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Volumn 33, Issue 8, 2014, Pages 477-483

The final moments of misfolded proteins en route to the proteasome

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CELL ENZYME; POLYPEPTIDE; PROTEASOME; UBIQUITINATED PROTEIN;

EID: 84905253325     PISSN: 10445498     EISSN: 15577430     Source Type: Journal    
DOI: 10.1089/dna.2014.2452     Document Type: Article
Times cited : (21)

References (68)
  • 1
    • 33947134399 scopus 로고    scopus 로고
    • Small heat-shock proteins select deltaF508-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 deltaF508-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
  • 2
    • 84865094127 scopus 로고    scopus 로고
    • Identification of the Cdc48*20S proteasome as an ancient AAA+ proteolytic machine
    • Barthelme, D., and Sauer, R.T. (2012). Identification of the Cdc48*20S proteasome as an ancient AAA+ proteolytic machine. Science 337, 843-846.
    • (2012) Science , vol.337 , pp. 843-846
    • Barthelme, D.1    Sauer, R.T.2
  • 3
    • 84874452437 scopus 로고    scopus 로고
    • Bipartite determinants mediate an evolutionarily conserved interaction between Cdc48 and the 20S peptidase
    • Barthelme, D., and Sauer, R.T. (2013). Bipartite determinants mediate an evolutionarily conserved interaction between Cdc48 and the 20S peptidase. Proc Natl Acad Sci U S A 110, 3327-3332.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 3327-3332
    • Barthelme, D.1    Sauer, R.T.2
  • 4
    • 0037076507 scopus 로고    scopus 로고
    • Cdc48-Ufd1-Npl4: Stuck in the middle with Ub
    • Bays, N.W., and Hampton, R.Y. (2002). Cdc48-Ufd1-Npl4: stuck in the middle with Ub. Curr Biol 12, R366-R371.
    • (2002) Curr Biol , vol.12
    • Bays, N.W.1    Hampton, R.Y.2
  • 5
    • 0035658442 scopus 로고    scopus 로고
    • HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins
    • Bays, N.W., Wilhovsky, S.K., Goradia, A., Hodgkiss-Harlow, K., and Hampton, R.Y. (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.W.1    Wilhovsky, S.K.2    Goradia, A.3    Hodgkiss-Harlow, K.4    Hampton, R.Y.5
  • 6
    • 33746228127 scopus 로고    scopus 로고
    • Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins
    • Carvalho, P., Goder, V., and Rapoport, T.A. (2006). Distinct ubiquitin-ligase 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
  • 7
    • 78149482323 scopus 로고    scopus 로고
    • Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p
    • Carvalho, P., Stanley, A.M., and Rapoport, T.A. (2010). Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p. Cell 143, 579-591.
    • (2010) Cell , vol.143 , pp. 579-591
    • Carvalho, P.1    Stanley, A.M.2    Rapoport, T.A.3
  • 9
    • 84898729879 scopus 로고    scopus 로고
    • Cleaning up in the endoplasmic reticulum: Ubiquitin in charge
    • Christianson, J.C., and Ye, Y. (2014). Cleaning up in the endoplasmic reticulum: ubiquitin in charge. Nat Struct Mol Biol 21, 325-335.
    • (2014) Nat Struct Mol Biol , vol.21 , pp. 325-335
    • Christianson, J.C.1    Ye, Y.2
  • 10
    • 82955207151 scopus 로고    scopus 로고
    • BAT3 guides misfolded glycoproteins out of the endoplasmic reticulum
    • Claessen, J.H., and Ploegh, H.L. (2011). BAT3 guides misfolded glycoproteins out of the endoplasmic reticulum. PLoS One 6, e28542.
    • (2011) PLoS One , vol.6
    • Claessen, J.H.1    Ploegh, H.L.2
  • 11
    • 0141507032 scopus 로고    scopus 로고
    • Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains
    • Delabarre, B., and Brunger, A.T. (2003). Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains. Nat Struct Biol 10, 856-863.
    • (2003) Nat Struct Biol , vol.10 , pp. 856-863
    • Delabarre, B.1    Brunger, A.T.2
  • 12
    • 14644415865 scopus 로고    scopus 로고
    • Nucleotide dependent motion and mechanism of action of p97/VCP
    • Delabarre, B., and Brunger, A.T. (2005). Nucleotide dependent motion and mechanism of action of p97/VCP. J Mol Biol 347, 437-452.
    • (2005) J Mol Biol , vol.347 , pp. 437-452
    • Delabarre, B.1    Brunger, A.T.2
  • 13
    • 33646535590 scopus 로고    scopus 로고
    • Central pore residues mediate the p97/VCP activity required for ERAD
    • Delabarre, B., Christianson, J.C., Kopito, R.R., and Brunger, A.T. (2006). Central pore residues mediate the p97/VCP activity required for ERAD. Mol Cell 22, 451-462.
    • (2006) Mol Cell , vol.22 , pp. 451-462
    • Delabarre, B.1    Christianson, J.C.2    Kopito, R.R.3    Brunger, A.T.4
  • 14
    • 33746208871 scopus 로고    scopus 로고
    • A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation
    • Denic, V., Quan, E.M., and Weissman, J.S. (2006). 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
  • 15
    • 0041315902 scopus 로고    scopus 로고
    • Polyubiquitin serves as a recognition signal, rather than a ratcheting molecule, during retrotranslocation of proteins across the endoplasmic reticulum membrane
    • Flierman, D., Ye, Y., Dai, M., Chau, V., and Rapoport, T.A. (2003). Polyubiquitin serves as a recognition signal, rather than a ratcheting molecule, during retrotranslocation of proteins across the endoplasmic reticulum membrane. J Biol Chem 278, 34774-34782.
    • (2003) J Biol Chem , vol.278 , pp. 34774-34782
    • Flierman, D.1    Ye, Y.2    Dai, M.3    Chau, V.4    Rapoport, T.A.5
  • 17
    • 33745265260 scopus 로고    scopus 로고
    • Protein disulfide isomerase-like proteins play opposing roles during retrotranslocation
    • Forster, M.L., Sivick, K., Park, Y.N., Arvan, P., Lencer, W.I., and Tsai, B. (2006). Protein disulfide isomerase-like proteins play opposing roles during retrotranslocation. J Cell Biol 173, 853-859.
    • (2006) J Cell Biol , vol.173 , pp. 853-859
    • Forster, M.L.1    Sivick, K.2    Park, Y.N.3    Arvan, P.4    Lencer, W.I.5    Tsai, B.6
  • 18
    • 33746587049 scopus 로고    scopus 로고
    • A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery
    • Gauss, R., Jarosch, E., Sommer, T., and Hirsch, C. (2006). A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery. Nat Cell Biol 8, 849-854.
    • (2006) Nat Cell Biol , vol.8 , pp. 849-854
    • Gauss, R.1    Jarosch, E.2    Sommer, T.3    Hirsch, C.4
  • 19
    • 0032079329 scopus 로고    scopus 로고
    • The ClpXP and ClpAP proteases degrade proteins with carboxyterminal peptide tails added by the SsrA-tagging system
    • Gottesman, S., Roche, E., Zhou, Y., and Sauer, R.T. (1998). The ClpXP and ClpAP proteases degrade proteins with carboxyterminal peptide tails added by the SsrA-tagging system. Genes Dev 12, 1338-1347.
    • (1998) Genes Dev , vol.12 , pp. 1338-1347
    • Gottesman, S.1    Roche, E.2    Zhou, Y.3    Sauer, R.T.4
  • 20
    • 33745224935 scopus 로고    scopus 로고
    • P97: The cell's molecular purgatory?
    • Halawani, D., and Latterich, M. (2006). p97: The cell's molecular purgatory? Mol Cell 22, 713-717.
    • (2006) Mol Cell , vol.22 , pp. 713-717
    • Halawani, D.1    Latterich, M.2
  • 21
    • 84865298998 scopus 로고    scopus 로고
    • Finding the will and the way of ERAD substrate retrotranslocation
    • Hampton, R.Y., and Sommer, T. (2012). Finding the will and the way of ERAD substrate retrotranslocation. Curr Opin Cell Biol 24, 460-466.
    • (2012) Curr Opin Cell Biol , vol.24 , pp. 460-466
    • Hampton, R.Y.1    Sommer, T.2
  • 22
    • 35748948975 scopus 로고    scopus 로고
    • In and out of the ER: Protein folding, quality control, degradation, and related human diseases
    • Hebert, D.N., and Molinari, M. (2007). In and out of the ER: protein folding, quality control, degradation, and related human diseases. Physiol Rev 87, 1377-1408.
    • (2007) Physiol Rev , vol.87 , pp. 1377-1408
    • Hebert, D.N.1    Molinari, M.2
  • 23
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
    • Hiller, M.M., Finger, A., Schweiger, M., and Wolf, D.H. (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.M.1    Finger, A.2    Schweiger, M.3    Wolf, D.H.4
  • 24
    • 21244480104 scopus 로고    scopus 로고
    • Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation
    • Hinnerwisch, J., Fenton, W.A., Furtak, K.J., Farr, G.W., and Horwich, A.L. (2005). Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation. Cell 121, 1029-1041.
    • (2005) Cell , vol.121 , pp. 1029-1041
    • Hinnerwisch, J.1    Fenton, W.A.2    Furtak, K.J.3    Farr, G.W.4    Horwich, A.L.5
  • 25
    • 0037416196 scopus 로고    scopus 로고
    • A role for Nglycanase in the cytosolic turnover of glycoproteins
    • Hirsch, C., Blom, D., and Ploegh, H.L. (2003). A role for Nglycanase in the cytosolic turnover of glycoproteins. EMBO J 22, 1036-1046.
    • (2003) EMBO J , vol.22 , pp. 1036-1046
    • Hirsch, C.1    Blom, D.2    Ploegh, H.L.3
  • 26
    • 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
  • 27
    • 80052212289 scopus 로고    scopus 로고
    • Stalled proteasomes are directly relieved by P97 recruitment
    • Isakov, E., and Stanhill, A. (2011). Stalled proteasomes are directly relieved by P97 recruitment. J Biol Chem 286, 30274-30283.
    • (2011) J Biol Chem , vol.286 , pp. 30274-30283
    • Isakov, E.1    Stanhill, A.2
  • 29
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson, E.S., Ma, P.C., Ota, I.M., and Varshavsky, A. (1995). A proteolytic pathway that recognizes ubiquitin as a degradation signal. J Biol Chem 270, 17442-17456.
    • (1995) J Biol Chem , vol.270 , pp. 17442-17456
    • Johnson, E.S.1    Ma, P.C.2    Ota, I.M.3    Varshavsky, A.4
  • 31
    • 3042764201 scopus 로고    scopus 로고
    • Multiple interactions of rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis
    • Kim, I., Mi, K., and Rao, H. (2004). Multiple interactions of rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis. Mol Biol Cell 15, 3357-3365.
    • (2004) Mol Biol Cell , vol.15 , pp. 3357-3365
    • Kim, I.1    Mi, K.2    Rao, H.3
  • 32
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • Koegl, M., Hoppe, T., Schlenker, S., Ulrich, H.D., Mayer, T.U., and Jentsch, S. (1999). A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 96, 635-644.
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1    Hoppe, T.2    Schlenker, S.3    Ulrich, H.D.4    Mayer, T.U.5    Jentsch, S.6
  • 33
    • 84874976264 scopus 로고    scopus 로고
    • Bag6/Bat3/Scythe: A novel chaperone activity with diverse regulatory functions in protein biogenesis and degradation
    • Lee, J.G., and Ye, Y. (2013). Bag6/Bat3/Scythe: a novel chaperone activity with diverse regulatory functions in protein biogenesis and degradation. Bioessays 35, 377-385.
    • (2013) Bioessays , vol.35 , pp. 377-385
    • Lee, J.G.1    Ye, Y.2
  • 35
    • 79960066445 scopus 로고    scopus 로고
    • Proteostasis regulation at the endoplasmic reticulum: A new perturbation site for targeted cancer therapy
    • Liu, Y., and Ye, Y. (2011). Proteostasis regulation at the endoplasmic reticulum: a new perturbation site for targeted cancer therapy. Cell Res 21, 867-883.
    • (2011) Cell Res , vol.21 , pp. 867-883
    • Liu, Y.1    Ye, Y.2
  • 36
    • 84856474838 scopus 로고    scopus 로고
    • Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system
    • Meyer, H., Bug, M., and Bremer, S. (2012). Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system. Nat Cell Biol 14, 117-123.
    • (2012) Nat Cell Biol , vol.14 , pp. 117-123
    • Meyer, H.1    Bug, M.2    Bremer, S.3
  • 37
    • 0037470410 scopus 로고    scopus 로고
    • Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle
    • Molinari, M., Calanca, V., Galli, C., Lucca, P., and Paganetti, P. (2003). Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle. Science 299, 1397-1400.
    • (2003) Science , vol.299 , pp. 1397-1400
    • Molinari, M.1    Calanca, V.2    Galli, C.3    Lucca, P.4    Paganetti, P.5
  • 38
    • 0037157856 scopus 로고    scopus 로고
    • Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER
    • Molinari, M., Galli, C., Piccaluga, V., Pieren, M., and Paganetti, P. (2002). Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER. J Cell Biol 158, 247-257.
    • (2002) J Cell Biol , vol.158 , pp. 247-257
    • Molinari, M.1    Galli, C.2    Piccaluga, V.3    Pieren, M.4    Paganetti, P.5
  • 39
    • 43149096666 scopus 로고    scopus 로고
    • The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum
    • Nakatsukasa, K., and Brodsky, J.L. (2008). The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum. Traffic 9, 861-870.
    • (2008) Traffic , vol.9 , pp. 861-870
    • Nakatsukasa, K.1    Brodsky, J.L.2
  • 40
    • 84878730933 scopus 로고    scopus 로고
    • A stalled retrotranslocation complex reveals physical linkage between substrate recognition and proteasomal degradation during ER-associated degradation
    • S1-S8
    • Nakatsukasa, K., Brodsky, J.L., and Kamura, T. (2013). A stalled retrotranslocation complex reveals physical linkage between substrate recognition and proteasomal degradation during ER-associated degradation. Mol Biol Cell 24, 1765-1775, S1-S8.
    • (2013) Mol Biol Cell , vol.24 , pp. 1765-1775
    • Nakatsukasa, K.1    Brodsky, J.L.2    Kamura, T.3
  • 41
    • 0037470515 scopus 로고    scopus 로고
    • EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin
    • Oda, Y., Hosokawa, N., Wada, I., and Nagata, K. (2003). EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin. Science 299, 1394-1397.
    • (2003) Science , vol.299 , pp. 1394-1397
    • Oda, Y.1    Hosokawa, N.2    Wada, I.3    Nagata, K.4
  • 42
    • 0037389970 scopus 로고    scopus 로고
    • Structural insights into the U-box, a domain associated with multi-ubiquitination
    • Ohi, M.D., Vander Kooi, C.W., Rosenberg, J.A., Chazin, W.J., and Gould, K.L. (2003). Structural insights into the U-box, a domain associated with multi-ubiquitination. Nat Struct Biol 10, 250-255.
    • (2003) Nat Struct Biol , vol.10 , pp. 250-255
    • Ohi, M.D.1    Vander Kooi, C.W.2    Rosenberg, J.A.3    Chazin, W.J.4    Gould, K.L.5
  • 43
    • 36249022750 scopus 로고    scopus 로고
    • Characterization of an ERAD pathway for nonglycosylated BiP substrates, which require Herp
    • Okuda-Shimizu, Y., and Hendershot, L.M. (2007). Characterization of an ERAD pathway for nonglycosylated BiP substrates, which require Herp. Mol Cell 28, 544-554.
    • (2007) Mol Cell , vol.28 , pp. 544-554
    • Okuda-Shimizu, Y.1    Hendershot, L.M.2
  • 44
    • 21744460209 scopus 로고    scopus 로고
    • Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites
    • Park, S., Isaacson, R., Kim, H.T., Silver, P.A., and Wagner, G. (2005). Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites. Structure 13, 995-1005.
    • (2005) Structure , vol.13 , pp. 995-1005
    • Park, S.1    Isaacson, R.2    Kim, H.T.3    Silver, P.A.4    Wagner, G.5
  • 47
    • 0036136901 scopus 로고    scopus 로고
    • AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation
    • Rabinovich, E., Kerem, A., Frohlich, 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    Frohlich, K.U.3    Diamant, N.4    Bar-Nun, S.5
  • 48
    • 11844263929 scopus 로고    scopus 로고
    • A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting
    • Richly, H., Rape, M., Braun, S., Rumpf, S., Hoege, C., and Jentsch, S. (2005). A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell 120, 73-84.
    • (2005) Cell , vol.120 , pp. 73-84
    • Richly, H.1    Rape, M.2    Braun, S.3    Rumpf, S.4    Hoege, C.5    Jentsch, S.6
  • 50
    • 49249130739 scopus 로고    scopus 로고
    • UBX domain proteins: Major regulators of the AAA ATPase Cdc48/p97
    • Schuberth, C., and Buchberger, A. (2008). UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97. Cell Mol Life Sci 65, 2360-2371.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 2360-2371
    • Schuberth, C.1    Buchberger, A.2
  • 51
    • 34548274872 scopus 로고    scopus 로고
    • Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry
    • Smith, D.M., Chang, S.C., Park, S., Finley, D., Cheng, Y., and Goldberg, A.L. (2007). Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry. Mol Cell 27, 731-744.
    • (2007) Mol Cell , vol.27 , pp. 731-744
    • Smith, D.M.1    Chang, S.C.2    Park, S.3    Finley, D.4    Cheng, Y.5    Goldberg, A.L.6
  • 52
    • 77954957347 scopus 로고    scopus 로고
    • A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of diseaserelated mutants
    • Tang, W.K., Li, D., Li, C.C., Esser, L., Dai, R., Guo, L., and Xia, D. (2010). A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of diseaserelated mutants. EMBO J 29, 2217-2229.
    • (2010) EMBO J , vol.29 , pp. 2217-2229
    • Tang, W.K.1    Li, D.2    Li, C.C.3    Esser, L.4    Dai, R.5    Guo, L.6    Xia, D.7
  • 53
    • 0036270698 scopus 로고    scopus 로고
    • Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
    • Tsai, B., Ye, Y., and Rapoport, T.A. (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.A.3
  • 54
    • 35649014889 scopus 로고    scopus 로고
    • Structure and function of the yeast U-box-containing ubiquitin ligase Ufd2p
    • Tu, D., Li, W., Ye, Y., and Brunger, A.T. (2007). Structure and function of the yeast U-box-containing ubiquitin ligase Ufd2p. Proc Natl Acad Sci U S A 104, 15599-15606.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 15599-15606
    • Tu, D.1    Li, W.2    Ye, Y.3    Brunger, A.T.4
  • 55
    • 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
  • 56
    • 0033791447 scopus 로고    scopus 로고
    • Proteasomal proteomics: Identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes
    • Verma, R., Chen, S., Feldman, R., Schieltz, D., Yates, J., Dohmen, J., and Deshaies, R.J. (2000). Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes. Mol Biol Cell 11, 3425-3439.
    • (2000) Mol Biol Cell , vol.11 , pp. 3425-3439
    • Verma, R.1    Chen, S.2    Feldman, R.3    Schieltz, D.4    Yates, J.5    Dohmen, J.6    Deshaies, R.J.7
  • 57
    • 3142566639 scopus 로고    scopus 로고
    • Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system
    • Verma, R., Oania, R., Graumann, J., and Deshaies, R.J. (2004). Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system. Cell 118, 99-110.
    • (2004) Cell , vol.118 , pp. 99-110
    • Verma, R.1    Oania, R.2    Graumann, J.3    Deshaies, R.J.4
  • 58
    • 79959347089 scopus 로고    scopus 로고
    • A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation
    • Wang, Q., Liu, Y., Soetandyo, N., Baek, K., Hegde, R., and Ye, Y. (2011). A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation. Mol Cell 42, 758-770.
    • (2011) Mol Cell , vol.42 , pp. 758-770
    • Wang, Q.1    Liu, Y.2    Soetandyo, N.3    Baek, K.4    Hegde, R.5    Ye, Y.6
  • 59
    • 1642309633 scopus 로고    scopus 로고
    • Molecular perspectives on p97-VCP: Progress in understanding its structure and diverse biological functions
    • Wang, Q., Song, C., and Li, C.C. (2004). Molecular perspectives on p97-VCP: progress in understanding its structure and diverse biological functions. J Struct Biol 146, 44-57.
    • (2004) J Struct Biol , vol.146 , pp. 44-57
    • Wang, Q.1    Song, C.2    Li, C.C.3
  • 60
    • 34249042608 scopus 로고    scopus 로고
    • Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3
    • Wang, X., Herr, R.A., Chua, W.J., Lybarger, L., Wiertz, E.J., and Hansen, T.H. (2007). Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3. J Cell Biol 177, 613-624.
    • (2007) J Cell Biol , vol.177 , pp. 613-624
    • Wang, X.1    Herr, R.A.2    Chua, W.J.3    Lybarger, L.4    Wiertz, E.J.5    Hansen, T.H.6
  • 62
    • 84871682623 scopus 로고    scopus 로고
    • SGTA recognizes a noncanonical ubiquitin-like domain in the Bag6- Ubl4A-Trc35 complex to promote endoplasmic reticulumassociated degradation
    • Xu, Y., Cai, M., Yang, Y., Huang, L., and Ye, Y. (2012). SGTA recognizes a noncanonical ubiquitin-like domain in the Bag6- Ubl4A-Trc35 complex to promote endoplasmic reticulumassociated degradation. Cell Rep 2, 1633-1644.
    • (2012) Cell Rep , vol.2 , pp. 1633-1644
    • Xu, Y.1    Cai, M.2    Yang, Y.3    Huang, L.4    Ye, Y.5
  • 63
    • 84880048596 scopus 로고    scopus 로고
    • A ubiquitin-like domain recruits an oligomeric chaperone to a retrotranslocation complex in endoplasmic reticulum-associated degradation
    • Xu, Y., Liu, Y., Lee, J.G., and Ye, Y. (2013). A ubiquitin-like domain recruits an oligomeric chaperone to a retrotranslocation complex in endoplasmic reticulum-associated degradation. J Biol Chem 288, 18068-18076.
    • (2013) J Biol Chem , vol.288 , pp. 18068-18076
    • Xu, Y.1    Liu, Y.2    Lee, J.G.3    Ye, Y.4
  • 64
    • 33749236210 scopus 로고    scopus 로고
    • Diverse functions with a common regulator: Ubiquitin takes command of an AAA ATPase
    • Ye, Y. (2006). Diverse functions with a common regulator: ubiquitin takes command of an AAA ATPase. J Struct Biol 156, 29-40.
    • (2006) J Struct Biol , vol.156 , pp. 29-40
    • Ye, Y.1
  • 65
    • 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.H., and Rapoport, T.A. (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.H.2    Rapoport, T.A.3
  • 66
    • 0038487228 scopus 로고    scopus 로고
    • Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: Dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains
    • Ye, Y., Meyer, H.H., and Rapoport, T.A. (2003). Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J Cell Biol 162, 71-84.
    • (2003) J Cell Biol , vol.162 , pp. 71-84
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 67
    • 70350461507 scopus 로고    scopus 로고
    • Building ubiquitin chains: E2 enzymes at work
    • Ye, Y., and Rape, M. (2009). Building ubiquitin chains: E2 enzymes at work. Nat Rev Mol Cell Biol 10, 755-764.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 755-764
    • Ye, Y.1    Rape, M.2


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