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Volumn 119, Issue 2, 2006, Pages 303-313

Uncoupling proteasome peptidase and ATPase activities results in cytosolic release of an ER polytopic protein

Author keywords

CFTR; Cystic fibrosis; ER dislocation; ER associated degradation; p97; Polytopic proteins; Proteasome inhibitors

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; PEPTIDASE; PROTEASOME; PROTEASOME INHIBITOR; TRANSMEMBRANE CONDUCTANCE REGULATOR; TRICHLOROACETIC ACID; UNCOUPLING PROTEIN;

EID: 32244432065     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.02732     Document Type: Article
Times cited : (21)

References (83)
  • 2
    • 0037076507 scopus 로고    scopus 로고
    • Cdc48-Ufd1-Npl4: Stuck in the middle with Ub
    • Bays, N. and Hampton, R. (2002). Cdc48-Ufd1-Npl4: Stuck in the middle with Ub. Curr. Biol. 12, R366-371.
    • (2002) Curr. Biol. , vol.12
    • Bays, N.1    Hampton, R.2
  • 3
    • 0035658442 scopus 로고    scopus 로고
    • HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins
    • Bays, N., Wilhovsky, S., Goradia, A., Hodgkill-Harlow, K. and Hampton, R. (2001). HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins. Mol. Biol. Cell 12, 4114-4128.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 4114-4128
    • Bays, N.1    Wilhovsky, S.2    Goradia, A.3    Hodgkill-Harlow, K.4    Hampton, R.5
  • 4
    • 0032491397 scopus 로고    scopus 로고
    • The mechanism underlying cystic fibrosis transmembrane conductance regulator transport from the endoplasmic reticulum to the proteasome includes Sec61β and a cytosolic, deglycosylated intermediary
    • Bebök, Z., Mazzochi, C., King, S., Hong, J. and Sorscher, E. (1998). The mechanism underlying cystic fibrosis transmembrane conductance regulator transport from the endoplasmic reticulum to the proteasome includes Sec61β and a cytosolic, deglycosylated intermediary. J. Biol. Chem. 273, 29873-29878.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29873-29878
    • Bebök, Z.1    Mazzochi, C.2    King, S.3    Hong, J.4    Sorscher, E.5
  • 5
    • 0033769733 scopus 로고    scopus 로고
    • PAN, the proteasome -activating nucleotidase from archaebacteria, is a protein-unfolding molecular chaperone
    • Benaroudj, N. and Goldberg, A. (2000). PAN, the proteasome -activating nucleotidase from archaebacteria, is a protein-unfolding molecular chaperone. Nat. Cell Biol. 2, 833-839.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 833-839
    • Benaroudj, N.1    Goldberg, A.2
  • 6
    • 0037248908 scopus 로고    scopus 로고
    • ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation
    • Benaroudj, N., Zwickl, P., Seegmueller, E., Baumeister, W. and Goldberg, A. (2003). ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation. Mol. Cell 11, 69-78.
    • (2003) Mol. Cell , vol.11 , pp. 69-78
    • Benaroudj, N.1    Zwickl, P.2    Seegmueller, E.3    Baumeister, W.4    Goldberg, A.5
  • 7
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence, N., Sampat, R. and Kopito, R. (2001). Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292, 1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.1    Sampat, R.2    Kopito, R.3
  • 8
    • 0030666729 scopus 로고    scopus 로고
    • Role of Cue1p in ubiquitination and degradation at the ER surface
    • Biederer, T., Volkwein, C. and Sommer, T. (1997). Role of Cue1p in ubiquitination and degradation at the ER surface. Science 278, 1806-1809.
    • (1997) Science , vol.278 , pp. 1806-1809
    • Biederer, T.1    Volkwein, C.2    Sommer, T.3
  • 9
    • 0031010398 scopus 로고    scopus 로고
    • Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HsIV by a new class of inhibitors
    • Bogyo, M., McMaster, J., Gaczynska, M., Tortorella, D., Goldberg, A. and Ploegh, H. (1997). Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HsIV by a new class of inhibitors. Proc. Natl. Acad. Sci. USA 94, 6629-6634.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6629-6634
    • Bogyo, M.1    McMaster, J.2    Gaczynska, M.3    Tortorella, D.4    Goldberg, A.5    Ploegh, H.6
  • 11
    • 0037084028 scopus 로고    scopus 로고
    • Role of the ubiquitin-selective CDC48(UFD1/NPL4)chaperone (segregase) in ERAD of OLE1 and other substrates
    • Braun, S., Matuschewski, K., Rape, M., Thorns, S. and Jentsch, S. (2002). Role of the ubiquitin-selective CDC48(UFD1/NPL4)chaperone (segregase) in ERAD of OLE1 and other substrates. EMBO J. 21, 615-621.
    • (2002) EMBO J. , vol.21 , pp. 615-621
    • Braun, S.1    Matuschewski, K.2    Rape, M.3    Thorns, S.4    Jentsch, S.5
  • 12
    • 0031128320 scopus 로고    scopus 로고
    • ER-associated and proteasome-mediated protein degradation: How two topologically restricted events came together
    • Brodsky J. and McCracken, A. (1997). ER-associated and proteasome-mediated protein degradation: how two topologically restricted events came together. Trends Cell Biol. 7, 151-155.
    • (1997) Trends Cell Biol. , vol.7 , pp. 151-155
    • Brodsky, J.1    McCracken, A.2
  • 13
    • 0030898710 scopus 로고    scopus 로고
    • Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones and thermotolerance
    • Bush, K., Goldberg, A. and Nigam, S. (1997). Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones and thermotolerance. J. Biol. Chem. 272, 9086-9092.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9086-9092
    • Bush, K.1    Goldberg, A.2    Nigam, S.3
  • 14
    • 0034637555 scopus 로고    scopus 로고
    • Processing by endoplasmic reticulum mannosidase partitions a secretion-impaired glycoprotein into distinct disposal pathways
    • Cabral, C., Choudhury, P. and Sifers, R. (2000). Processing by endoplasmic reticulum mannosidase partitions a secretion-impaired glycoprotein into distinct disposal pathways. J. Biol. Chem. 275, 25015-25022.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25015-25022
    • Cabral, C.1    Choudhury, P.2    Sifers, R.3
  • 15
    • 9444239782 scopus 로고    scopus 로고
    • A misassembled transmembrane domain of a polytopic protein associates with signal peptide peptidase
    • Crawshaw, S., Martoglio, B., Meacock, S. and High, S. (2004). A misassembled transmembrane domain of a polytopic protein associates with signal peptide peptidase. Biochem. J. 384, 9-17.
    • (2004) Biochem. J. , vol.384 , pp. 9-17
    • Crawshaw, S.1    Martoglio, B.2    Meacock, S.3    High, S.4
  • 16
    • 0742323006 scopus 로고    scopus 로고
    • Distinct roles for the AAA ATPases NSF and p97 in the secretory pathway
    • Dalal, S., Rosser, M., Cyr, D. and Hanson, P. (2004). Distinct roles for the AAA ATPases NSF and p97 in the secretory pathway. Mol. Biol. Cell 15, 637-648.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 637-648
    • Dalal, S.1    Rosser, M.2    Cyr, D.3    Hanson, P.4
  • 18
    • 0035424237 scopus 로고    scopus 로고
    • ER quality control: Toward an understanding at the molecular level
    • Ellgard, L. and Helenius, A. (2001). ER quality control: toward an understanding at the molecular level. Curr. Opin. Cell Biol. 13, 431-437.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 431-437
    • Ellgard, L.1    Helenius, A.2
  • 19
    • 0019223260 scopus 로고
    • Control of protein degradation in reticulocytes and reticulocyte extracts by hemin
    • Etlinger, J. and Goldberg, A. (1980). Control of protein degradation in reticulocytes and reticulocyte extracts by hemin. J. Biol. Chem. 255, 4563-4568.
    • (1980) J. Biol. Chem. , vol.255 , pp. 4563-4568
    • Etlinger, J.1    Goldberg, A.2
  • 20
    • 0037023764 scopus 로고    scopus 로고
    • A principal role for the proteasome in endoplasmic reticulum-associated degradation of misfolded intracellular cystic fibrosis transmembrane conductance regulator
    • Gelman, M., Kannegaard, E. and Kopito, R. (2002). A principal role for the proteasome in endoplasmic reticulum-associated degradation of misfolded intracellular cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 277, 11709-11714.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11709-11714
    • Gelman, M.1    Kannegaard, E.2    Kopito, R.3
  • 21
    • 4344560565 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane conductance regulator degradation depends on the lectins Htm1p/EDEM and the Cdc48 protein complex in yeast
    • Gnann, A., Riordan, J. and Wolf, D. (2004). Cystic fibrosis transmembrane conductance regulator degradation depends on the lectins Htm1p/EDEM and the Cdc48 protein complex in yeast. Mol. Biol. Cell 15, 4125-4135.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4125-4135
    • Gnann, A.1    Riordan, J.2    Wolf, D.3
  • 23
    • 0019841509 scopus 로고
    • Hemin inhibits ATP-dependent ubiquitin-dependent proteolysis: Role of hemin in regulating ubiquitin conjugate degradation
    • Haas, A. and Rose, I. (1981). Hemin inhibits ATP-dependent ubiquitin-dependent proteolysis: role of hemin in regulating ubiquitin conjugate degradation. Proc. Natl. Acad. Sci. USA 78, 6845-6848.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 6845-6848
    • Haas, A.1    Rose, I.2
  • 24
    • 0029811218 scopus 로고    scopus 로고
    • Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein
    • Hampton, R., Gardner, R. and Rine, J. (1996). Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol. Biol. Cell 7, 2029-2044.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 2029-2044
    • Hampton, R.1    Gardner, R.2    Rine, J.3
  • 25
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
    • Hiller, M., Finger, A., Schweiger, M. and Wolf, D. (1996). ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science 273, 1725-1728.
    • (1996) Science , vol.273 , pp. 1725-1728
    • Hiller, M.1    Finger, A.2    Schweiger, M.3    Wolf, D.4
  • 26
    • 9644300910 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated protein degradation-one model fits all?
    • Hirsch, C., Jarosch, E., Sommer, T. and Wolf, D. (2004). Endoplasmic reticulum-associated protein degradation-one model fits all? Biochim. Biophys. Acta 1695, 208-216.
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 208-216
    • Hirsch, C.1    Jarosch, E.2    Sommer, T.3    Wolf, D.4
  • 27
    • 16944366641 scopus 로고    scopus 로고
    • Nucleotidase activities of the 26 S proteasome and its regulatory complex
    • Hoffman, L. and Rechsteiner, M. (1996). Nucleotidase activities of the 26 S proteasome and its regulatory complex. J. Biol. Chem. 271, 32538-32545.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32538-32545
    • Hoffman, L.1    Rechsteiner, M.2
  • 30
    • 0023655017 scopus 로고
    • Purification of two high molecular weight proteases from rabbit reticulocyte lysate
    • Hough, R., Pratt, G. and Rechsteiner, M. (1987). Purification of two high molecular weight proteases from rabbit reticulocyte lysate. J. Biol. Chem. 262, 8303-8313.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8303-8313
    • Hough, R.1    Pratt, G.2    Rechsteiner, M.3
  • 31
    • 4444355303 scopus 로고    scopus 로고
    • Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble lumenal protein
    • Huyer, G., Piluek, W., Fansler, Z., Kreft, S., Hochstrasser, M., Brodsky, J. and Michaelis, S. (2004). Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble lumenal protein. J. Biol. Chem. 279, 38369-38378.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38369-38378
    • Huyer, G.1    Piluek, W.2    Fansler, Z.3    Kreft, S.4    Hochstrasser, M.5    Brodsky, J.6    Michaelis, S.7
  • 32
    • 0021004695 scopus 로고
    • Preparation and use of nuclease-treated rabbit reticulocyte lysates for the translation of eukaryotic messenger RNA
    • Jackson, R. and Hunt, T. (1983). Preparation and use of nuclease-treated rabbit reticulocyte lysates for the translation of eukaryotic messenger RNA. Methods Enzymol. 96, 50-74.
    • (1983) Methods Enzymol. , vol.96 , pp. 50-74
    • Jackson, R.1    Hunt, T.2
  • 34
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • Jensen, T., Loo, M., Pind, S., Williams, D., Goldberg, A. and Riordan, J. (1995). Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83, 129-136.
    • (1995) Cell , vol.83 , pp. 129-136
    • Jensen, T.1    Loo, M.2    Pind, S.3    Williams, D.4    Goldberg, A.5    Riordan, J.6
  • 35
    • 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., Wu, Y., Dai, Q., Cyr, D., 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, 42938-42934.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42934-42938
    • Jiang, J.1    Ballinger, C.2    Wu, Y.3    Dai, Q.4    Cyr, D.5    Hohfeld, J.6    Patterson, C.7
  • 36
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston, J., Ward, C. and Kopito, R. (1998). Aggresomes: A cellular response to misfolded proteins. J. Cell Biol. 143, 1883-1898.
    • (1998) J. Cell Biol. , vol.143 , pp. 1883-1898
    • Johnston, J.1    Ward, C.2    Kopito, R.3
  • 37
    • 0033525086 scopus 로고    scopus 로고
    • The sizes of peptides generated from protein by mammalian 26 and 20 S proteasomes
    • Kisselev, A., Akopian, A., Woo, K. and Goldberg, A. (1999). The sizes of peptides generated from protein by mammalian 26 and 20 S proteasomes. J. Biol. Chem. 274, 3363-3371.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3363-3371
    • Kisselev, A.1    Akopian, A.2    Woo, K.3    Goldberg, A.4
  • 38
    • 0347298790 scopus 로고    scopus 로고
    • Functional ATPase activity of p97/valosin-containing protein (VCP) is required for the quality control of endoplasmic reticulum in neuronally differentiated mammalian PC12 Cells
    • Kobayashi, T., Tanaka, K., Inoue, K. and Kakizuka, A. (2002). Functional ATPase activity of p97/valosin-containing protein (VCP) is required for the quality control of endoplasmic reticulum in neuronally differentiated mammalian PC12 Cells. J. Biol. Chem. 277, 47358-47365.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47358-47365
    • Kobayashi, T.1    Tanaka, K.2    Inoue, K.3    Kakizuka, A.4
  • 39
    • 0034964524 scopus 로고    scopus 로고
    • The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release
    • Köhler, A., Cascio, P., Leggett, D., Woo, K., Goldberg, A. and Finley, D. (2001). The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release. Mol. Cell 7, 1143-1152.
    • (2001) Mol. Cell , vol.7 , pp. 1143-1152
    • Köhler, A.1    Cascio, P.2    Leggett, D.3    Woo, K.4    Goldberg, A.5    Finley, D.6
  • 40
    • 0035266072 scopus 로고    scopus 로고
    • ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal
    • Lee, C., Schwartz, M., Prakash, S., Iwakura, M. and Matouschek, A. (2001). ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal. Mol. Cell 7, 627-637.
    • (2001) Mol. Cell , vol.7 , pp. 627-637
    • Lee, C.1    Schwartz, M.2    Prakash, S.3    Iwakura, M.4    Matouschek, A.5
  • 41
  • 42
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the ER
    • Lilley, B. and Ploegh, H. (2004). A membrane protein required for dislocation of misfolded proteins from the ER. Nature 429, 834-839.
    • (2004) Nature , vol.429 , pp. 834-839
    • Lilley, B.1    Ploegh, H.2
  • 43
    • 0032401771 scopus 로고    scopus 로고
    • Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome
    • Loo, M., Jensen, T., Cui, L., Hou, Y., Chang, X. and Riordan, J. (1998). Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome. EMBO J. 17, 6879-6887.
    • (1998) EMBO J. , vol.17 , pp. 6879-6887
    • Loo, M.1    Jensen, T.2    Cui, L.3    Hou, Y.4    Chang, X.5    Riordan, J.6
  • 44
    • 0032483985 scopus 로고    scopus 로고
    • Quality control by proteases in the endoplasmic reticulum. Removal of a protease-sensitive site enhances expression of human P-glycoprotein
    • Loo, T. and Clarke, D. (1998). Quality control by proteases in the endoplasmic reticulum. Removal of a protease-sensitive site enhances expression of human P-glycoprotein. J. Biol. Chem. 273, 32373-32376.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32373-32376
    • Loo, T.1    Clarke, D.2
  • 45
    • 0037195647 scopus 로고    scopus 로고
    • Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol
    • Ma, J., Wollmann, R. and Lindquist, S. (2002). Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science 298, 1781-1785.
    • (2002) Science , vol.298 , pp. 1781-1785
    • Ma, J.1    Wollmann, R.2    Lindquist, S.3
  • 46
    • 0032526433 scopus 로고    scopus 로고
    • Role of the proteasome in membrane extraction of a short-lived ER-transmembrane protein
    • Mayer, T., Braun, T. and Jentsch, S. (1998). Role of the proteasome in membrane extraction of a short-lived ER-transmembrane protein. EMBO J. 17, 3251-3257.
    • (1998) EMBO J. , vol.17 , pp. 3251-3257
    • Mayer, T.1    Braun, T.2    Jentsch, S.3
  • 47
    • 0030070704 scopus 로고    scopus 로고
    • Assembly of ER-associated protein degradation in vitro: Dependence on cytosol, calnexin and ATP
    • McCracken, A. and Brodsky, J. (1996). Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin and ATP. J. Cell Biol. 132, 291-298.
    • (1996) J. Cell Biol. , vol.132 , pp. 291-298
    • McCracken, A.1    Brodsky, J.2
  • 48
    • 0042318739 scopus 로고    scopus 로고
    • Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD)
    • McCracken, A. and Brodsky, J. (2003). Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD). BioEssays 25, 868-877.
    • (2003) BioEssays , vol.25 , pp. 868-877
    • McCracken, A.1    Brodsky, J.2
  • 49
    • 0033559258 scopus 로고    scopus 로고
    • The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis
    • Meacham, G., Lu, Z., King, S., Sorscher, E., Tousson, A. and Cyr, D. (1999). The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis. EMBO J. 18, 1492-1505.
    • (1999) EMBO J. , vol.18 , pp. 1492-1505
    • Meacham, G.1    Lu, Z.2    King, S.3    Sorscher, E.4    Tousson, A.5    Cyr, D.6
  • 50
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • Meacham, G., Patterson, C., Zhang, W., Younger, J. and Cyr, D. (2001). The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat. Cell Biol. 3, 100-105.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 100-105
    • Meacham, G.1    Patterson, C.2    Zhang, W.3    Younger, J.4    Cyr, D.5
  • 51
    • 0033032942 scopus 로고    scopus 로고
    • Substrate sequestration by a proteolytically inactive Lon mutant
    • Melderen, L. and Gottesman, S. (1999). Substrate sequestration by a proteolytically inactive Lon mutant. Proc. Natl. Acad. Sci. USA 96, 6064-6071.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6064-6071
    • Melderen, L.1    Gottesman, S.2
  • 52
    • 0036845476 scopus 로고    scopus 로고
    • Direct binding of ubiquitin conjugates by the mammalian P97 adapter complexes, P47 and Ufd1-Npl4
    • Meyer, H., Wang, Y. and Warren, G. (2002). Direct binding of ubiquitin conjugates by the mammalian P97 adapter complexes, P47 and Ufd1-Npl4. EMBO J. 21, 5645-5652.
    • (2002) EMBO J. , vol.21 , pp. 5645-5652
    • Meyer, H.1    Wang, Y.2    Warren, G.3
  • 53
    • 0035694696 scopus 로고    scopus 로고
    • Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome
    • Navon, A. and Goldberg, A. (2001). Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome. Mol. Cell 8, 1339-1349.
    • (2001) Mol. Cell , vol.8 , pp. 1339-1349
    • Navon, A.1    Goldberg, A.2
  • 55
    • 0036012513 scopus 로고    scopus 로고
    • In vitro reconstitution of CFTR biogenesis and degradation
    • (ed. W. Skach), Totowa, New Jersey: Humana Press Inc
    • Oberdorf, J. and Skach, W. (2002). In vitro reconstitution of CFTR biogenesis and degradation. In Methods in Molecular Medicine (ed. W. Skach), pp. 295-310. Totowa, New Jersey: Humana Press Inc.
    • (2002) Methods in Molecular Medicine , pp. 295-310
    • Oberdorf, J.1    Skach, W.2
  • 56
    • 0035818445 scopus 로고    scopus 로고
    • Redundancy of proteasome beta subunit function during endoplasmic reticulum associated degradation
    • Oberdorf, J., Carlson, E. and Skach, W. (2001). Redundancy of proteasome beta subunit function during endoplasmic reticulum associated degradation. Biochemistry 40, 13397-13305.
    • (2001) Biochemistry , vol.40 , pp. 13305-13397
    • Oberdorf, J.1    Carlson, E.2    Skach, W.3
  • 57
    • 1542344435 scopus 로고    scopus 로고
    • Proteasomes and their kin: Proteases in the machine age
    • Pickart, C. and Cohen, R. (2004). Proteasomes and their kin:proteases in the machine age. Nat. Rev. Mol. Cell. Biol. 5, 177-187.
    • (2004) Nat. Rev. Mol. Cell. Biol. , vol.5 , pp. 177-187
    • Pickart, C.1    Cohen, R.2
  • 58
    • 0030789680 scopus 로고    scopus 로고
    • Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation
    • Pilon, M., Schekman, R. and Römisch, K. (1997). Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation. EMBO J. 16, 4540-4548.
    • (1997) EMBO J. , vol.16 , pp. 4540-4548
    • Pilon, M.1    Schekman, R.2    Römisch, K.3
  • 59
    • 0033168382 scopus 로고    scopus 로고
    • Retrograde protein translocation: ERADication of secretary proteins in health and disease
    • Plemper, R. and Wolf, D. (1999). Retrograde protein translocation: ERADication of secretary proteins in health and disease. Trends Biol. Sci. 24, 266-270.
    • (1999) Trends Biol. Sci. , vol.24 , pp. 266-270
    • Plemper, R.1    Wolf, D.2
  • 60
    • 0032484024 scopus 로고    scopus 로고
    • Endoplasmic reticulum degradation of a mutated ATP-binding cassette transporter Pdr5 proceeds in a concerted action of Sec61 and the proteasome
    • Plemper, R., Egner, R., Kuchler, K. and Wolf, D. (1998). Endoplasmic reticulum degradation of a mutated ATP-binding cassette transporter Pdr5 proceeds in a concerted action of Sec61 and the proteasome. J. Biol. Chem. 273, 32848-32856.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32848-32856
    • Plemper, R.1    Egner, R.2    Kuchler, K.3    Wolf, D.4
  • 61
    • 11144355537 scopus 로고    scopus 로고
    • Overexpression of the endoplasmic reticulum protein ER-60 downregulates ApoB100 secretion by inducing its intracellular degradation via a nonproteasomal pathway: Evidence for an ER-60-mediated and pCMB-sensitive intracellular degradative pathway
    • Qiu, W., Kohen-Avramoglu, R., Rashid-Kolvear, F., Au, C. S., Chong, T. M., Lewis, G. F., Trinh, D. K., Austin, R. C., Urade, R. and Adeli, K. (2004). Overexpression of the endoplasmic reticulum protein ER-60 downregulates ApoB100 secretion by inducing its intracellular degradation via a nonproteasomal pathway: evidence for an ER-60-mediated and pCMB-sensitive intracellular degradative pathway. Biochemistry 43, 4819-4831.
    • (2004) Biochemistry , vol.43 , pp. 4819-4831
    • Qiu, W.1    Kohen-Avramoglu, R.2    Rashid-Kolvear, F.3    Au, C.S.4    Chong, T.M.5    Lewis, G.F.6    Trinh, D.K.7    Austin, R.C.8    Urade, R.9    Adeli, K.10
  • 62
    • 0036136901 scopus 로고    scopus 로고
    • AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation
    • Rabinovich, E., Kerem, A., Frölich, K.-U., Diamant, N. and Bar-Nun, S. (2002). AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Mol. Cell. Biol. 22, 626-634.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 626-634
    • Rabinovich, E.1    Kerem, A.2    Frölich, K.-U.3    Diamant, N.4    Bar-Nun, S.5
  • 63
    • 0035957317 scopus 로고    scopus 로고
    • ClpA mediates directional translocation of substrate proteins into the ClpP protease
    • Reid, B., Fenton, W., Horwich, A. and Weber-Ban, E. (2001). ClpA mediates directional translocation of substrate proteins into the ClpP protease. Proc. Natl. Acad. Sci. USA 98, 3768-3772.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3768-3772
    • Reid, B.1    Fenton, W.2    Horwich, A.3    Weber-Ban, E.4
  • 64
    • 24944446266 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation
    • Römisch, K. (2005). Endoplasmic reticulum-associated degradation. Annu. Rev. Cell Dev. Biol. 21, 435-456.
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 435-456
    • Römisch, K.1
  • 65
    • 1042292018 scopus 로고    scopus 로고
    • Endoplasmic reticulum-localized amyloid β-peptide is degraded in the cytosol by two distinct degradation pathways
    • Schmitz, A., Schneider, A., Kummer, M. and Herzog, V. (2004). Endoplasmic reticulum-localized amyloid β-peptide is degraded in the cytosol by two distinct degradation pathways. Traffic 5, 89-101.
    • (2004) Traffic , vol.5 , pp. 89-101
    • Schmitz, A.1    Schneider, A.2    Kummer, M.3    Herzog, V.4
  • 66
    • 0034254908 scopus 로고    scopus 로고
    • Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP
    • Singh, S., Grimaud, R., Hoskins, J., Wickner, S. and Maurizi, M. (2000). Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP. Proc. Natl. Acad. Sci. USA 97, 8898-8903.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8898-8903
    • Singh, S.1    Grimaud, R.2    Hoskins, J.3    Wickner, S.4    Maurizi, M.5
  • 67
    • 0037423187 scopus 로고    scopus 로고
    • ATPase activity of p97-valosin-containing protein (VCP). D2 mediates the major enzyme activity, and D1 contributes to heat-induced activity
    • Song, C., Wang, Q. and Li, C. (2003). ATPase activity of p97-valosin-containing protein (VCP). D2 mediates the major enzyme activity, and D1 contributes to heat-induced activity. J. Biol. Chem. 278, 3648-3655.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3648-3655
    • Song, C.1    Wang, Q.2    Li, C.3
  • 69
    • 0036270698 scopus 로고    scopus 로고
    • Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
    • Tsai, B., Ye, Y. and Rapoport, T. (2002). Retro-translocation of proteins from the endoplasmic reticulum into the cytosol. Nat. Rev. Mol. Cell. Biol. 3, 246-255.
    • (2002) Nat. Rev. Mol. Cell. Biol. , vol.3 , pp. 246-255
    • Tsai, B.1    Ye, Y.2    Rapoport, T.3
  • 70
    • 0037193468 scopus 로고    scopus 로고
    • Dislocation and degradation from the ER are regulated by cytosolic stress
    • VanSlyke, J. and Musil, L. (2002). Dislocation and degradation from the ER are regulated by cytosolic stress. J. Cell Biol. 157, 381-394.
    • (2002) J. Cell Biol. , vol.157 , pp. 381-394
    • VanSlyke, J.1    Musil, L.2
  • 71
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • Voges, C., Zwickl, P. and Baumeister, W. (1999). The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu. Rev. Biochem. 68, 1015-1068.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 1015-1068
    • Voges, C.1    Zwickl, P.2    Baumeister, W.3
  • 72
    • 0020994721 scopus 로고
    • Preparation of microsomal membranes for cotranslational protein translocation
    • (ed. S. Fleischer and B. Fleischer), New York: Academic Press
    • Walter, P. and Blobel, G. (1983). Preparation of microsomal membranes for cotranslational protein translocation. In Methods in Enzymology (ed. S. Fleischer and B. Fleischer), pp. 84-93. New York: Academic Press.
    • (1983) Methods in Enzymology , pp. 84-93
    • Walter, P.1    Blobel, G.2
  • 73
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteosome pathway
    • Ward, C., Omura, C. and Kopito, R. (1995). Degradation of CFTR by the ubiquitin-proteosome pathway. Cell 83, 121-128.
    • (1995) Cell , vol.83 , pp. 121-128
    • Ward, C.1    Omura, C.2    Kopito, R.3
  • 74
    • 0029828991 scopus 로고    scopus 로고
    • Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
    • Wiertz, E., Tortorella, D., Bogyo, M., Yu, J., Mothes, W., Jones, T., Rapoport, T. and Ploegh, H. (1996). Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 384, 432-438.
    • (1996) Nature , vol.384 , pp. 432-438
    • Wiertz, E.1    Tortorella, D.2    Bogyo, M.3    Yu, J.4    Mothes, W.5    Jones, T.6    Rapoport, T.7    Ploegh, H.8
  • 76
    • 0033614038 scopus 로고    scopus 로고
    • Evidence that endoplasmic reticulum (ER)-associated degradation of cystic fibrosis transmembrane conductance regulator is linked to retrograde translocation from the ER membrane
    • Xiong, X., Chong, E. and Skach, W. (1999). Evidence that endoplasmic reticulum (ER)-associated degradation of cystic fibrosis transmembrane conductance regulator is linked to retrograde translocation from the ER membrane. J. Biol. Chem. 274, 2616-2624.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2616-2624
    • Xiong, X.1    Chong, E.2    Skach, W.3
  • 77
    • 0027488993 scopus 로고
    • The common variant of cystic fibrosis transmembrane conductance regulator is recognized by hsp70 and degraded in a pre-Golgi nonlysosomal compartment
    • Yang, Y., Janach, S., Cohn, J. and Wilson, J. (1993). The common variant of cystic fibrosis transmembrane conductance regulator is recognized by hsp70 and degraded in a pre-Golgi nonlysosomal compartment. Proc. Natl. Acad. Sci. USA 90, 9480-9484.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9480-9484
    • Yang, Y.1    Janach, S.2    Cohn, J.3    Wilson, J.4
  • 78
    • 0028788228 scopus 로고
    • In vivo assembly of the proteasomal complexes, implications for antigen processing
    • Yang, Y., Früh, K., Ahn, K. and Peterson, P. (1995). In vivo assembly of the proteasomal complexes, implications for antigen processing. J. Biol. Chem. 270, 27687-27694.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27687-27694
    • Yang, Y.1    Früh, K.2    Ahn, K.3    Peterson, P.4
  • 79
    • 0035818999 scopus 로고    scopus 로고
    • The AAA-ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye, Y., Meyer, H. and Rapoport, T. (2001). The AAA-ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 414, 652-656.
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.2    Rapoport, T.3
  • 80
    • 0038487228 scopus 로고    scopus 로고
    • Function of the p97-Ufd1-Npl4 complex in retro-translocation from the ER to the cytosol: Dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains
    • Ye, Y., Meyer, H. and Rapoport, T. (2003). Function of the p97-Ufd1-Npl4 complex in retro-translocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J. Cell Biol. 162, 71-74.
    • (2003) J. Cell Biol. , vol.162 , pp. 71-74
    • Ye, Y.1    Meyer, H.2    Rapoport, T.3
  • 81
    • 3042677637 scopus 로고    scopus 로고
    • A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
    • Ye, Y., Shibata, Y., Yun, C., Ron, D. and Rapoport, T. (2004). A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Nature 429, 841-847.
    • (2004) Nature , vol.429 , pp. 841-847
    • Ye, Y.1    Shibata, Y.2    Yun, C.3    Ron, D.4    Rapoport, T.5
  • 82
    • 6344275303 scopus 로고    scopus 로고
    • Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast
    • Youker, R., Walsh, P., Beilarz, T., Lithgow, T. and Brodsky, J. (2004). Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast. Mol. Biol. Cell 15, 4787-4797.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4787-4797
    • Youker, R.1    Walsh, P.2    Beilarz, T.3    Lithgow, T.4    Brodsky, J.5
  • 83
    • 0030817978 scopus 로고    scopus 로고
    • Cytosolic degradation of T-cell Receptor alpha chains by the proteasome
    • Yu, H., Kaung, S., Kobayashi, S. and Kopito, R. (1997). Cytosolic degradation of T-cell Receptor alpha chains by the proteasome. J. Biol. Chem. 272, 20800-20804.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20800-20804
    • Yu, H.1    Kaung, S.2    Kobayashi, S.3    Kopito, R.4


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