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Volumn 6, Issue 4, 2010, Pages 1-18

Multilayered mechanism of CD4 downregulation by HIV-1 vpu involving distinct ER retention and ERAD targeting steps

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; LYSINE; NEF PROTEIN; PROTEIN P97; SERINE; SMALL INTERFERING RNA; THREONINE; UBIQUITIN; VPU PROTEIN; CD4 ANTIGEN; CDC48 PROTEIN; CELL CYCLE PROTEIN; HUMAN IMMUNODEFICIENCY VIRUS PROTEIN; MULTIPROTEIN COMPLEX; NPLOC4 PROTEIN, HUMAN; NUCLEAR PROTEIN; PROTEIN; UFD1L PROTEIN, HUMAN; VIRUS PROTEIN; VPU PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 77954047969     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1000869     Document Type: Article
Times cited : (143)

References (67)
  • 1
    • 33645414100 scopus 로고    scopus 로고
    • HIV-1 coreceptors and their inhibitors
    • Ray N, Doms RW (2006) HIV-1 coreceptors and their inhibitors. Curr Top Microbiol Immunol 303: 97-120.
    • (2006) Curr Top Microbiol Immunol , vol.303 , pp. 97-120
    • Ray, N.1    Doms, R.W.2
  • 2
    • 0023003334 scopus 로고
    • Alterations in T4 (CD4) protein and mRNA synthesis in cells infected with HIV
    • Hoxie JA, Alpers JD, Rackowski JL, Huebner K, Haggarty BS, et al. (1986) Alterations in T4 (CD4) protein and mRNA synthesis in cells infected with HIV. Science 234: 1123-1127.
    • (1986) Science , vol.234 , pp. 1123-1127
    • Hoxie, J.A.1    Alpers, J.D.2    Rackowski, J.L.3    Huebner, K.4    Haggarty, B.S.5
  • 3
    • 0024204991 scopus 로고
    • Loss of CD4 membrane expression and CD4 mRNA during acute human immunodeficiency virus replication
    • Salmon P, Olivier R, Riviere Y, Brisson E, Gluckman JC, et al. (1988) Loss of CD4 membrane expression and CD4 mRNA during acute human immunodeficiency virus replication. J Exp Med 168: 1953-1969.
    • (1988) J Exp Med , vol.168 , pp. 1953-1969
    • Salmon, P.1    Olivier, R.2    Riviere, Y.3    Brisson, E.4    Gluckman, J.C.5
  • 5
    • 0026567269 scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein regulates the formation of intracellular gp160-CD4 complexes
    • Willey RL, Maldarelli F, Martin MA, 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
  • 6
    • 0141780822 scopus 로고    scopus 로고
    • Enhanced CD4 down-modulation by late stage HIV-1 nef alleles is associated with increased Env incorporation and viral replication
    • Arganaraz ER, Schindler M, Kirchhoff F, Cortes MJ, Lama J (2003) Enhanced CD4 down-modulation by late stage HIV-1 nef alleles is associated with increased Env incorporation and viral replication. J Biol Chem 278: 33912-33919.
    • (2003) J Biol Chem , vol.278 , pp. 33912-33919
    • Arganaraz, E.R.1    Schindler, M.2    Kirchhoff, F.3    Cortes, M.J.4    Lama, J.5
  • 7
    • 0023814638 scopus 로고
    • T cells can present antigens such as HIV gp120 targeted to their own surface molecules
    • Lanzavecchia A, Roosnek E, Gregory T, Berman P, Abrignani S (1988) T cells can present antigens such as HIV gp120 targeted to their own surface molecules. Nature 334: 530-532.
    • (1988) Nature , vol.334 , pp. 530-532
    • Lanzavecchia, A.1    Roosnek, E.2    Gregory, T.3    Berman, P.4    Abrignani, S.5
  • 8
    • 0034312298 scopus 로고    scopus 로고
    • The plasma membrane as a combat zone in the HIV battlefield
    • Doms RW, Trono D (2000) The plasma membrane as a combat zone in the HIV battlefield. Genes Dev 14: 2677-2688.
    • (2000) Genes Dev , vol.14 , pp. 2677-2688
    • Doms, R.W.1    Trono, D.2
  • 9
    • 33947627531 scopus 로고    scopus 로고
    • Mechanisms of CD4 downregulation by the Nef and Vpu proteins of primate immunodeficiency viruses
    • Lindwasser OW, Chaudhuri R, Bonifacino JS (2007) Mechanisms of CD4 downregulation by the Nef and Vpu proteins of primate immunodeficiency viruses. Curr Mol Med 7: 171-184.
    • (2007) Curr Mol Med , vol.7 , pp. 171-184
    • Lindwasser, O.W.1    Chaudhuri, R.2    Bonifacino, J.S.3
  • 10
    • 44649139364 scopus 로고    scopus 로고
    • HIV-1 accessory proteins-ensuring viral survival in a hostile environment
    • Malim MH, Emerman M (2008) HIV-1 accessory proteins-ensuring viral survival in a hostile environment. Cell Host Microbe 3: 388-398.
    • (2008) Cell Host Microbe , vol.3 , pp. 388-398
    • Malim, M.H.1    Emerman, M.2
  • 11
    • 0028180868 scopus 로고
    • Nef induces CD4 endocytosis: Requirement for a critical dileucine motif in the membraneproximal CD4 cytoplasmic domain
    • Aiken C, Konner J, Landau NR, Lenburg ME, Trono D (1994) Nef induces CD4 endocytosis: requirement for a critical dileucine motif in the membraneproximal CD4 cytoplasmic domain. Cell 76: 853-864.
    • (1994) Cell , vol.76 , pp. 853-864
    • Aiken, C.1    Konner, J.2    Landau, N.R.3    Lenburg, M.E.4    Trono, D.5
  • 12
    • 0028200761 scopus 로고
    • Human immunodeficiency virus type 1 Nef-induced down-modulation of CD4 is due to rapid internalization and degradation of surface CD4
    • Rhee SS, Marsh JW (1994) Human immunodeficiency virus type 1 Nef-induced down-modulation of CD4 is due to rapid internalization and degradation of surface CD4. J Virol 68: 5156-5163.
    • (1994) J Virol , vol.68 , pp. 5156-5163
    • Rhee, S.S.1    Marsh, J.W.2
  • 13
    • 34247129671 scopus 로고    scopus 로고
    • Downregulation of CD4 by human immunodeficiency virus type 1 Nef is dependent on clathrin and involves direct interaction of Nef with the AP2 clathrin adaptor
    • Chaudhuri R, Lindwasser OW, Smith WJ, Hurley JH, Bonifacino JS (2007) Downregulation of CD4 by human immunodeficiency virus type 1 Nef is dependent on clathrin and involves direct interaction of Nef with the AP2 clathrin adaptor. J Virol 81: 3877-3890.
    • (2007) J Virol , vol.81 , pp. 3877-3890
    • Chaudhuri, R.1    Lindwasser, O.W.2    Smith, W.J.3    Hurley, J.H.4    Bonifacino, J.S.5
  • 14
    • 67449092266 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef protein targets CD4 to the multivesicular body pathway
    • daSilva LL, Sougrat R, Burgos PV, Janvier K, Mattera R, et al. (2009) Human immunodeficiency virus type 1 Nef protein targets CD4 to the multivesicular body pathway. J Virol 83: 6578-6590.
    • (2009) J Virol , vol.83 , pp. 6578-6590
    • da Silva, L.L.1    Sougrat, R.2    Burgos, P.V.3    Janvier, K.4    Mattera, R.5
  • 15
    • 67349166158 scopus 로고    scopus 로고
    • Is the high virulence of HIV-1 an unfortunate coincidence of primate lentiviral evolution?
    • Kirchhoff F (2009) Is the high virulence of HIV-1 an unfortunate coincidence of primate lentiviral evolution? Nat Rev Microbiol 7: 467-476.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 467-476
    • Kirchhoff, F.1
  • 16
    • 0026452726 scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein induces rapid degradation of CD4
    • Willey RL, Maldarelli F, Martin MA, Strebel K (1992) Human immunodeficiency virus type 1 Vpu protein induces rapid degradation of CD4. J Virol 66: 7193-7200.
    • (1992) J Virol , vol.66 , pp. 7193-7200
    • Willey, R.L.1    Maldarelli, F.2    Martin, M.A.3    Strebel, K.4
  • 17
    • 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, Anton LC, Bacik I, Cox JH, Bour S, et al. (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.
    • (1998) J Virol , vol.72 , pp. 2280-2288
    • Schubert, U.1    Anton, L.C.2    Bacik, I.3    Cox, J.H.4    Bour, S.5
  • 18
    • 0029793620 scopus 로고    scopus 로고
    • CD4 down-modulation during infection of human T cells with human immunodeficiency virus type 1 involves independent activities of vpu, env, and nef
    • Chen BK, Gandhi RT, Baltimore D (1996) CD4 down-modulation during infection of human T cells with human immunodeficiency virus type 1 involves independent activities of vpu, env, and nef. J Virol 70: 6044-6053.
    • (1996) J Virol , vol.70 , pp. 6044-6053
    • Chen, B.K.1    Gandhi, R.T.2    Baltimore, D.3
  • 19
    • 33746799703 scopus 로고    scopus 로고
    • Contribution of Vpu, Env, and Nef to CD4 down-modulation and resistance of human immunodeficiency virus type 1-infected T cells to superinfection
    • Wildum S, Schindler M, Munch J, Kirchhoff F (2006) Contribution of Vpu, Env, and Nef to CD4 down-modulation and resistance of human immunodeficiency virus type 1-infected T cells to superinfection. J Virol 80: 8047-8059.
    • (2006) J Virol , vol.80 , pp. 8047-8059
    • Wildum, S.1    Schindler, M.2    Munch, J.3    Kirchhoff, F.4
  • 20
    • 0028816432 scopus 로고
    • The human immunodeficiency virus type 1 Vpu protein specifically binds to the cytoplasmic domain of CD4: Implications for the mechanism of degradation
    • Bour S, Schubert U, Strebel K (1995) The human immunodeficiency virus type 1 Vpu protein specifically binds to the cytoplasmic domain of CD4: implications for the mechanism of degradation. J Virol 69: 1510-1520.
    • (1995) J Virol , vol.69 , pp. 1510-1520
    • Bour, S.1    Schubert, U.2    Strebel, K.3
  • 21
    • 0032012456 scopus 로고    scopus 로고
    • A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif
    • Margottin F, Bour SP, Durand H, Selig L, Benichou S, et al. (1998) A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif. Mol Cell 1: 565-574.
    • (1998) Mol Cell , vol.1 , pp. 565-574
    • Margottin, F.1    Bour, S.P.2    Durand, H.3    Selig, L.4    Benichou, S.5
  • 22
    • 33846510877 scopus 로고    scopus 로고
    • Silencing of both beta-TrCP1 and HOS (beta-TrCP2) is required to suppress human immunodeficiency virus type 1 Vpu-mediated CD4 down-modulation
    • Butticaz C, Michielin O, Wyniger J, Telenti A, Rothenberger S (2007) Silencing of both beta-TrCP1 and HOS (beta-TrCP2) is required to suppress human immunodeficiency virus type 1 Vpu-mediated CD4 down-modulation. J Virol 81: 1502-1505.
    • (2007) J Virol , vol.81 , pp. 1502-1505
    • Butticaz, C.1    Michielin, O.2    Wyniger, J.3    Telenti, A.4    Rothenberger, S.5
  • 23
    • 1942534656 scopus 로고    scopus 로고
    • Vpu-mediated degradation of CD4 reconstituted in yeast reveals mechanistic differences to cellular ER-associated protein degradation
    • Meusser B, Sommer T (2004) Vpu-mediated degradation of CD4 reconstituted in yeast reveals mechanistic differences to cellular ER-associated protein degradation. Mol Cell 14: 247-258.
    • (2004) Mol Cell , vol.14 , pp. 247-258
    • Meusser, B.1    Sommer, T.2
  • 24
    • 37749032764 scopus 로고    scopus 로고
    • Requirements for the selective degradation of CD4 receptor molecules by the human immunodeficiency virus type 1 Vpu protein in the endoplasmic reticulum
    • Binette J, Dube M, Mercier J, Halawani D, Latterich M, et al. (2007) Requirements for the selective degradation of CD4 receptor molecules by the human immunodeficiency virus type 1 Vpu protein in the endoplasmic reticulum. Retrovirology 4: 75.
    • (2007) Retrovirology , vol.4 , pp. 75
    • Binette, J.1    Dube, M.2    Mercier, J.3    Halawani, D.4    Latterich, M.5
  • 25
    • 0028349047 scopus 로고
    • Differential activities of the human immunodeficiency virus type 1-encoded Vpu protein are regulated by phosphorylation and occur in different cellular compartments
    • Schubert U, Strebel K (1994) Differential activities of the human immunodeficiency virus type 1-encoded Vpu protein are regulated by phosphorylation and occur in different cellular compartments. J Virol 68: 2260-2271.
    • (1994) J Virol , vol.68 , pp. 2260-2271
    • Schubert, U.1    Strebel, K.2
  • 26
    • 67349113489 scopus 로고    scopus 로고
    • Ubiquitin ligase adaptors: Regulators of ubiquitylation and endocytosis of plasma membrane proteins
    • Leon S, Haguenauer-Tsapis R (2009) Ubiquitin ligase adaptors: regulators of ubiquitylation and endocytosis of plasma membrane proteins. Exp Cell Res 315: 1574-1583.
    • (2009) Exp Cell Res , vol.315 , pp. 1574-1583
    • Leon, S.1    Haguenauer-Tsapis, R.2
  • 28
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: Endoplasmic reticulumassociated degradation
    • Vembar SS, Brodsky JL (2008) One step at a time: endoplasmic reticulumassociated 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
  • 29
    • 0036270698 scopus 로고    scopus 로고
    • Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
    • Tsai B, Ye Y, Rapoport TA (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
  • 30
    • 0033083158 scopus 로고    scopus 로고
    • Signal-induced ubiquitination of IkappaBalpha by the F-box protein Slimb/beta-TrCP
    • Spencer E, Jiang J, Chen ZJ (1999) Signal-induced ubiquitination of IkappaBalpha by the F-box protein Slimb/beta-TrCP. Genes Dev 13: 284-294.
    • (1999) Genes Dev , vol.13 , pp. 284-294
    • Spencer, E.1    Jiang, J.2    Chen, Z.J.3
  • 31
    • 0033611567 scopus 로고    scopus 로고
    • The human F box protein beta-Trcp associates with the Cul1/Skp1 complex and regulates the stability of betacatenin
    • Latres E, Chiaur DS, Pagano M (1999) The human F box protein beta-Trcp associates with the Cul1/Skp1 complex and regulates the stability of betacatenin. Oncogene 18: 849-854.
    • (1999) Oncogene , vol.18 , pp. 849-854
    • Latres, E.1    Chiaur, D.S.2    Pagano, M.3
  • 32
    • 9144239817 scopus 로고    scopus 로고
    • Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum
    • Kikkert M, Doolman R, Dai M, Avner R, Hassink G, et al. (2004) Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum. J Biol Chem 279: 3525-3534.
    • (2004) J Biol Chem , vol.279 , pp. 3525-3534
    • Kikkert, M.1    Doolman, R.2    Dai, M.3    Avner, R.4    Hassink, G.5
  • 33
    • 26244431960 scopus 로고    scopus 로고
    • Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane
    • Lilley BN, Ploegh HL (2005) Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane. Proc Natl Acad Sci U S A 102: 14296-14301.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 14296-14301
    • Lilley, B.N.1    Ploegh, H.L.2
  • 34
    • 20544440605 scopus 로고    scopus 로고
    • TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum
    • Hassink G, Kikkert M, van Voorden S, Lee SJ, Spaapen R, et al. (2005) TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum. Biochem J 388: 647-655.
    • (2005) Biochem J , vol.388 , pp. 647-655
    • Hassink, G.1    Kikkert, M.2    van Voorden, S.3    Lee, S.J.4    Spaapen, R.5
  • 35
    • 0035807839 scopus 로고    scopus 로고
    • The tumor autocrine motility factor receptor, gp78, is an ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum
    • Fang S, Ferrone M, Yang C, Jensen JP, Tiwari S, et al. (2001) The tumor autocrine motility factor receptor, gp78, is an ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum. Proc Natl Acad Sci U S A 98: 14422-14427.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14422-14427
    • Fang, S.1    Ferrone, M.2    Yang, C.3    Jensen, J.P.4    Tiwari, S.5
  • 36
    • 44949249968 scopus 로고    scopus 로고
    • Gp78 cooperates with RMA1 in endoplasmic reticulum-associated degradation of CFTRDeltaF508
    • Morito D, Hirao K, Oda Y, Hosokawa N, Tokunaga F, et al. (2008) Gp78 cooperates with RMA1 in endoplasmic reticulum-associated degradation of CFTRDeltaF508. Mol Biol Cell 19: 1328-1336.
    • (2008) Mol Biol Cell , vol.19 , pp. 1328-1336
    • Morito, D.1    Hirao, K.2    Oda, Y.3    Hosokawa, N.4    Tokunaga, F.5
  • 37
    • 0036173013 scopus 로고    scopus 로고
    • Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48
    • Jarosch E, Taxis C, Volkwein C, Bordallo J, Finley D, et al. (2002) Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. Nat Cell Biol 4: 134-139.
    • (2002) Nat Cell Biol , vol.4 , pp. 134-139
    • Jarosch, E.1    Taxis, C.2    Volkwein, C.3    Bordallo, J.4    Finley, D.5
  • 38
    • 0036136901 scopus 로고    scopus 로고
    • AAAATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation
    • Rabinovich E, Kerem A, Frohlich KU, Diamant N, Bar-Nun S (2002) AAAATPase 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
  • 39
    • 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 HH, Rapoport TA (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
  • 40
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye Y, Meyer HH, Rapoport TA (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
  • 41
    • 1342343136 scopus 로고    scopus 로고
    • Codon optimization of the HIV-1 vpu and vif genes stabilizes their mRNA and allows for highly efficient Rev-independent expression
    • Nguyen KL, llano M, Akari H, Miyagi E, Poeschla EM, et al. (2004) Codon optimization of the HIV-1 vpu and vif genes stabilizes their mRNA and allows for highly efficient Rev-independent expression. Virology 319: 163-175.
    • (2004) Virology , vol.319 , pp. 163-175
    • Nguyen, K.L.1    Llano, M.2    Akari, H.3    Miyagi, E.4    Poeschla, E.M.5
  • 42
    • 0026508087 scopus 로고
    • Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum
    • Braakman I, Helenius J, Helenius A (1992) Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum. Nature 356: 260-262.
    • (1992) Nature , vol.356 , pp. 260-262
    • Braakman, I.1    Helenius, J.2    Helenius, A.3
  • 43
    • 0034658270 scopus 로고    scopus 로고
    • A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways
    • Meyer HH, Shorter JG, Seemann J, Pappin D, Warren G (2000) A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways. Embo J 19: 2181-2192.
    • (2000) Embo J , vol.19 , pp. 2181-2192
    • Meyer, H.H.1    Shorter, J.G.2    Seemann, J.3    Pappin, D.4    Warren, G.5
  • 44
    • 9644255751 scopus 로고    scopus 로고
    • The AAA ATPase p97/VCP interacts with its alternative co-factors, Ufd1-Npl4 and p47, through a common bipartite binding mechanism
    • Bruderer RM, Brasseur C, Meyer HH (2004) The AAA ATPase p97/VCP interacts with its alternative co-factors, Ufd1-Npl4 and p47, through a common bipartite binding mechanism. J Biol Chem 279: 49609-49616.
    • (2004) J Biol Chem , vol.279 , pp. 49609-49616
    • Bruderer, R.M.1    Brasseur, C.2    Meyer, H.H.3
  • 45
    • 0035195012 scopus 로고    scopus 로고
    • Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly
    • Hetzer M, Meyer HH, Walther TC, Bilbao-Cortes D, Warren G, et al. (2001) Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly. Nat Cell Biol 3: 1086-1091.
    • (2001) Nat Cell Biol , vol.3 , pp. 1086-1091
    • Hetzer, M.1    Meyer, H.H.2    Walther, T.C.3    Bilbao-Cortes, D.4    Warren, G.5
  • 46
    • 67349231313 scopus 로고    scopus 로고
    • Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains
    • Komander D, Reyes-Turcu F, Licchesi JD, Odenwaelder P, Wilkinson KD, et al. (2009) Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains. EMBO Rep 10: 466-473.
    • (2009) EMBO Rep , vol.10 , pp. 466-473
    • Komander, D.1    Reyes-Turcu, F.2    Licchesi, J.D.3    Odenwaelder, P.4    Wilkinson, K.D.5
  • 47
    • 33747371085 scopus 로고    scopus 로고
    • Destabilization of the VCP-Ufd1-Npl4 complex is associated with decreased levels of ERAD substrates
    • Nowis D, McConnell E, Wojcik C (2006) Destabilization of the VCP-Ufd1-Npl4 complex is associated with decreased levels of ERAD substrates. Exp Cell Res 312: 2921-2932.
    • (2006) Exp Cell Res , vol.312 , pp. 2921-2932
    • Nowis, D.1    McConnell, E.2    Wojcik, C.3
  • 48
    • 0028030526 scopus 로고
    • Stimulation of heterologous protein degradation by the Vpu protein of HIV-1 requires the transmembrane and cytoplasmic domains of CD4
    • Buonocore L, Turi TG, Crise B, Rose JK (1994) Stimulation of heterologous protein degradation by the Vpu protein of HIV-1 requires the transmembrane and cytoplasmic domains of CD4. Virology 204: 482-486.
    • (1994) Virology , vol.204 , pp. 482-486
    • Buonocore, L.1    Turi, T.G.2    Crise, B.3    Rose, J.K.4
  • 49
    • 0032506276 scopus 로고    scopus 로고
    • Structural and functional analysis of the membrane-spanning domain of the human immunodeficiency virus type 1 Vpu protein
    • Tiganos E, Friborg J, Allain B, Daniel NG, Yao XJ, et al. (1998) Structural and functional analysis of the membrane-spanning domain of the human immunodeficiency virus type 1 Vpu protein. Virology 251: 96-107.
    • (1998) Virology , vol.251 , pp. 96-107
    • Tiganos, E.1    Friborg, J.2    Allain, B.3    Daniel, N.G.4    Yao, X.J.5
  • 50
    • 0030812940 scopus 로고    scopus 로고
    • A di-acidic signal required for selective export from the endoplasmic reticulum
    • Nishimura N, Balch WE (1997) A di-acidic signal required for selective export from the endoplasmic reticulum. Science 277: 556-558.
    • (1997) Science , vol.277 , pp. 556-558
    • Nishimura, N.1    Balch, W.E.2
  • 51
    • 44449107477 scopus 로고    scopus 로고
    • Palmitoylation and ubiquitination regulate exit of the Wnt signaling protein LRP6 from the endoplasmic reticulum
    • Abrami L, Kunz B, Iacovache I, van der Goot FG (2008) Palmitoylation and ubiquitination regulate exit of the Wnt signaling protein LRP6 from the endoplasmic reticulum. Proc Natl Acad Sci U S A 105: 5384-5389.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 5384-5389
    • Abrami, L.1    Kunz, B.2    Iacovache, I.3    van der Goot, F.G.4
  • 52
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the ER
    • Lilley BN, Ploegh HL (2004) A membrane protein required for dislocation of misfolded proteins from the ER. Nature 429: 834-840.
    • (2004) Nature , vol.429 , pp. 834-840
    • Lilley, B.N.1    Ploegh, H.L.2
  • 53
    • 33745207334 scopus 로고    scopus 로고
    • Signal peptide peptidase is required for dislocation from the endoplasmic reticulum
    • Loureiro J, Lilley BN, Spooner E, Noriega V, Tortorella D, et al. (2006) Signal peptide peptidase is required for dislocation from the endoplasmic reticulum. Nature 441: 894-897.
    • (2006) Nature , vol.441 , pp. 894-897
    • Loureiro, J.1    Lilley, B.N.2    Spooner, E.3    Noriega, V.4    Tortorella, D.5
  • 54
    • 33646846643 scopus 로고    scopus 로고
    • The viral E3 ubiquitin ligase mK3 uses the Derlin/p97 endoplasmic reticulum-associated degradation pathway to mediate down-regulation of major histocompatibility complex class I proteins
    • Wang X, Ye Y, Lencer W, Hansen TH (2006) The viral E3 ubiquitin ligase mK3 uses the Derlin/p97 endoplasmic reticulum-associated degradation pathway to mediate down-regulation of major histocompatibility complex class I proteins. J Biol Chem 281: 8636-8644.
    • (2006) J Biol Chem , vol.281 , pp. 8636-8644
    • Wang, X.1    Ye, Y.2    Lencer, W.3    Hansen, T.H.4
  • 55
    • 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 RA, Chua WJ, Lybarger L, Wiertz EJ, et al. (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
  • 56
    • 38549095979 scopus 로고    scopus 로고
    • Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu
    • Neil SJ, Zang T, Bieniasz PD (2008) Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu. Nature 451: 425-430.
    • (2008) Nature , vol.451 , pp. 425-430
    • Neil, S.J.1    Zang, T.2    Bieniasz, P.D.3
  • 57
    • 41849116366 scopus 로고    scopus 로고
    • The interferon-induced protein BST-2 restricts HIV-1 release and is downregulated from the cell surface by the viral Vpu protein
    • Van Damme N, Goff D, Katsura C, Jorgenson RL, Mitchell R, et al. (2008) The interferon-induced protein BST-2 restricts HIV-1 release and is downregulated from the cell surface by the viral Vpu protein. Cell Host Microbe 3: 245-252.
    • (2008) Cell Host Microbe , vol.3 , pp. 245-252
    • van Damme, N.1    Goff, D.2    Katsura, C.3    Jorgenson, R.L.4    Mitchell, R.5
  • 58
    • 0022495870 scopus 로고
    • Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone
    • Adachi A, Gendelman HE, Koenig S, Folks T, Willey R, et al. (1986) Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone. J Virol 59: 284-291.
    • (1986) J Virol , vol.59 , pp. 284-291
    • Adachi, A.1    Gendelman, H.E.2    Koenig, S.3    Folks, T.4    Willey, R.5
  • 59
    • 26444621357 scopus 로고    scopus 로고
    • Inaugural Article: Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane
    • Ye Y, Shibata Y, Kikkert M, van Voorden S, Wiertz E, et al. (2005) Inaugural Article: Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane. Proc Natl Acad Sci U S A 102: 14132-14138.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 14132-14138
    • Ye, Y.1    Shibata, Y.2    Kikkert, M.3    van Voorden, S.4    Wiertz, E.5
  • 60
    • 33845917801 scopus 로고    scopus 로고
    • The role of a novel p97/valosincontaining protein-interacting motif of gp78 in endoplasmic reticulumassociated degradation
    • Ballar P, Shen Y, Yang H, Fang S (2006) The role of a novel p97/valosincontaining protein-interacting motif of gp78 in endoplasmic reticulumassociated degradation. J Biol Chem 281: 35359-35368.
    • (2006) J Biol Chem , vol.281 , pp. 35359-35368
    • Ballar, P.1    Shen, Y.2    Yang, H.3    Fang, S.4
  • 62
    • 0027209705 scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein is an oligomeric type I integral membrane protein
    • Maldarelli F, Chen MY, Willey RL, Strebel K (1993) Human immunodeficiency virus type 1 Vpu protein is an oligomeric type I integral membrane protein. J Virol 67: 5056-5061.
    • (1993) J Virol , vol.67 , pp. 5056-5061
    • Maldarelli, F.1    Chen, M.Y.2    Willey, R.L.3    Strebel, K.4
  • 65
    • 0035947775 scopus 로고    scopus 로고
    • Stonin 2: An adaptor-like protein that interacts with components of the endocytic machinery
    • Martina JA, Bonangelino CJ, Aguilar RC, Bonifacino JS (2001) Stonin 2: an adaptor-like protein that interacts with components of the endocytic machinery. J Cell Biol 153: 1111-1120.
    • (2001) J Cell Biol , vol.153 , pp. 1111-1120
    • Martina, J.A.1    Bonangelino, C.J.2    Aguilar, R.C.3    Bonifacino, J.S.4
  • 66
    • 34548482956 scopus 로고    scopus 로고
    • The trans-Golgi network accessory protein p56 promotes long-range movement of GGA/clathrin-containing transport carriers and lysosomal enzyme sorting
    • Mardones GA, Burgos PV, Brooks DA, Parkinson-Lawrence E, Mattera R, et al. (2007) The trans-Golgi network accessory protein p56 promotes long-range movement of GGA/clathrin-containing transport carriers and lysosomal enzyme sorting. Mol Biol Cell 18: 3486-3501.
    • (2007) Mol Biol Cell , vol.18 , pp. 3486-3501
    • Mardones, G.A.1    Burgos, P.V.2    Brooks, D.A.3    Parkinson-Lawrence, E.4    Mattera, R.5
  • 67
    • 54249087710 scopus 로고    scopus 로고
    • Retrotranslocation of prion proteins from the endoplasmic reticulum by preventing GPI signal transamidation
    • Ashok A, Hegde RS (2008) Retrotranslocation of prion proteins from the endoplasmic reticulum by preventing GPI signal transamidation. Mol Biol Cell 19: 3463-3476.
    • (2008) Mol Biol Cell , vol.19 , pp. 3463-3476
    • Ashok, A.1    Hegde, R.S.2


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