp. 533-543
    • Ravid, T.1    Kreft, S.G.2    Hochstrasser, M.3
  • 71
    • 0035283043 scopus 로고    scopus 로고
    • Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone
    • Rudiger, S., Schneider-Mergener, J., and Bukau, B. (2001). Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone EMBO J. 20, 1042-1050.
    • (2001) EMBO J , vol.20 , pp. 1042-1050
    • Rudiger, S.1    Schneider-Mergener, J.2    Bukau, B.3
  • 72
    • 28844457289 scopus 로고    scopus 로고
    • Yeast genomics in the elucidation of endoplasmic reticulum (ER) quality control and associated protein degradation (ERQD)
    • ed. R. J. Deshaies, Academic Press
    • Schafer, A., and Wolf, D. H. (2005). Yeast genomics in the elucidation of endoplasmic reticulum (ER) quality control and associated protein degradation (ERQD). In: Methods in Enzymology, Vol. 399, ed. R. J. Deshaies, Academic Press, 459-468.
    • (2005) Methods in Enzymology , vol.399 , pp. 459-468
    • Schafer, A.1    Wolf, D.H.2
  • 73
    • 30344460012 scopus 로고    scopus 로고
    • CPY* and the power of yeast genetics in the elucidation of quality control and associated protein degradation of endoplasmic reticulum
    • Schafer, A., and Wolf, D. H. (2006). CPY* and the power of yeast genetics in the elucidation of quality control and associated protein degradation of endoplasmic reticulum. Curr. Top. Microbiol. Immunol. 300, 41-56.
    • (2006) Curr. Top. Microbiol. Immunol , vol.300 , pp. 41-56
    • Schafer, A.1    Wolf, D.H.2
  • 75
    • 0025164762 scopus 로고
    • Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins
    • Seufert, W., and Jentsch, S. (1990). Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins. EMBO J. 9, 543-550.
    • (1990) EMBO J , vol.9 , pp. 543-550
    • Seufert, W.1    Jentsch, S.2
  • 77
    • 0029042422 scopus 로고
    • BiP/ Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast
    • Simons, J. F., Ferro-Novick, S., Rose, M. D., and Helenius, A. (1993). BiP/ Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast. J. Cell Biol. 130, 41-49.
    • (1993) J. Cell Biol , vol.130 , pp. 41-49
    • Simons, J.F.1    Ferro-Novick, S.2    Rose, M.D.3    Helenius, A.4
  • 78
    • 0346096508 scopus 로고    scopus 로고
    • Quality control in the endoplasniic reticulum protein factory
    • Sitia, R., and Braakman, I. (2003). Quality control in the endoplasniic reticulum protein factory. Nature 426, 891-894.
    • (2003) Nature , vol.426 , pp. 891-894
    • Sitia, R.1    Braakman, I.2
  • 79
    • 0030700576 scopus 로고    scopus 로고
    • Endoplasmic reticulum degradation reverse protein flow of no return
    • Sommer, T., and Wolf, D. H. (1997). Endoplasmic reticulum degradation reverse protein flow of no return. FASEB J. 11, 1227-1233.
    • (1997) FASEB J , vol.11 , pp. 1227-1233
    • Sommer, T.1    Wolf, D.H.2
  • 80
    • 0037031902 scopus 로고    scopus 로고
    • Prediction of novel Bag-1 homologs based on structure/function analysis identifies Snl1p as an Hsp70 co-chaperone in Saccharomyces cerevisiae
    • Sondermann, H., Ho, A. K., Listenberger, L. L., Siegers, K., Moarefi, I., Wente, S. R., Hartl, F. U., and Young, J. C. (2002). Prediction of novel Bag-1 homologs based on structure/function analysis identifies Snl1p as an Hsp70 co-chaperone in Saccharomyces cerevisiae. J. Biol. Chem. 277, 33220-33227.
    • (2002) J. Biol. Chem , vol.277 , pp. 33220-33227
    • Sondermann, H.1    Ho, A.K.2    Listenberger, L.L.3    Siegers, K.4    Moarefi, I.5    Wente, S.R.6    Hartl, F.U.7    Young, J.C.8
  • 81
    • 0035936826 scopus 로고    scopus 로고
    • Structure of a Bag/Hsc70 complex: Convergent functional evolution of Hsp70 nucleotide exchange factors
    • Sondermann, H., Scheufler, C., Schneider, C., Hohfeld, J., Hartl, F. U., and Moarefi, I. (2001). Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors. Science 291, 1553-1557.
    • (2001) Science , vol.291 , pp. 1553-1557
    • Sondermann, H.1    Scheufler, C.2    Schneider, C.3    Hohfeld, J.4    Hartl, F.U.5    Moarefi, I.6
  • 82
    • 0035887277 scopus 로고    scopus 로고
    • A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalphn2 repressor degradation
    • Swanson, R., Locher, M., and Hochstrasser, M. (2001). A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalphn2 repressor degradation. Genes Dev. 15, 2660-2674.
    • (2001) Genes Dev , vol.15 , pp. 2660-2674
    • Swanson, R.1    Locher, M.2    Hochstrasser, M.3
  • 83
    • 0141592584 scopus 로고    scopus 로고
    • Use of modular substrates demonstrates mechanistic diversity and reveals differences in chaperone requirement of ERAD
    • Taxis, C., Hitt, R., Park, S. H., Deak, P. M., Kostava, Z., and Wolf, D. H. (2003). Use of modular substrates demonstrates mechanistic diversity and reveals differences in chaperone requirement of ERAD. J. Biol. Chem. 278, 35903-35913.
    • (2003) J. Biol. Chem , vol.278 , pp. 35903-35913
    • Taxis, C.1    Hitt, R.2    Park, S.H.3    Deak, P.M.4    Kostava, Z.5    Wolf, D.H.6
  • 84
    • 0035976835 scopus 로고    scopus 로고
    • alpha-synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome
    • Tofaris, C. K., Layfield, K., and Spillantini, M. G. (2001). alpha-synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome. FEBS Lett. 509, 22-26.
    • (2001) FEBS Lett , vol.509 , pp. 22-26
    • Tofaris, C.K.1    Layfield, K.2    Spillantini, M.G.3
  • 85
    • 0030867774 scopus 로고    scopus 로고
    • The ubiquitin system
    • Vaeshavsky, A. (1997). The ubiquitin system. Trends Biochem. Sci. 22, 383-387.
    • (1997) Trends Biochem. Sci , vol.22 , pp. 383-387
    • Vaeshavsky, A.1
  • 86
    • 0034640110 scopus 로고    scopus 로고
    • A proteasome howdunit: The case of the missiog signal
    • Verma, R., and Deshaies, R.J. (2000). A proteasome howdunit: the case of the missiog signal. Cell 101, 341-344.
    • (2000) Cell , vol.101 , pp. 341-344
    • Verma, R.1    Deshaies, R.J.2
  • 87
    • 0037830586 scopus 로고    scopus 로고
    • Sti1 is a novel activator of the Ssa proteins
    • Wegele, H., Haslbeck, M., Reinstein, J., and Buchner, J. (2003). Sti1 is a novel activator of the Ssa proteins. J. Biol. Chem. 278, 25970-25976.
    • (2003) J. Biol. Chem , vol.278 , pp. 25970-25976
    • Wegele, H.1    Haslbeck, M.2    Reinstein, J.3    Buchner, J.4
  • 88
    • 20144366969 scopus 로고    scopus 로고
    • HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome
    • Westhoff, B., Chapple, J. P., van der Spuy, J., Hohfeld, J., and Cheetham, M. E. (2005). HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome. Curr. Biol. 15, 1058-1064.
    • (2005) Curr. Biol , vol.15 , pp. 1058-1064
    • Westhoff, B.1    Chapple, J.P.2    van der Spuy, J.3    Hohfeld, J.4    Cheetham, M.E.5
  • 89
    • 9644300915 scopus 로고    scopus 로고
    • The proteasome: A proteolytic nanomachine of cell regulation and waste disposal
    • Wolf, D. H., and Hill, W. (2004). The proteasome: a proteolytic nanomachine of cell regulation and waste disposal. Biochim. Biophys. Acta 1695, 19-31.
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 19-31
    • Wolf, D.H.1    Hill, W.2
  • 90
    • 2442645033 scopus 로고    scopus 로고
    • Proteasome begin ornithine decarboxylase digestion at the C terminus
    • Zhang, M., MacDonald, A. I., Hoyt, M. A., and Coffino, P. (2004). Proteasome begin ornithine decarboxylase digestion at the C terminus. J. Biol. Chem. 279, 20959-20965.
    • (2004) J. Biol. Chem , vol.279 , pp. 20959-20965
    • Zhang, M.1    MacDonald, A.I.2    Hoyt, M.A.3    Coffino, P.4
  • 91
    • 0345701307 scopus 로고    scopus 로고
    • Determinants of proteasome recognition of ornithine decarboxyalase, a ubiquitin-independent substrate
    • Zhang, M., Pickart, C. M., and Coffino, P. (2003). Determinants of proteasome recognition of ornithine decarboxyalase, a ubiquitin-independent substrate. EMBO J. 22, 1488-1496.
    • (2003) EMBO J , vol.22 , pp. 1488-1496
    • Zhang, M.1    Pickart, C.M.2    Coffino, P.3
  • 92
    • 33646354916 scopus 로고    scopus 로고
    • Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation
    • Zietkiewicz, S., Lewandowska, A., Stocki, P., and Liberek, K. (2006). Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation. J. Biol. Chem. 281, 7022-7029.
    • (2006) J. Biol. Chem , vol.281 , pp. 7022-7029
    • Zietkiewicz, S.1    Lewandowska, A.2    Stocki, P.3    Liberek, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.