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Volumn 288, Issue 43, 2013, Pages 31069-31079

Endoplasmic reticulum protein quality control is determined by cooperative interactions between Hsp/c70 protein and the CHIP E3 ligase

Author keywords

[No Author keywords available]

Indexed keywords

C TERMINUS; CHIP SUBSTRATES; COOPERATIVE INTERACTIONS; E3 LIGASE; ENDOPLASMIC RETICULUM; IN-CHIP; MULTIPLE DOMAINS; PROTEIN QUALITY CONTROL;

EID: 84886649071     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.479345     Document Type: Article
Times cited : (54)

References (67)
  • 1
    • 0030949874 scopus 로고    scopus 로고
    • ER quality control: The cytoplasmic connection
    • Kopito, R. R. (1997) ER quality control: the cytoplasmic connection. Cell 88, 427-430
    • (1997) Cell , vol.88 , pp. 427-430
    • Kopito, R.R.1
  • 3
    • 33746208871 scopus 로고    scopus 로고
    • ERAD: The long road to destruction. A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation
    • Denic, V., Quan, E. M., and Weissman, J. S. (2006) ERAD: the long road to destruction. A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation. Cell 126, 349-359
    • (2006) Cell , vol.126 , pp. 349-359
    • Denic, V.1    Quan, E.M.2    Weissman, J.S.3
  • 4
    • 33746228127 scopus 로고    scopus 로고
    • Distinct ubiquitinligase complexes define convergent pathways for the degradation of ER proteins
    • Carvalho, P., Goder, V., and Rapoport, T. A. (2006) Distinct ubiquitinligase complexes define convergent pathways for the degradation of ER proteins. Cell 126, 361-373
    • (2006) Cell , vol.126 , pp. 361-373
    • Carvalho, P.1    Goder, V.2    Rapoport, T.A.3
  • 5
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: Endoplasmic reticulum-associated degradation
    • Vembar, S. S., and Brodsky, J. L. (2008) One step at a time: endoplasmic reticulum-associated degradation. Nat. Rev. Mol. Cell Biol. 9, 944-957
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 7
    • 79960711299 scopus 로고    scopus 로고
    • Protein folding and quality control in the endoplasmic reticulum: Recent lessons from yeast and mammalian cell systems
    • Brodsky, J. L., and Skach, W. R. (2011) Protein folding and quality control in the endoplasmic reticulum: Recent lessons from yeast and mammalian cell systems.. Curr. Opin. Cell Biol. 23, 464-475
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 464-475
    • Brodsky, J.L.1    Skach, W.R.2
  • 8
    • 1542344435 scopus 로고    scopus 로고
    • Proteasomes and their kin: Proteases in the machine age
    • Pickart, C. M., and Cohen, R. E. (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.M.1    Cohen, R.E.2
  • 9
    • 33845416970 scopus 로고    scopus 로고
    • Global organization and function of mammalian cytosolic proteasome pools: Implications for PA28 and 19S regulatory complexes
    • Shibatani, T., Carlson, E. J., Larabee, F., McCormack, A. L., Früh, K., and Skach, W. R. (2006) Global organization and function of mammalian cytosolic proteasome pools: Implications for PA28 and 19S regulatory complexes.. Mol. Biol. Cell 17, 4962-4971
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4962-4971
    • Shibatani, T.1    Carlson, E.J.2    Larabee, F.3    McCormack, A.L.4    Früh, K.5    Skach, W.R.6
  • 10
    • 63649161943 scopus 로고    scopus 로고
    • The ubiquitylation machinery of the endoplasmic reticulum
    • Hirsch, C., Gauss, R., Horn, S. C., Neuber, O., and Sommer, T. (2009) The ubiquitylation machinery of the endoplasmic reticulum. Nature 458, 453-460
    • (2009) Nature , vol.458 , pp. 453-460
    • Hirsch, C.1    Gauss, R.2    Horn, S.C.3    Neuber, O.4    Sommer, T.5
  • 11
    • 4344578534 scopus 로고    scopus 로고
    • The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator
    • Alberti, S., Böhse, K., Arndt, V., Schmitz, A., and Höhfeld, J. (2004) The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator.. Mol. Biol. Cell 15, 4003-4010
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4003-4010
    • Alberti, S.1    Böhse, K.2    Arndt, V.3    Schmitz, A.4    Höhfeld, J.5
  • 12
    • 28644442088 scopus 로고    scopus 로고
    • BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP
    • Arndt, V., Daniel, C., Nastainczyk, W., Alberti, S., and Höhfeld, J. (2005) BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP. Mol. Biol. Cell 16, 5891-5900
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5891-5900
    • Arndt, V.1    Daniel, C.2    Nastainczyk, W.3    Alberti, S.4    Höhfeld, J.5
  • 14
    • 77954947810 scopus 로고    scopus 로고
    • The HSP70 chaperone machinery: J proteins as drivers of functional specificity
    • Kampinga, H. H., and Craig, E. A. (2010) The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat. Rev. Mol. Cell Biol. 11, 579-592
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 579-592
    • Kampinga, H.H.1    Craig, E.A.2
  • 15
    • 80051689133 scopus 로고    scopus 로고
    • Role of Hsc70 binding cycle in CFTR folding and endoplasmic reticulum-associated degradation
    • Matsumura, Y., David, L. L., and Skach, W. R. (2011) Role of Hsc70 binding cycle in CFTR folding and endoplasmic reticulum-associated degradation. Mol. Biol. Cell 22, 2797-2809
    • (2011) Mol. Biol. Cell , vol.22 , pp. 2797-2809
    • Matsumura, Y.1    David, L.L.2    Skach, W.R.3
  • 17
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • Meacham, G. C., Patterson, C., Zhang, W., Younger, J. M., and Cyr, D. M. (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.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 18
    • 1242291789 scopus 로고    scopus 로고
    • CHIP: A link between the chaperone and proteasome systems
    • McDonough, H., and Patterson, C. (2003) CHIP: a link between the chaperone and proteasome systems. Cell Stress Chaperones 8, 303-308
    • (2003) Cell Stress Chaperones , vol.8 , pp. 303-308
    • McDonough, H.1    Patterson, C.2
  • 19
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeatcontaining protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • Ballinger, C. A., Connell, P., Wu, Y., Hu, Z., Thompson, L. J., Yin, L. Y., and Patterson, C. (1999) Identification of CHIP, a novel tetratricopeptide repeatcontaining protein that interacts with heat shock proteins and negatively regulates chaperone functions.. Mol. Cell. Biol. 19, 4535-4545
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3    Hu, Z.4    Thompson, L.J.5    Yin, L.Y.6    Patterson, C.7
  • 20
    • 1642576077 scopus 로고    scopus 로고
    • Dimerization of the human E3 ligase CHIP via a coiled-coil domain is essential for its activity
    • Nikolay, R., Wiederkehr, T., Rist, W., Kramer, G., Mayer, M. P., and Bukau, B. (2004) Dimerization of the human E3 ligase CHIP via a coiled-coil domain is essential for its activity. J. Biol. Chem. 279, 2673-2678
    • (2004) J. Biol. Chem. , vol.279 , pp. 2673-2678
    • Nikolay, R.1    Wiederkehr, T.2    Rist, W.3    Kramer, G.4    Mayer, M.P.5    Bukau, B.6
  • 21
    • 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., Höhfeld, 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    Höhfeld, J.6    Patterson, C.7
  • 22
    • 11244349206 scopus 로고    scopus 로고
    • A foldable CFTRαF508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase
    • Younger, J. M., Ren, H. Y., Chen, L., Fan, C. Y., Fields, A., Patterson, C., and Cyr, D. M. (2004) A foldable CFTRαF508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase.. J. Cell Biol. 167, 1075-1085
    • (2004) J. Cell Biol. , vol.167 , pp. 1075-1085
    • Younger, J.M.1    Ren, H.Y.2    Chen, L.3    Fan, C.Y.4    Fields, A.5    Patterson, C.6    Cyr, D.M.7
  • 23
    • 27944495299 scopus 로고    scopus 로고
    • Chaperoned ubiquitylation-crystal structures of the CHIPUbox E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex
    • Zhang, M., Windheim, M., Roe, S. M., Peggie, M., Cohen, P., Prodromou, C., and Pearl, L. H. (2005) Chaperoned ubiquitylation-crystal structures of the CHIPUbox E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex.. Mol. Cell 20, 525-538
    • (2005) Mol. Cell , vol.20 , pp. 525-538
    • Zhang, M.1    Windheim, M.2    Roe, S.M.3    Peggie, M.4    Cohen, P.5    Prodromou, C.6    Pearl, L.H.7
  • 24
    • 44349182079 scopus 로고    scopus 로고
    • Interactions between the quality control ubiquitin ligase CHIP and ubiquitin conjugating enzymes
    • Xu, Z., Kohli, E., Devlin, K. I., Bold, M., Nix, J. C., and Misra, S. (2008) Interactions between the quality control ubiquitin ligase CHIP and ubiquitin conjugating enzymes. BMC Struct. Biol. 8, 26
    • (2008) BMC Struct. Biol. , vol.8 , pp. 26
    • Xu, Z.1    Kohli, E.2    Devlin, K.I.3    Bold, M.4    Nix, J.C.5    Misra, S.6
  • 25
    • 33845874433 scopus 로고    scopus 로고
    • Brain CHIP: Removing the culprits in neurodegenerative disease
    • Dickey, C. A., Patterson, C., Dickson, D., and Petrucelli, L. (2007) Brain CHIP: removing the culprits in neurodegenerative disease. Trends Mol. Med. 13, 32-38
    • (2007) Trends Mol. Med. , vol.13 , pp. 32-38
    • Dickey, C.A.1    Patterson, C.2    Dickson, D.3    Petrucelli, L.4
  • 26
    • 78449296171 scopus 로고    scopus 로고
    • E3 ubiquitin ligases in ErbB receptor quantity control
    • 3rd
    • Carraway, K. L., 3rd. (2010) E3 ubiquitin ligases in ErbB receptor quantity control. Semin. Cell Dev. Biol. 21, 936-943
    • (2010) Semin. Cell Dev. Biol. , vol.21 , pp. 936-943
    • Carraway, K.L.1
  • 27
    • 0036789884 scopus 로고    scopus 로고
    • Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu
    • Xu, W., Marcu, M., Yuan, X., Mimnaugh, E., Patterson, C., and Neckers, L. (2002) Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu. Proc. Natl. Acad. Sci. U. S. A. 99, 12847-12852
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 12847-12852
    • Xu, W.1    Marcu, M.2    Yuan, X.3    Mimnaugh, E.4    Patterson, C.5    Neckers, L.6
  • 29
    • 1042266624 scopus 로고    scopus 로고
    • CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival
    • Shimura, H., Schwartz, D., Gygi, S. P., and Kosik, K. S. (2004) CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival. J. Biol. Chem. 279, 4869-4876
    • (2004) J. Biol. Chem. , vol.279 , pp. 4869-4876
    • Shimura, H.1    Schwartz, D.2    Gygi, S.P.3    Kosik, K.S.4
  • 30
    • 3042817421 scopus 로고    scopus 로고
    • CHIP promotes proteasomal degradation of familial ALS-linked mutant SOD1 by ubiquitinating Hsp/Hsc70
    • Urushitani, M., Kurisu, J., Tateno, M., Hatakeyama, S., Nakayama, K., Kato, S., and Takahashi, R. (2004) CHIP promotes proteasomal degradation of familial ALS-linked mutant SOD1 by ubiquitinating Hsp/Hsc70.. J. Neurochem. 90, 231-244
    • (2004) J. Neurochem. , vol.90 , pp. 231-244
    • Urushitani, M.1    Kurisu, J.2    Tateno, M.3    Hatakeyama, S.4    Nakayama, K.5    Kato, S.6    Takahashi, R.7
  • 31
    • 0038788824 scopus 로고    scopus 로고
    • Overexpression of the cochaperone CHIP enhances Hsp70-dependent folding activity in mammalian cells
    • Kampinga, H. H., Kanon, B., Salomons, F. A., Kabakov, A. E., and Patterson, C. (2003) Overexpression of the cochaperone CHIP enhances Hsp70-dependent folding activity in mammalian cells.. Mol. Cell. Biol. 23, 4948-4958
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4948-4958
    • Kampinga, H.H.1    Kanon, B.2    Salomons, F.A.3    Kabakov, A.E.4    Patterson, C.5
  • 33
    • 77955257617 scopus 로고    scopus 로고
    • CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substrates
    • Stankiewicz, M., Nikolay, R., Rybin, V., and Mayer, M. P. (2010) CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substrates.. FEBS J. 277, 3353-3367
    • (2010) FEBS J. , vol.277 , pp. 3353-3367
    • Stankiewicz, M.1    Nikolay, R.2    Rybin, V.3    Mayer, M.P.4
  • 34
    • 0025242929 scopus 로고
    • Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis
    • Cheng, S. H., Gregory, R. J., Marshall, J., Paul, S., Souza, D. W., White, G. A., O'Riordan, C. R., and Smith, A. E. (1990) Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis.. Cell 63, 827-834
    • (1990) Cell , vol.63 , pp. 827-834
    • Cheng, S.H.1    Gregory, R.J.2    Marshall, J.3    Paul, S.4    Souza, D.W.5    White, G.A.6    O'Riordan, C.R.7    Smith, A.E.8
  • 35
    • 0028006681 scopus 로고
    • Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins
    • Ward, C. L., and Kopito, R. R. (1994) Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins. J. Biol. Chem. 269, 25710-25718
    • (1994) J. Biol. Chem. , vol.269 , pp. 25710-25718
    • Ward, C.L.1    Kopito, R.R.2
  • 36
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward, C. L., Omura, S., and Kopito, R. R. (1995) Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83, 121-127
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 37
    • 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. R. (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.R.3
  • 38
    • 50649123290 scopus 로고    scopus 로고
    • CFTR function and prospects for therapy
    • Riordan, J. R. (2008) CFTR function and prospects for therapy. Annu. Rev. Biochem. 77, 701-726
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 701-726
    • Riordan, J.R.1
  • 39
    • 33746675669 scopus 로고    scopus 로고
    • Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator
    • Younger, J. M., Chen, L., Ren, H. Y., Rosser, M. F., Turnbull, E. L., Fan, C. Y., Patterson, C., and Cyr, D. M. (2006) Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator.. Cell 126, 571-582
    • (2006) Cell , vol.126 , pp. 571-582
    • Younger, J.M.1    Chen, L.2    Ren, H.Y.3    Rosser, M.F.4    Turnbull, E.L.5    Fan, C.Y.6    Patterson, C.7    Cyr, D.M.8
  • 41
    • 69949130128 scopus 로고    scopus 로고
    • Rescue of αF508-CFTR by the SGK1/Nedd4-2 signaling pathway
    • Caohuy, H., Jozwik, C., and Pollard, H. B. (2009) Rescue of αF508-CFTR by the SGK1/Nedd4-2 signaling pathway. J. Biol. Chem. 284, 25241-25253
    • (2009) J. Biol. Chem. , vol.284 , pp. 25241-25253
    • Caohuy, H.1    Jozwik, C.2    Pollard, H.B.3
  • 42
    • 3042856481 scopus 로고    scopus 로고
    • Interaction of U-box-type ubiquitin-protein ligases (E3s) with molecular chaperones
    • Hatakeyama, S., Matsumoto, M., Yada, M., and Nakayama, K. I. (2004) Interaction of U-box-type ubiquitin-protein ligases (E3s) with molecular chaperones. Genes Cells 9, 533-548
    • (2004) Genes Cells , vol.9 , pp. 533-548
    • Hatakeyama, S.1    Matsumoto, M.2    Yada, M.3    Nakayama, K.I.4
  • 43
    • 0036012513 scopus 로고    scopus 로고
    • In vitro reconstitution of CFTR biogenesis and degradation
    • Oberdorf, J., and Skach, W. R. (2002) In vitro reconstitution of CFTR biogenesis and degradation. Methods Mol. Med. 70, 295-310
    • (2002) Methods Mol. Med. , vol.70 , pp. 295-310
    • Oberdorf, J.1    Skach, W.R.2
  • 44
    • 20344380980 scopus 로고    scopus 로고
    • Reticulocyte lysate as a model system to study endoplasmic reticulum membrane protein degradation
    • Carlson, E., Bays, N., David, L., and Skach, W. R. (2005) Reticulocyte lysate as a model system to study endoplasmic reticulum membrane protein degradation. Methods Mol. Biol. 301, 185-205
    • (2005) Methods Mol. Biol. , vol.301 , pp. 185-205
    • Carlson, E.1    Bays, N.2    David, L.3    Skach, W.R.4
  • 45
    • 84857102052 scopus 로고    scopus 로고
    • Protein export from endoplasmic reticulum to the cytosol: In vitro methods
    • Finazzi-Agrò, A., ed John Wiley & Sons, Inc., New York
    • Matsumura, Y., and Skach, W. R. (2009) Protein export from endoplasmic reticulum to the cytosol: In vitro methods. in Encyclopedia of Life Sciences (Finazzi-Agrò, A., ed) John Wiley & Sons, Inc., New York
    • (2009) Encyclopedia of Life Sciences
    • Matsumura, Y.1    Skach, W.R.2
  • 47
    • 0037428164 scopus 로고    scopus 로고
    • Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom
    • Young, J. C., Hoogenraad, N. J., and Hartl, F. U. (2003) Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom. Cell 112, 41-50
    • (2003) Cell , vol.112 , pp. 41-50
    • Young, J.C.1    Hoogenraad, N.J.2    Hartl, F.U.3
  • 49
    • 84886678220 scopus 로고    scopus 로고
    • J. Biol. Chem. 283, 27100-27109
    • J. Biol. Chem. , vol.283 , pp. 27100-27109
  • 50
    • 17144371281 scopus 로고    scopus 로고
    • Low resolution structural study of two human HSP40 chaperones in solution. DJA1 from subfamily A and DJB4 from subfamily B have different quaternary structures
    • Borges, J. C., Fischer, H., Craievich, A. F., and Ramos, C. H. (2005) Low resolution structural study of two human HSP40 chaperones in solution. DJA1 from subfamily A and DJB4 from subfamily B have different quaternary structures. J. Biol. Chem. 280, 13671-13681
    • (2005) J. Biol. Chem. , vol.280 , pp. 13671-13681
    • Borges, J.C.1    Fischer, H.2    Craievich, A.F.3    Ramos, C.H.4
  • 51
    • 33749353475 scopus 로고    scopus 로고
    • P97 functions as an auxiliary factor to facilitateTMdomain extraction during CFTR ER-associated degradation
    • Carlson, E. J., Pitonzo, D., and Skach, W. R. (2006) p97 functions as an auxiliary factor to facilitateTMdomain extraction during CFTR ER-associated degradation.. EMBO J. 25, 4557-4566
    • (2006) EMBO J. , vol.25 , pp. 4557-4566
    • Carlson, E.J.1    Pitonzo, D.2    Skach, W.R.3
  • 52
    • 0027509361 scopus 로고
    • The constitutive and stress inducible forms of hsp 70 exhibit functional similarities and interact with one another in an ATP-dependent fashion
    • Brown, C. R., Martin, R. L., Hansen, W. J., Beckmann, R. P., and Welch, W. J. (1993) The constitutive and stress inducible forms of hsp 70 exhibit functional similarities and interact with one another in an ATP-dependent fashion.. J. Cell Biol. 120, 1101-1112
    • (1993) J. Cell Biol. , vol.120 , pp. 1101-1112
    • Brown, C.R.1    Martin, R.L.2    Hansen, W.J.3    Beckmann, R.P.4    Welch, W.J.5
  • 53
    • 33845918996 scopus 로고    scopus 로고
    • Characterization and classification of ATP-binding cassette transporter ABCA3 mutants in fatal surfactant deficiency
    • Matsumura, Y., Ban, N., Ueda, K., and Inagaki, N. (2006) Characterization and classification of ATP-binding cassette transporter ABCA3 mutants in fatal surfactant deficiency.. J. Biol. Chem. 281, 34503-34514
    • (2006) J. Biol. Chem. , vol.281 , pp. 34503-34514
    • Matsumura, Y.1    Ban, N.2    Ueda, K.3    Inagaki, N.4
  • 54
    • 0030798979 scopus 로고    scopus 로고
    • The molecular chaperone Hsc70 assists the in vitro folding of the N-terminal nucleotidebinding domain of the cystic fibrosis transmembrane conductance regulator
    • Strickland, E., Qu, B. H., Millen, L., and Thomas, P. J. (1997) The molecular chaperone Hsc70 assists the in vitro folding of the N-terminal nucleotidebinding domain of the cystic fibrosis transmembrane conductance regulator.. J. Biol. Chem. 272, 25421-25424
    • (1997) J. Biol. Chem. , vol.272 , pp. 25421-25424
    • Strickland, E.1    Qu, B.H.2    Millen, L.3    Thomas, P.J.4
  • 55
    • 32244432065 scopus 로고    scopus 로고
    • Uncoupling proteasome peptidase and ATPase activities results in cytosolic release of an ER polytopic protein
    • Oberdorf, J., Carlson, E. J., and Skach, W. R. (2006) Uncoupling proteasome peptidase and ATPase activities results in cytosolic release of an ER polytopic protein.. J. Cell Sci. 119, 303-313
    • (2006) J. Cell Sci. , vol.119 , pp. 303-313
    • Oberdorf, J.1    Carlson, E.J.2    Skach, W.R.3
  • 56
    • 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
  • 57
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domainpeptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • Scheufler, C., Brinker, A., Bourenkov, G., Pegoraro, S., Moroder, L., Bartunik, H., Hartl, F. U., and Moarefi, I. (2000) Structure of TPR domainpeptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine.. Cell 101, 199-210
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl, F.U.7    Moarefi, I.8
  • 58
    • 77949371541 scopus 로고    scopus 로고
    • Insights into the conformational dynamics of the E3 ubiquitin ligase CHIP in complex with chaperones and E2 enzymes
    • Graf, C., Stankiewicz, M., Nikolay, R., and Mayer, M. P. (2010) Insights into the conformational dynamics of the E3 ubiquitin ligase CHIP in complex with chaperones and E2 enzymes.. Biochemistry 49, 2121-2129
    • (2010) Biochemistry , vol.49 , pp. 2121-2129
    • Graf, C.1    Stankiewicz, M.2    Nikolay, R.3    Mayer, M.P.4
  • 59
    • 70350093431 scopus 로고    scopus 로고
    • C-terminal sequences of hsp70 and hsp90 as non-specific anchors for tetratricopeptide repeat (TPR) proteins
    • Ramsey, A. J., Russell, L. C., and Chinkers, M. (2009) C-terminal sequences of hsp70 and hsp90 as non-specific anchors for tetratricopeptide repeat (TPR) proteins.. Biochem. J. 423, 411-419
    • (2009) Biochem. J. , vol.423 , pp. 411-419
    • Ramsey, A.J.1    Russell, L.C.2    Chinkers, M.3
  • 60
    • 84879412911 scopus 로고    scopus 로고
    • C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances
    • Muller, P., Ruckova, E., Halada, P., Coates, P. J., Hrstka, R., Lane, D. P., and Vojtesek, B. (2013) C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances.. Oncogene 32, 3101-3110
    • (2013) Oncogene , vol.32 , pp. 3101-3110
    • Muller, P.1    Ruckova, E.2    Halada, P.3    Coates, P.J.4    Hrstka, R.5    Lane, D.P.6    Vojtesek, B.7
  • 61
    • 0030809817 scopus 로고    scopus 로고
    • In vitro pharmacologic restoration of CFTR-mediated chloride transport with sodium 4-phenylbutyrate in cystic fibrosis epithelial cells containing αF508-CFTR
    • Rubenstein, R. C., Egan, M. E, and Zeitlin, P. L. (1997) In vitro pharmacologic restoration of CFTR-mediated chloride transport with sodium 4-phenylbutyrate in cystic fibrosis epithelial cells containing αF508-CFTR.. J. Clin. Invest. 100, 2457-2465
    • (1997) J. Clin. Invest. , vol.100 , pp. 2457-2465
    • Rubenstein, R.C.1    Egan, M.E.2    Zeitlin, P.L.3
  • 63
    • 0031889082 scopus 로고    scopus 로고
    • A pilot clinical trial of oral sodium 4-phenylbutyrate (Buphenyl) in αF508-homozygous cystic fibrosis patients: Partial restoration of nasal epithelial CFTR function
    • Rubenstein, R. C., and Zeitlin, P. L. (1998) A pilot clinical trial of oral sodium 4-phenylbutyrate (Buphenyl) in αF508-homozygous cystic fibrosis patients: partial restoration of nasal epithelial CFTR function.. Am. J. Respir. Crit. Care Med. 157, 484-490
    • (1998) Am. J. Respir. Crit. Care Med. , vol.157 , pp. 484-490
    • Rubenstein, R.C.1    Zeitlin, P.L.2
  • 64
    • 64749115962 scopus 로고    scopus 로고
    • A soluble sulfogalactosyl ceramide mimic promotes αF508 CFTR escape from endoplasmic reticulum associated degradation
    • Park, H. J., Mylvaganum, M., McPherson, A., Fewell, S. W., Brodsky, J. L., and Lingwood, C. A. (2009) A soluble sulfogalactosyl ceramide mimic promotes αF508 CFTR escape from endoplasmic reticulum associated degradation.. Chem. Biol. 16, 461-470
    • (2009) Chem. Biol. , vol.16 , pp. 461-470
    • Park, H.J.1    Mylvaganum, M.2    McPherson, A.3    Fewell, S.W.4    Brodsky, J.L.5    Lingwood, C.A.6
  • 65
    • 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. T., Walsh, P., Beilharz, T., Lithgow, T., and Brodsky, J. L. (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.T.1    Walsh, P.2    Beilharz, T.3    Lithgow, T.4    Brodsky, J.L.5
  • 66
    • 33947134399 scopus 로고    scopus 로고
    • Small heat-shock proteins select αF508-CFTR for endoplasmic reticulum-associated degradation
    • Ahner, A., Nakatsukasa, K., Zhang, H., Frizzell, R. A., and Brodsky, J. L. (2007) Small heat-shock proteins select αF508-CFTR for endoplasmic reticulum-associated degradation. Mol. Biol. Cell 18, 806-814
    • (2007) Mol. Biol. Cell , vol.18 , pp. 806-814
    • Ahner, A.1    Nakatsukasa, K.2    Zhang, H.3    Frizzell, R.A.4    Brodsky, J.L.5
  • 67
    • 0031106603 scopus 로고    scopus 로고
    • Chaperones get in touch: The Hip-Hop connection
    • Frydman, J., and Höhfeld, J. (1997) Chaperones get in touch: the Hip-Hop connection. Trends Biochem. Sci. 22, 87-92
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 87-92
    • Frydman, J.1    Höhfeld, J.2


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