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Volumn 289, Issue 1, 2014, Pages 1-12

CD4 and BST-2/tetherin proteins retro-translocate from endoplasmic reticulum to cytosol as partially folded and multimeric molecules

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; AMINO ACIDS; CELL MEMBRANES; COVALENT BONDS; GLYCOPROTEINS; MOLECULES;

EID: 84891724006     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.512368     Document Type: Article
Times cited : (22)

References (69)
  • 2
    • 36749001066 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
    • DOI 10.1038/nature06384, PII NATURE06384
    • Rapoport, T. A. (2007) Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes. Nature 450, 663-669 (Pubitemid 350207698)
    • (2007) Nature , vol.450 , Issue.7170 , pp. 663-669
    • Rapoport, T.A.1
  • 3
    • 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
  • 4
    • 26444575860 scopus 로고    scopus 로고
    • Retrotranslocation of the chaperone calreticulin from the endoplasmic reticulum lumen to the cytosol
    • DOI 10.1128/MCB.25.20.8844-8853.2005
    • Afshar, N., Black, B. E., and Paschal, B. M. (2005) Retrotranslocation of the chaperone calreticulin from the endoplasmic reticulum lumen to the cytosol. Mol. Cell. Biol. 25, 8844-8853 (Pubitemid 41429076)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.20 , pp. 8844-8853
    • Afshar, N.1    Black, B.E.2    Paschal, B.M.3
  • 5
    • 80455143829 scopus 로고    scopus 로고
    • BAP31 and BiP are essential for dislocation of SV40 from the endoplasmic reticulum to the cytosol
    • Geiger, R., Andritschke, D., Friebe, S., Herzog, F., Luisoni, S., Heger, T., and Helenius, A. (2011) BAP31 and BiP are essential for dislocation of SV40 from the endoplasmic reticulum to the cytosol. Nat. Cell Biol. 13, 1305-1314
    • (2011) Nat. Cell Biol. , vol.13 , pp. 1305-1314
    • Geiger, R.1    Andritschke, D.2    Friebe, S.3    Herzog, F.4    Luisoni, S.5    Heger, T.6    Helenius, A.7
  • 6
    • 84864051812 scopus 로고    scopus 로고
    • Cytosolic entry of Shiga-like toxin a chain from the yeast endoplasmic reticulum requires catalytically active Hrd1p
    • Li, S., Spooner, R. A., Hampton, R. Y., Lord, J. M., and Roberts, L. M. (2012) Cytosolic entry of Shiga-like toxin a chain from the yeast endoplasmic reticulum requires catalytically active Hrd1p. PLoS One 7, e41119
    • (2012) PLoS One , vol.7
    • Li, S.1    Spooner, R.A.2    Hampton, R.Y.3    Lord, J.M.4    Roberts, L.M.5
  • 7
    • 30344485142 scopus 로고    scopus 로고
    • Entry of protein toxins into mammalian cells by crossing the endoplasmic reticulum membrane: Co-opting basic mechanisms of endoplasmic reticulum-associated degradation
    • Lord, J. M., Roberts, L. M., and Lencer, W. I. (2005) Entry of protein toxins into mammalian cells by crossing the endoplasmic reticulum membrane: co-opting basic mechanisms of endoplasmic reticulum-associated degradation. Curr. Top. Microbiol. Immunol. 300, 149-168 (Pubitemid 43057940)
    • (2006) Current Topics in Microbiology and Immunology , vol.300 , pp. 149-168
    • Lord, J.M.1    Roberts, L.M.2    Lencer, W.I.3
  • 8
    • 79956042755 scopus 로고    scopus 로고
    • A single point mutation in ricin A-chain increases toxin degradation and inhibits EDEM1-dependent ER retrotranslocation
    • Sokołowska, I., Wälchli, S., Wȩgrzyn, G., Sandvig, K., and Słominska-Wojewódzka, M. (2011) A single point mutation in ricin A-chain increases toxin degradation and inhibits EDEM1-dependent ER retrotranslocation. Biochem. J. 436, 371-385
    • (2011) Biochem. J. , vol.436 , pp. 371-385
    • Sokołowska, I.1    Wälchli, S.2    Wȩgrzyn, G.3    Sandvig, K.4    Słominska-Wojewódzka, M.5
  • 9
    • 0036839684 scopus 로고    scopus 로고
    • Transfer of the cholera toxin A1 polypeptide from the endoplasmic reticulum to the cytosol is a rapid process facilitated by the endoplasmic reticulum-associated degradation pathway
    • DOI 10.1128/IAI.70.11.6166-6171.2002
    • Teter, K., Allyn, R. L., Jobling, M. G., and Holmes, R. K. (2002) Transfer of the cholera toxin A1 polypeptide from the endoplasmic reticulum to the cytosol is a rapid process facilitated by the endoplasmic reticulum-associated degradation pathway. Infect. Immun. 70, 6166-6171 (Pubitemid 35192707)
    • (2002) Infection and Immunity , vol.70 , Issue.11 , pp. 6166-6171
    • Teter, K.1    Allyn, R.L.2    Jobling, M.G.3    Holmes, R.K.4
  • 10
    • 79954423426 scopus 로고    scopus 로고
    • ERAD and ERAD tuning: Disposal of cargo and of ERAD regulators from the mammalian ER
    • Bernasconi, R., and Molinari, M. (2011) ERAD and ERAD tuning: disposal of cargo and of ERAD regulators from the mammalian ER. Curr. Opin. Cell Biol. 23, 176-183
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 176-183
    • Bernasconi, R.1    Molinari, M.2
  • 11
    • 80051975610 scopus 로고    scopus 로고
    • Efficient detection of proteins retro-translocated from the ER to the cytosol by in vivo biotinylation
    • Petris, G., Vecchi, L., Bestagno, M., and Burrone, O. R. (2011) Efficient detection of proteins retro-translocated from the ER to the cytosol by in vivo biotinylation. PLoS One 6, e23712
    • (2011) PLoS One , vol.6
    • Petris, G.1    Vecchi, L.2    Bestagno, M.3    Burrone, O.R.4
  • 14
    • 38549095979 scopus 로고    scopus 로고
    • Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu
    • DOI 10.1038/nature06553, PII NATURE06553
    • Neil, S. J., Zang, T., and Bieniasz, P. D. (2008) Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu. Nature 451, 425-430 (Pubitemid 351158893)
    • (2008) Nature , vol.451 , Issue.7177 , pp. 425-430
    • Neil, S.J.D.1    Zang, T.2    Bieniasz, P.D.3
  • 16
    • 60049094369 scopus 로고    scopus 로고
    • Inhibition of Lassa and Marburg virus production by tetherin
    • Sakuma, T., Noda, T., Urata, S., Kawaoka, Y., and Yasuda, J. (2009) Inhibition of Lassa and Marburg virus production by tetherin. J. Virol. 83, 2382-2385
    • (2009) J. Virol. , vol.83 , pp. 2382-2385
    • Sakuma, T.1    Noda, T.2    Urata, S.3    Kawaoka, Y.4    Yasuda, J.5
  • 17
    • 20244374809 scopus 로고
    • Molecular cloning and chromosomal mapping of a bone marrow stromal cell surface gene, BST2, that may be involved in pre-B-cell growth
    • Ishikawa, J., Kaisho, T., Tomizawa, H., Lee, B. O., Kobune, Y., Inazawa, J., Oritani, K., Itoh, M., Ochi, T., and Ishihara, K. (1995) Molecular cloning and chromosomal mapping of a bone marrow stromal cell surface gene, BST2, that may be involved in pre-B-cell growth. Genomics 26, 527-534
    • (1995) Genomics , vol.26 , pp. 527-534
    • Ishikawa, J.1    Kaisho, T.2    Tomizawa, H.3    Lee, B.O.4    Kobune, Y.5    Inazawa, J.6    Oritani, K.7    Itoh, M.8    Ochi, T.9    Ishihara, K.10
  • 18
    • 0141494290 scopus 로고    scopus 로고
    • Bst-2/HM1.24 is a raft-associated apical membrane protein with an unusual topology
    • DOI 10.1034/j.1600-0854.2003.00129.x
    • Kupzig, S., Korolchuk, V., Rollason, R., Sugden, A., Wilde, A., and Banting, G. (2003) Bst-2/HM1.24 is a raft-associated apical membrane protein with an unusual topology. Traffic 4, 694-709 (Pubitemid 37168591)
    • (2003) Traffic , vol.4 , Issue.10 , pp. 694-709
    • Kupzig, S.1    Korolchuk, V.2    Rollason, R.3    Sugden, A.4    Wilde, A.5    Banting, G.6
  • 19
    • 77954047969 scopus 로고    scopus 로고
    • Multilayered mechanism of CD4 down-regulation by HIV-1 Vpu involving distinct ER retention and ERAD targeting steps
    • Magadán, J. G., Pérez-Victoria, F. J., Sougrat, R., Ye, Y., Strebel, K., and Bonifacino, J. S. (2010) Multilayered mechanism of CD4 down-regulation by HIV-1 Vpu involving distinct ER retention and ERAD targeting steps. PLoS Pathog. 6, e1000869
    • (2010) PLoS Pathog. , vol.6
    • Magadán, J.G.1    Pérez-Victoria, F.J.2    Sougrat, R.3    Ye, Y.4    Strebel, K.5    Bonifacino, J.S.6
  • 20
    • 0032012456 scopus 로고    scopus 로고
    • A novel human WD protein, h-βTrCP, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif
    • Margottin, F., Bour, S. P., Durand, H., Selig, L., Benichou, S., Richard, V., Thomas, D., Strebel, K., and Benarous, R. (1998) A novel human WD protein, h-αTrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif. Mol. Cell 1, 565-574 (Pubitemid 128374692)
    • (1998) Molecular Cell , vol.1 , Issue.4 , pp. 565-574
    • Margottin, F.1    Bour, S.P.2    Durand, H.3    Selig, L.4    Benichou, S.5    Richard, V.6    Thomas, D.7    Strebel, K.8    Benarous, R.9
  • 21
    • 0031935031 scopus 로고    scopus 로고
    • CD4 glycoprotein degradation induced by human immunodeficiency virus type 1 Vpu protein requires the function of proteasomes and the ubiquitin- conjugating pathway
    • Schubert, U., Antón, L. C., Bacík, I., Cox, J. H., Bour, S., Bennink, J. R., Orlowski, M., Strebel, K., and Yewdell, J. W. (1998) CD4 glycoprotein degradation induced by human immunodeficiency virus type 1 Vpu protein requires the function of proteasomes and the ubiquitin-conjugating pathway. J. Virol. 72, 2280-2288 (Pubitemid 28100787)
    • (1998) Journal of Virology , vol.72 , Issue.3 , pp. 2280-2288
    • Schubert, U.1    Anton, L.C.2    Bacik, I.3    Cox, J.H.4    Bour, S.5    Bennink, J.R.6    Orlowski, M.7    Strebel, K.8    Yewdell, J.W.9
  • 22
    • 67749095196 scopus 로고    scopus 로고
    • Vpu directs the degradation of the human immunodeficiency virus restriction factor BST-2/Tetherin via a αTrCP-dependent mechanism
    • Douglas, J. L., Viswanathan, K., McCarroll, M. N., Gustin, J. K., Früh, K., and Moses, A. V. (2009) Vpu directs the degradation of the human immunodeficiency virus restriction factor BST-2/Tetherin via a αTrCP-dependent mechanism. J. Virol. 83, 7931-7947
    • (2009) J. Virol. , vol.83 , pp. 7931-7947
    • Douglas, J.L.1    Viswanathan, K.2    McCarroll, M.N.3    Gustin, J.K.4    Früh, K.5    Moses, A.V.6
  • 24
    • 71749086904 scopus 로고    scopus 로고
    • HIV-1 accessory protein Vpu internalizes cell-surface BST-2/tetherin through transmembrane interactions leading to lysosomes
    • Iwabu, Y., Fujita, H., Kinomoto, M., Kaneko, K., Ishizaka, Y., Tanaka, Y., Sata, T., and Tokunaga, K. (2009) HIV-1 accessory protein Vpu internalizes cell-surface BST-2/tetherin through transmembrane interactions leading to lysosomes. J. Biol. Chem. 284, 35060-35072
    • (2009) J. Biol. Chem. , vol.284 , pp. 35060-35072
    • Iwabu, Y.1    Fujita, H.2    Kinomoto, M.3    Kaneko, K.4    Ishizaka, Y.5    Tanaka, Y.6    Sata, T.7    Tokunaga, K.8
  • 25
    • 70349663496 scopus 로고    scopus 로고
    • HIV-1 Vpu neutralizes the antiviral factor Tetherin/BST-2 by binding it and directing its α-TrCP2-dependent degradation
    • Mangeat, B., Gers-Huber, G., Lehmann, M., Zufferey, M., Luban, J., and Piguet, V. (2009) HIV-1 Vpu neutralizes the antiviral factor Tetherin/BST-2 by binding it and directing its α-TrCP2-dependent degradation. PLoS Pathog. 5, e1000574
    • (2009) PLoS Pathog. , vol.5
    • Mangeat, B.1    Gers-Huber, G.2    Lehmann, M.3    Zufferey, M.4    Luban, J.5    Piguet, V.6
  • 27
    • 0032917076 scopus 로고    scopus 로고
    • A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation
    • Beckett, D., Kovaleva, E., and Schatz, P. J. (1999) A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation. Protein Sci. 8, 921-929 (Pubitemid 29165423)
    • (1999) Protein Science , vol.8 , Issue.4 , pp. 921-929
    • Beckett, D.1    Kovaleva, E.2    Schatz, P.J.3
  • 28
    • 78951496038 scopus 로고    scopus 로고
    • Structural and biophysical analysis of BST-2/tetherin ectodomains reveals an evolutionary conserved design to inhibit virus release
    • Swiecki, M., Scheaffer, S. M., Allaire, M., Fremont, D. H., Colonna, M., and Brett, T. J. (2011) Structural and biophysical analysis of BST-2/tetherin ectodomains reveals an evolutionary conserved design to inhibit virus release. J. Biol. Chem. 286, 2987-2997
    • (2011) J. Biol. Chem. , vol.286 , pp. 2987-2997
    • Swiecki, M.1    Scheaffer, S.M.2    Allaire, M.3    Fremont, D.H.4    Colonna, M.5    Brett, T.J.6
  • 29
    • 0026567269 scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein regulates the formation of intracellular gp160-CD4 complexes
    • Willey, R. L., Maldarelli, F., Martin, M. A., and Strebel, K. (1992) Human immunodeficiency virus type 1 Vpu protein regulates the formation of intracellular gp160-CD4 complexes. J. Virol. 66, 226-234
    • (1992) J. Virol. , vol.66 , pp. 226-234
    • Willey, R.L.1    Maldarelli, F.2    Martin, M.A.3    Strebel, K.4
  • 30
    • 43049102042 scopus 로고    scopus 로고
    • In vivo site-specific biotinylation of proteins within the secretory pathway using a single vector system
    • Predonzani, A., Arnoldi, F., López-Requena, A., and Burrone, O. R. (2008) In vivo site-specific biotinylation of proteins within the secretory pathway using a single vector system. BMC Biotechnol. 8, 41
    • (2008) BMC Biotechnol. , vol.8 , pp. 41
    • Predonzani, A.1    Arnoldi, F.2    López-Requena, A.3    Burrone, O.R.4
  • 31
    • 79956014819 scopus 로고    scopus 로고
    • Induction of lysosomal dilatation, arrested autophagy, and cell death by chloroquine in cultured ARPE-19 cells
    • Yoon, Y. H., Cho, K. S., Hwang, J. J., Lee, S. J., Choi, J. A., and Koh, J. Y. (2010) Induction of lysosomal dilatation, arrested autophagy, and cell death by chloroquine in cultured ARPE-19 cells. Invest. Ophthalmol. Vis. Sci. 51, 6030-6037
    • (2010) Invest. Ophthalmol. Vis. Sci. , vol.51 , pp. 6030-6037
    • Yoon, Y.H.1    Cho, K.S.2    Hwang, J.J.3    Lee, S.J.4    Choi, J.A.5    Koh, J.Y.6
  • 32
    • 36249022750 scopus 로고    scopus 로고
    • Characterization of an ERAD Pathway for Nonglycosylated BiP Substrates, which Require Herp
    • DOI 10.1016/j.molcel.2007.09.012, PII S1097276507006247
    • 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 (Pubitemid 350137789)
    • (2007) Molecular Cell , vol.28 , Issue.4 , pp. 544-554
    • Okuda-Shimizu, Y.1    Hendershot, L.M.2
  • 33
    • 0035167960 scopus 로고    scopus 로고
    • Polyubiquitination is required for US11-dependent movement of MHC class I heavy chain from endoplasmic reticulum into cytosol
    • Shamu, C. E., Flierman, D., Ploegh, H. L., Rapoport, T. A., and Chau, V. (2001) Polyubiquitination is required for US11-dependent movement of MHC class I heavy chain from endoplasmic reticulum into cytosol. Mol. Biol. Cell 12, 2546-2555 (Pubitemid 33051974)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.8 , pp. 2546-2555
    • Shamu, C.E.1    Flierman, D.2    Ploegh, H.L.3    Rapoport, T.A.4    Chau, V.5
  • 34
    • 0034689054 scopus 로고    scopus 로고
    • Cholera toxin is exported from microsomes by the Sec61p complex
    • Schmitz, A., Herrgen, H., Winkeler, A., and Herzog, V. (2000) Cholera toxin is exported from microsomes by the Sec61p complex. J. Cell Biol. 148, 1203-1212
    • (2000) J. Cell Biol. , vol.148 , pp. 1203-1212
    • Schmitz, A.1    Herrgen, H.2    Winkeler, A.3    Herzog, V.4
  • 35
    • 0029828991 scopus 로고    scopus 로고
    • Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
    • DOI 10.1038/384432a0
    • Wiertz, E. J., Tortorella, D., Bogyo, M., Yu, J., Mothes, W., Jones, T. R., Rapoport, T. A., and Ploegh, H. L. (1996) Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 384, 432-438 (Pubitemid 26414653)
    • (1996) Nature , vol.384 , Issue.6608 , pp. 432-438
    • Wiertz, E.J.H.J.1    Tortorella, D.2    Bogyo, M.3    Yu, J.4    Mothes, W.5    Jones, T.R.6    Rapoport, T.A.7    Ploegh, H.L.8
  • 36
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the ER
    • DOI 10.1038/nature02592
    • Lilley, B. N., and Ploegh, H. L. (2004) A membrane protein required for dislocation of misfolded proteins from the ER. Nature 429, 834-840 (Pubitemid 38843291)
    • (2004) Nature , vol.429 , Issue.6994 , pp. 834-840
    • Lilley, B.N.1    Ploegh, H.L.2
  • 37
    • 33846008398 scopus 로고    scopus 로고
    • Derlin-1 promotes the efficient degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) and CFTR folding mutants
    • DOI 10.1074/jbc.M607085200
    • Sun, F., Zhang, R., Gong, X., Geng, X., Drain, P. F., and Frizzell, R. A. (2006) Derlin-1 promotes the efficient degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) and CFTR folding mutants. J. Biol. Chem. 281, 36856-36863 (Pubitemid 46042153)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.48 , pp. 36856-36863
    • Sun, F.1    Zhang, R.2    Gong, X.3    Geng, X.4    Drain, P.F.5    Frizzell, R.A.6
  • 38
    • 77953811896 scopus 로고    scopus 로고
    • TRAM1 is involved in disposal of ER membrane degradation substrates
    • Ng, C. L., Oresic, K., and Tortorella, D. (2010) TRAM1 is involved in disposal of ER membrane degradation substrates. Exp. Cell Res. 316, 2113-2122
    • (2010) Exp. Cell Res. , vol.316 , pp. 2113-2122
    • Ng, C.L.1    Oresic, K.2    Tortorella, D.3
  • 39
    • 44649096231 scopus 로고    scopus 로고
    • BAP31 Interacts with Sec61 Translocons and Promotes Retrotranslocation of CFTRΔF508 via the Derlin-1 Complex
    • DOI 10.1016/j.cell.2008.04.042, PII S0092867408006168
    • Wang, B., Heath-Engel, H., Zhang, D., Nguyen, N., Thomas, D. Y., Hanrahan, J. W., and Shore, G. C. (2008) BAP31 interacts with Sec61 translocons and promotes retrotranslocation of CFTRΔF508 via the derlin-1 complex. Cell 133, 1080-1092 (Pubitemid 351787744)
    • (2008) Cell , vol.133 , Issue.6 , pp. 1080-1092
    • Wang, B.1    Heath-Engel, H.2    Zhang, D.3    Nguyen, N.4    Thomas, D.Y.5    Hanrahan, J.W.6    Shore, G.C.7
  • 40
    • 33749353475 scopus 로고    scopus 로고
    • P97 functions as an auxiliary factor to facilitate TM domain extraction during CFTR ER-associated degradation
    • DOI 10.1038/sj.emboj.7601307, PII 7601307
    • 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 (Pubitemid 44498129)
    • (2006) EMBO Journal , vol.25 , Issue.19 , pp. 4557-4566
    • Carlson, E.J.1    Pitonzo, D.2    Skach, W.R.3
  • 41
    • 1042278180 scopus 로고    scopus 로고
    • Distinct steps in dislocation of luminal endoplasmic reticulum-associated degradation substrates. Roles of endoplasmic reticulum-bound p97/Cdc48p and proteasome
    • DOI 10.1074/jbc.M309938200
    • Elkabetz, Y., Shapira, I., Rabinovich, E., and Bar-Nun, S. (2004) Distinct steps in dislocation of luminal endoplasmic reticulum-associated degradation substrates: roles of endoplasmic reticulum-bound p97/Cdc48p and proteasome. J. Biol. Chem. 279, 3980-3989 (Pubitemid 38198980)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.6 , pp. 3980-3989
    • Elkabetz, Y.1    Shapira, I.2    Rabinovich, E.3    Bar-Nun, S.4
  • 42
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • DOI 10.1038/414652a
    • 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 (Pubitemid 33151262)
    • (2001) Nature , vol.414 , Issue.6864 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 43
    • 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
  • 45
    • 79954417748 scopus 로고    scopus 로고
    • Disulfide bonds in ER protein folding and homeostasis
    • Feige, M. J., and Hendershot, L. M. (2011) Disulfide bonds in ER protein folding and homeostasis. Curr. Opin. Cell Biol. 23, 167-175
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 167-175
    • Feige, M.J.1    Hendershot, L.M.2
  • 46
    • 84855320818 scopus 로고    scopus 로고
    • Protein quality control in the ER: Balancing the ubiquitin checkbook
    • Claessen, J. H., Kundrat, L., and Ploegh, H. L. (2012) Protein quality control in the ER: balancing the ubiquitin checkbook. Trends Cell Biol. 22, 22-32
    • (2012) Trends Cell Biol. , vol.22 , pp. 22-32
    • Claessen, J.H.1    Kundrat, L.2    Ploegh, H.L.3
  • 47
    • 84862007841 scopus 로고    scopus 로고
    • Selective targeting of proteins within secretory pathway for endoplasmic reticulum-associated degradation
    • Vecchi, L., Petris, G., Bestagno, M., and Burrone, O. R. (2012) Selective targeting of proteins within secretory pathway for endoplasmic reticulum-associated degradation. J. Biol. Chem. 287, 20007-20015
    • (2012) J. Biol. Chem. , vol.287 , pp. 20007-20015
    • Vecchi, L.1    Petris, G.2    Bestagno, M.3    Burrone, O.R.4
  • 48
    • 84881398313 scopus 로고    scopus 로고
    • Decoupling the role of ubiquitination for the dislocation versus degradation of major histocompatibility complex (MHC) class I proteins during endoplasmic reticulum-associated degradation (ERAD)
    • Wang, X., Yu, Y. Y., Myers, N., and Hansen, T. H. (2013) Decoupling the role of ubiquitination for the dislocation versus degradation of major histocompatibility complex (MHC) class I proteins during endoplasmic reticulum-associated degradation (ERAD). J. Biol. Chem. 288, 23295-23306
    • (2013) J. Biol. Chem. , vol.288 , pp. 23295-23306
    • Wang, X.1    Yu, Y.Y.2    Myers, N.3    Hansen, T.H.4
  • 49
    • 78650434660 scopus 로고    scopus 로고
    • Compartment-restricted biotinylation reveals novel features of prion protein metabolism in vivo
    • Emerman, A. B., Zhang, Z. R., Chakrabarti, O., and Hegde, R. S. (2010) Compartment-restricted biotinylation reveals novel features of prion protein metabolism in vivo. Mol. Biol. Cell 21, 4325-4337
    • (2010) Mol. Biol. Cell , vol.21 , pp. 4325-4337
    • Emerman, A.B.1    Zhang, Z.R.2    Chakrabarti, O.3    Hegde, R.S.4
  • 50
    • 0036499973 scopus 로고    scopus 로고
    • Visualization of the ER-to-cytosol dislocation reaction of a type I membrane protein
    • DOI 10.1093/emboj/21.5.1041
    • Fiebiger, E., Story, C., Ploegh, H. L., and Tortorella, D. (2002) Visualization of the ER-to-cytosol dislocation reaction of a type I membrane protein. EMBO J. 21, 1041-1053 (Pubitemid 34206177)
    • (2002) EMBO Journal , vol.21 , Issue.5 , pp. 1041-1053
    • Fiebiger, E.1    Story, C.2    Ploegh, H.L.3    Tortorella, D.4
  • 51
    • 0037470054 scopus 로고    scopus 로고
    • Protein unfolding is not a prerequisite for endoplasmic reticulum-to-cytosol dislocation
    • DOI 10.1074/jbc.M210158200
    • Tirosh, B., Furman, M. H., Tortorella, D., and Ploegh, H. L. (2003) Protein unfolding is not a prerequisite for endoplasmic reticulum-to-cytosol dislocation. J. Biol. Chem. 278, 6664-6672 (Pubitemid 36800652)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.9 , pp. 6664-6672
    • Tirosh, B.1    Furman, M.H.2    Tortorella, D.3    Ploegh, H.L.4
  • 52
    • 33748658449 scopus 로고    scopus 로고
    • Murine polyomavirus requires the endoplasmic reticulum protein Derlin-2 to initiate infection
    • DOI 10.1128/JVI.00791-06
    • Lilley, B. N., Gilbert, J. M., Ploegh, H. L., and Benjamin, T. L. (2006) Murine polyomavirus requires the endoplasmic reticulum protein Derlin-2 to initiate infection. J. Virol. 80, 8739-8744 (Pubitemid 44384883)
    • (2006) Journal of Virology , vol.80 , Issue.17 , pp. 8739-8744
    • Lilley, B.N.1    Gilbert, J.M.2    Ploegh, H.L.3    Benjamin, T.L.4
  • 53
    • 1442313919 scopus 로고    scopus 로고
    • A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised
    • DOI 10.1038/sj.emboj.7600090
    • Blom, D., Hirsch, C., Stern, P., Tortorella, D., and Ploegh, H. L. (2004) A glycosylated type I membrane protein becomes cytosolic when peptide N-glycanase is compromised. EMBO J. 23, 650-658 (Pubitemid 38282396)
    • (2004) EMBO Journal , vol.23 , Issue.3 , pp. 650-658
    • Blom, D.1    Hirsch, C.2    Stern, P.3    Tortorella, D.4    Ploegh, H.L.5
  • 54
    • 10644226176 scopus 로고    scopus 로고
    • Using a small molecule inhibitor of peptide: N-glycanaseto probe its role in glycoprotein turnover
    • DOI 10.1016/j.chembiol.2004.11.010, PII S1074552104003345
    • Misaghi, S., Pacold, M. E., Blom, D., Ploegh, H. L., and Korbel, G. A. (2004) Using a small molecule inhibitor of peptideN-glycanase to probe its role in glycoprotein turnover. Chem. Biol. 11, 1677-1687 (Pubitemid 39651302)
    • (2004) Chemistry and Biology , vol.11 , Issue.12 , pp. 1677-1687
    • Misaghi, S.1    Pacold, M.E.2    Blom, D.3    Ploegh, H.L.4    Korbel, G.A.5
  • 55
    • 0032572582 scopus 로고    scopus 로고
    • Dislocation of type I membrane proteins from the er to the cytosol is sensitive to changes in redox potential
    • DOI 10.1083/jcb.142.2.365
    • Tortorella, D., Story, C. M., Huppa, J. B., Wiertz, E. J., Jones, T. R., Bacik, I., Bennink, J. R., Yewdell, J. W., and Ploegh, H. L. (1998) Dislocation of type I membrane proteins from the ER to the cytosol is sensitive to changes in redox potential. J. Cell Biol. 142, 365-376 (Pubitemid 28361545)
    • (1998) Journal of Cell Biology , vol.142 , Issue.2 , pp. 365-376
    • Tortorella, D.1    Story, C.M.2    Huppa, J.B.3    Wiertz, E.J.H.J.4    Jones, T.R.5    Ploegh, H.L.6
  • 56
    • 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
  • 58
    • 48249117110 scopus 로고    scopus 로고
    • ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER
    • Ushioda, R., Hoseki, J., Araki, K., Jansen, G., Thomas, D. Y., and Nagata, K. (2008) ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER. Science 321, 569-572
    • (2008) Science , vol.321 , pp. 569-572
    • Ushioda, R.1    Hoseki, J.2    Araki, K.3    Jansen, G.4    Thomas, D.Y.5    Nagata, K.6
  • 59
    • 33645827537 scopus 로고    scopus 로고
    • EDEM accelerates ERAD by preventing aberrant dimer formation of misfolded α1-antitrypsin
    • Hosokawa, N., Wada, I., Natsuka, Y., and Nagata, K. (2006) EDEM accelerates ERAD by preventing aberrant dimer formation of misfolded α1-antitrypsin. Genes Cells 11, 465-476
    • (2006) Genes Cells , vol.11 , pp. 465-476
    • Hosokawa, N.1    Wada, I.2    Natsuka, Y.3    Nagata, K.4
  • 61
    • 0030911709 scopus 로고    scopus 로고
    • Dimeric association and segmental variability in the structure of human CD4
    • DOI 10.1038/387527a0
    • Wu, H., Kwong, P. D., and Hendrickson, W. A. (1997) Dimeric association and segmental variability in the structure of human CD4. Nature 387, 527-530 (Pubitemid 27235474)
    • (1997) Nature , vol.387 , Issue.6632 , pp. 527-530
    • Wu, H.1    Kwong, P.D.2    Hendrickson, W.A.3
  • 64
    • 22744456680 scopus 로고    scopus 로고
    • The protein translocation channel binds proteasomes to the endoplasmic reticulum membrane
    • DOI 10.1038/sj.emboj.7600731
    • Kalies, K. U., Allan, S., Sergeyenko, T., Kröger, H., and Römisch, K. (2005) The protein translocation channel binds proteasomes to the endoplasmic reticulum membrane. EMBO J. 24, 2284-2293 (Pubitemid 41032581)
    • (2005) EMBO Journal , vol.24 , Issue.13 , pp. 2284-2293
    • Kalies, K.-U.1    Allan, S.2    Sergeyenko, T.3    Kroger, H.4    Romisch, K.5
  • 67
    • 0028961333 scopus 로고
    • Perforin: Structure and function
    • Liu, C. C., Walsh, C. M., and Young, J. D. (1995) Perforin: structure and function. Immunol. Today 16, 194-201
    • (1995) Immunol. Today , vol.16 , pp. 194-201
    • Liu, C.C.1    Walsh, C.M.2    Young, J.D.3
  • 68
    • 34547216748 scopus 로고    scopus 로고
    • A lipid-based model for the creation of an escape hatch from the endoplasmic reticulum
    • DOI 10.1038/nature06004, PII NATURE06004
    • Ploegh, H. L. (2007) A lipid-based model for the creation of an escape hatch from the endoplasmic reticulum. Nature 448, 435-438 (Pubitemid 47123517)
    • (2007) Nature , vol.448 , Issue.7152 , pp. 435-438
    • Ploegh, H.L.1
  • 69
    • 80051540452 scopus 로고    scopus 로고
    • Lipid droplet formation is dispensable for endoplasmic reticulum-associated degradation
    • Olzmann, J. A., and Kopito, R. R. (2011) Lipid droplet formation is dispensable for endoplasmic reticulum-associated degradation. J. Biol. Chem. 286, 27872-27874
    • (2011) J. Biol. Chem. , vol.286 , pp. 27872-27874
    • Olzmann, J.A.1    Kopito, R.R.2


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