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Volumn 174, Issue 4, 2009, Pages 1415-1425

COP9-associated CSN5 regulates exosomal protein deubiquitination and sorting

Author keywords

[No Author keywords available]

Indexed keywords

COP9 SIGNALOSOME; HEAT SHOCK PROTEIN 70; SMALL INTERFERING RNA; COPS5 PROTEIN, HUMAN; GAG PROTEIN; HIV GAG P24 PROTEIN (29 60); HIV GAG P24 PROTEIN (29-60); MULTIPROTEIN COMPLEX; PEPTIDE FRAGMENT; PEPTIDE HYDROLASE; PROTEIN; SIGNAL PEPTIDE;

EID: 65349196684     PISSN: 00029440     EISSN: 15252191     Source Type: Journal    
DOI: 10.2353/ajpath.2009.080861     Document Type: Article
Times cited : (54)

References (62)
  • 1
    • 33751199883 scopus 로고    scopus 로고
    • Exosomes: From biogenesis and secretion to biological function
    • Keller S, Sanderson MP, Stoeck A, Altevogt P: Exosomes: from biogenesis and secretion to biological function. Immunol Lett 2006, 107:102-108
    • (2006) Immunol Lett , vol.107 , pp. 102-108
    • Keller, S.1    Sanderson, M.P.2    Stoeck, A.3    Altevogt, P.4
  • 2
    • 43149120419 scopus 로고    scopus 로고
    • Exosome function: From tumor immunology to pathogen biology
    • Schorey JS, Bhatnagar S: Exosome function: from tumor immunology to pathogen biology. Traffic 2008, 9:871-881
    • (2008) Traffic , vol.9 , pp. 871-881
    • Schorey, J.S.1    Bhatnagar, S.2
  • 4
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex. ESCRT-I
    • Katzmann DJ, Babst M, Emr SD: Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex. ESCRT-I, Cell 2001, 106:145-155
    • (2001) Cell , vol.106 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 5
    • 0347993084 scopus 로고    scopus 로고
    • Evidence that HIV budding in primary macrophages occurs through the exosome release pathway
    • Nguyen DG, Booth A, Gould SJ, Hildreth JE: Evidence that HIV budding in primary macrophages occurs through the exosome release pathway. J Biol Chem 2003, 278:52347-52354
    • (2003) J Biol Chem , vol.278 , pp. 52347-52354
    • Nguyen, D.G.1    Booth, A.2    Gould, S.J.3    Hildreth, J.E.4
  • 6
    • 34250325547 scopus 로고    scopus 로고
    • Higher-order oligomerization targets plasma membrane proteins and HIV gag to exosomes
    • Fang Y, Wu N, Gan X, Yan W, Morrell JC, Gould SJ: Higher-order oligomerization targets plasma membrane proteins and HIV gag to exosomes. PLoS Biol 2007, 5:e158
    • (2007) PLoS Biol , vol.5
    • Fang, Y.1    Wu, N.2    Gan, X.3    Yan, W.4    Morrell, J.C.5    Gould, S.J.6
  • 7
    • 33846998968 scopus 로고    scopus 로고
    • The potential of retroviral vectors to cotransfer human endogenous retroviruses (HERVs) from human packaging cell lines
    • Zeilfelder U, Frank O, Sparacio S, Schon U, Bosch V, Seifarth W, Leib-Mosch C: The potential of retroviral vectors to cotransfer human endogenous retroviruses (HERVs) from human packaging cell lines. Gene 2007, 390:175-179
    • (2007) Gene , vol.390 , pp. 175-179
    • Zeilfelder, U.1    Frank, O.2    Sparacio, S.3    Schon, U.4    Bosch, V.5    Seifarth, W.6    Leib-Mosch, C.7
  • 8
    • 0036696804 scopus 로고    scopus 로고
    • Escrt- III: An endosome-associated heterooligomeric protein complex required for mvb sorting
    • Babst M, Katzmann DJ, Estepa-Sabal EJ, Meerloo T, Emr SD: Escrt- III: an endosome-associated heterooligomeric protein complex required for mvb sorting. Dev Cell 2002, 3:271-282
    • (2002) Dev Cell , vol.3 , pp. 271-282
    • Babst, M.1    Katzmann, D.J.2    Estepa-Sabal, E.J.3    Meerloo, T.4    Emr, S.D.5
  • 11
    • 18944391961 scopus 로고    scopus 로고
    • CSN5/Jab1 is involved in ligand- dependent degradation of estrogen receptor {alpha} by the protea- some
    • Callige M, Kieffer I, Richard-Foy H: CSN5/Jab1 is involved in ligand- dependent degradation of estrogen receptor {alpha} by the protea- some. Mol Cell Biol 2005, 25:4349-4358
    • (2005) Mol Cell Biol , vol.25 , pp. 4349-4358
    • Callige, M.1    Kieffer, I.2    Richard-Foy, H.3
  • 12
    • 2542456590 scopus 로고    scopus 로고
    • JAB1 enhances HAND2 transcriptional activity by regulating HAND2 DNA binding
    • Dai YS, Hao J, Bonin C, Morikawa Y, Cserjesi P: JAB1 enhances HAND2 transcriptional activity by regulating HAND2 DNA binding. J Neurosci Res 2004, 76:613-622
    • (2004) J Neurosci Res , vol.76 , pp. 613-622
    • Dai, Y.S.1    Hao, J.2    Bonin, C.3    Morikawa, Y.4    Cserjesi, P.5
  • 13
    • 0036848655 scopus 로고    scopus 로고
    • CSN5/Jab1 mutations affect axis formation in the Drosophila oocyte by activating a meiotic checkpoint
    • Doronkin S, Djagaeva I, Beckendorf SK: CSN5/Jab1 mutations affect axis formation in the Drosophila oocyte by activating a meiotic checkpoint. Development 2002, 129:5053-5064
    • (2002) Development , vol.129 , pp. 5053-5064
    • Doronkin, S.1    Djagaeva, I.2    Beckendorf, S.K.3
  • 14
    • 33846559388 scopus 로고    scopus 로고
    • COP9 signalosome subunit 5 (CSN5/Jab1) regulates the development of the Drosophila immune system: Effects on Cactus. Dorsal and hematopoiesis
    • Harari-Steinberg O, Cantera R, Denti S, Bianchi E, Oron E, Segal D, Chamovitz DA: COP9 signalosome subunit 5 (CSN5/Jab1) regulates the development of the Drosophila immune system: effects on Cactus. Dorsal and hematopoiesis, Genes Cells 2007, 12:183-195
    • (2007) Genes Cells , vol.12 , pp. 183-195
    • Harari-Steinberg, O.1    Cantera, R.2    Denti, S.3    Bianchi, E.4    Oron, E.5    Segal, D.6    Chamovitz, D.A.7
  • 16
    • 33646347134 scopus 로고    scopus 로고
    • Jab1, a novel pro- tease-activated receptor-2 (PAR-2)-interacting protein, is involved in PAR-2-induced activation of activator protein-1
    • Luo W, Wang Y, Hanck T, Stricker R, Reiser G: Jab1, a novel pro- tease-activated receptor-2 (PAR-2)-interacting protein, is involved in PAR-2-induced activation of activator protein-1. J Biol Chem 2006, 281:7927-7936
    • (2006) J Biol Chem , vol.281 , pp. 7927-7936
    • Luo, W.1    Wang, Y.2    Hanck, T.3    Stricker, R.4    Reiser, G.5
  • 17
    • 33745218066 scopus 로고    scopus 로고
    • Jab1 induces the cytoplasmic localization and degradation of p53 in coordination with Hdm2
    • Oh W, Lee EW, Sung YH, Yang MR, Ghim J, Lee HW, Song J: Jab1 induces the cytoplasmic localization and degradation of p53 in coordination with Hdm2. J Biol Chem 2006, 281:17457-17465
    • (2006) J Biol Chem , vol.281 , pp. 17457-17465
    • Oh, W.1    Lee, E.W.2    Sung, Y.H.3    Yang, M.R.4    Ghim, J.5    Lee, H.W.6    Song, J.7
  • 18
    • 11244272124 scopus 로고    scopus 로고
    • The Jab1/COP9 signalosome subcomplex is a downstream mediator of Bcr-Abl kinase activity and facilitates cell-cycle progression
    • Tomoda K, Kato JY, Tatsumi E, Takahashi T, Matsuo Y, Yoneda-Kato N: The Jab1/COP9 signalosome subcomplex is a downstream mediator of Bcr-Abl kinase activity and facilitates cell-cycle progression. Blood 2005, 105:775-783
    • (2005) Blood , vol.105 , pp. 775-783
    • Tomoda, K.1    Kato, J.Y.2    Tatsumi, E.3    Takahashi, T.4    Matsuo, Y.5    Yoneda-Kato, N.6
  • 21
    • 0031815994 scopus 로고    scopus 로고
    • The regulatory particle of the Saccharomyces cerevisiae proteasome
    • Glickman MH, Rubin DM, Fried VA, Finley D: The regulatory particle of the Saccharomyces cerevisiae proteasome. Mol Cell Biol 1998, 18:3149-3162
    • (1998) Mol Cell Biol , vol.18 , pp. 3149-3162
    • Glickman, M.H.1    Rubin, D.M.2    Fried, V.A.3    Finley, D.4
  • 22
    • 0037184947 scopus 로고    scopus 로고
    • Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde
    • Hu M, Li P, Li M, Li W, Yao T, Wu JW, Gu W, Cohen RE, Shi Y: Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde. Cell 2002, 111:1041-1054
    • (2002) Cell , vol.111 , pp. 1041-1054
    • Hu, M.1    Li, P.2    Li, M.3    Li, W.4    Yao, T.5    Wu, J.W.6    Gu, W.7    Cohen, R.E.8    Shi, Y.9
  • 24
    • 32044442093 scopus 로고    scopus 로고
    • Targeted silencing of Jab1/Csn5 in human cells downregulates SCF activity through reduction of F-box protein levels
    • Cope GA, Deshaies RJ: Targeted silencing of Jab1/Csn5 in human cells downregulates SCF activity through reduction of F-box protein levels, BMC Biochem 2006, 7:1-10
    • (2006) BMC Biochem , vol.7 , pp. 1-10
    • Cope, G.A.1    Deshaies, R.J.2
  • 26
    • 9644272422 scopus 로고    scopus 로고
    • The COP9 signalosome (CSN): An evolutionary conserved proteolysis regulator in eukaryotic development
    • Schwechheimer C: The COP9 signalosome (CSN): an evolutionary conserved proteolysis regulator in eukaryotic development. Biochim Biophys Acta 2004, 1695:45-54
    • (2004) Biochim Biophys Acta , vol.1695 , pp. 45-54
    • Schwechheimer, C.1
  • 28
    • 0029025180 scopus 로고
    • Deletion of thymidine kinase gene attenuates channel catfish herpesvirus while maintaining infectivity
    • Zhang HG, Hanson LA: Deletion of thymidine kinase gene attenuates channel catfish herpesvirus while maintaining infectivity, Virology 1995, 209:658-663
    • (1995) Virology , vol.209 , pp. 658-663
    • Zhang, H.G.1    Hanson, L.A.2
  • 29
    • 33644776551 scopus 로고    scopus 로고
    • Jab1 is a specificity factor for E2F1-induced apoptosis
    • Hallstrom TC, Nevins JR: Jab1 is a specificity factor for E2F1-induced apoptosis. Genes Dev 2006, 20:613-623
    • (2006) Genes Dev , vol.20 , pp. 613-623
    • Hallstrom, T.C.1    Nevins, J.R.2
  • 33
    • 0032567528 scopus 로고    scopus 로고
    • Crystal structure of the human ubiquitin-like protein NEDD8 and interactions with ubiquitin pathway enzymes
    • Whitby FG, Xia G, Pickart CM, Hill CP: Crystal structure of the human ubiquitin-like protein NEDD8 and interactions with ubiquitin pathway enzymes. J Biol Chem 1998, 273:34983-34991
    • (1998) J Biol Chem , vol.273 , pp. 34983-34991
    • Whitby, F.G.1    Xia, G.2    Pickart, C.M.3    Hill, C.P.4
  • 34
    • 33747375410 scopus 로고    scopus 로고
    • Interaction of AMSH with ESCRT- III and deubiquitination of endosomal cargo
    • Agromayor M, Martin-Serrano J: Interaction of AMSH with ESCRT- III and deubiquitination of endosomal cargo. J Biol Chem 2006, 281:23083-23091
    • (2006) J Biol Chem , vol.281 , pp. 23083-23091
    • Agromayor, M.1    Martin-Serrano, J.2
  • 35
    • 34548155408 scopus 로고    scopus 로고
    • Ubiquitination of human immunodeficiency virus type 1 Gag is highly dependent on Gag membrane association
    • Jager S, Gottwein E, Krausslich HG: Ubiquitination of human immunodeficiency virus type 1 Gag is highly dependent on Gag membrane association. J Virol 2007, 81:9193-9201
    • (2007) J Virol , vol.81 , pp. 9193-9201
    • Jager, S.1    Gottwein, E.2    Krausslich, H.G.3
  • 36
    • 14044259999 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in HIV replication: Potential targets for antiretroviral therapy
    • Klinger PP, Schubert U: The ubiquitin-proteasome system in HIV replication: potential targets for antiretroviral therapy. Expert Rev Anti Infect Ther 2005, 3:61-79
    • (2005) Expert Rev Anti Infect Ther , vol.3 , pp. 61-79
    • Klinger, P.P.1    Schubert, U.2
  • 37
    • 33749077805 scopus 로고    scopus 로고
    • The role of viral and cellular proteins in the budding of human immunodeficiency virus
    • Mazze FM, Degreve L: The role of viral and cellular proteins in the budding of human immunodeficiency virus. Acta Virol 2006, 50:75-85
    • (2006) Acta Virol , vol.50 , pp. 75-85
    • Mazze, F.M.1    Degreve, L.2
  • 38
    • 0034610238 scopus 로고    scopus 로고
    • Ott DE, Coren LV, Chertova EN, Gagliardi TD, Schubert U: Ubiquiti- nation of HIV-1 and MuLV Gag. Virology 2000, 278:111-121
    • Ott DE, Coren LV, Chertova EN, Gagliardi TD, Schubert U: Ubiquiti- nation of HIV-1 and MuLV Gag. Virology 2000, 278:111-121
  • 41
    • 0347634393 scopus 로고    scopus 로고
    • Cell-type-dependent targeting of human immunodeficiency virus type 1 assembly to the plasma membrane and the multivesicular body
    • Ono A, Freed EO: Cell-type-dependent targeting of human immunodeficiency virus type 1 assembly to the plasma membrane and the multivesicular body. J Virol 2004, 78:1552-1563
    • (2004) J Virol , vol.78 , pp. 1552-1563
    • Ono, A.1    Freed, E.O.2
  • 43
    • 0742288063 scopus 로고    scopus 로고
    • Multivesicular body sorting: Ubiquitin ligase Rsp5 is required for the modification and sorting of carboxypeptidase S
    • Katzmann DJ, Sarkar S, Chu T, Audhya A, Emr SD: Multivesicular body sorting: ubiquitin ligase Rsp5 is required for the modification and sorting of carboxypeptidase S. Mol Biol Cell 2004, 15:468-480
    • (2004) Mol Biol Cell , vol.15 , pp. 468-480
    • Katzmann, D.J.1    Sarkar, S.2    Chu, T.3    Audhya, A.4    Emr, S.D.5
  • 44
    • 33846807370 scopus 로고    scopus 로고
    • Characterization of multiple multivesicular body sorting determinants within Sna3: A role for the ubiquitin ligase Rsp5
    • Oestreich AJ, Aboian M, Lee J, Azmi I, Payne J, Issaka R, Davies BA, Katzmann DJ: Characterization of multiple multivesicular body sorting determinants within Sna3: a role for the ubiquitin ligase Rsp5. Mol Biol Cell 2007, 18:707-720
    • (2007) Mol Biol Cell , vol.18 , pp. 707-720
    • Oestreich, A.J.1    Aboian, M.2    Lee, J.3    Azmi, I.4    Payne, J.5    Issaka, R.6    Davies, B.A.7    Katzmann, D.J.8
  • 46
    • 0037509859 scopus 로고    scopus 로고
    • The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage
    • Groisman R, Polanowska J, Kuraoka I, Sawada J, Saijo M, Drapkin R, Kisselev AF, Tanaka K, Nakatani Y: The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. Cell 2003, 113:357-367
    • (2003) Cell , vol.113 , pp. 357-367
    • Groisman, R.1    Polanowska, J.2    Kuraoka, I.3    Sawada, J.4    Saijo, M.5    Drapkin, R.6    Kisselev, A.F.7    Tanaka, K.8    Nakatani, Y.9
  • 47
    • 0343012078 scopus 로고    scopus 로고
    • Ubiquitination of the human immunodeficiency virus type 1 env glycoprotein
    • Bultmann A, Eberle J, Haas J: Ubiquitination of the human immunodeficiency virus type 1 env glycoprotein. J Virol 2000, 74:5373-5376
    • (2000) J Virol , vol.74 , pp. 5373-5376
    • Bultmann, A.1    Eberle, J.2    Haas, J.3
  • 48
    • 0034087259 scopus 로고    scopus 로고
    • Immune response to an 18-kilodalton outer membrane antigen identifies lipoprotein 20 as a Helicobacter pylori vaccine candidate
    • Keenan J, Oliaro J, Domigan N, Potter H, Aitken G, Allardyce R, Roake J: Immune response to an 18-kilodalton outer membrane antigen identifies lipoprotein 20 as a Helicobacter pylori vaccine candidate. Infect Immun 2000, 68:3337-3343
    • (2000) Infect Immun , vol.68 , pp. 3337-3343
    • Keenan, J.1    Oliaro, J.2    Domigan, N.3    Potter, H.4    Aitken, G.5    Allardyce, R.6    Roake, J.7
  • 49
    • 0031900144 scopus 로고    scopus 로고
    • Ubiquitin is covalently attached to the p6Gag proteins of human immunodeficiency virus type 1 and simian immunodeficiency virus and to the p12Gag protein of Moloney murine leukemia virus
    • Ott DE, Coren LV, Copeland TD, Kane BP, Johnson DG, Sowder RC, 2nd, Yoshinaka Y, Oroszlan S, Arthur LO, Henderson LE: Ubiquitin is covalently attached to the p6Gag proteins of human immunodeficiency virus type 1 and simian immunodeficiency virus and to the p12Gag protein of Moloney murine leukemia virus. J Virol 1998, 72:2962-2968
    • (1998) J Virol , vol.72 , pp. 2962-2968
    • Ott, D.E.1    Coren, L.V.2    Copeland, T.D.3    Kane, B.P.4    Johnson, D.G.5    Sowder 2nd, R.C.6    Yoshinaka, Y.7    Oroszlan, S.8    Arthur, L.O.9    Henderson, L.E.10
  • 50
    • 48249136165 scopus 로고    scopus 로고
    • Overexpression of Jab1 in hepatocellular carcinoma and its inhibition by peroxisome proliferator-activated receptor{gamma} ligands in vitro and in vivo
    • Hsu MC, Huang CC, Chang HC, Hu TH, Hung WC: Overexpression of Jab1 in hepatocellular carcinoma and its inhibition by peroxisome proliferator-activated receptor{gamma} ligands in vitro and in vivo. Clin Cancer Res 2008, 14:4045-4052
    • (2008) Clin Cancer Res , vol.14 , pp. 4045-4052
    • Hsu, M.C.1    Huang, C.C.2    Chang, H.C.3    Hu, T.H.4    Hung, W.C.5
  • 52
    • 42549093548 scopus 로고    scopus 로고
    • Jab1 is overexpressed in human breast cancer and is a downstream target for HER-2/neu
    • Hsu MC, Chai CY, Hou MF, Chang HC, Chen WT, Hung WC: Jab1 is overexpressed in human breast cancer and is a downstream target for HER-2/neu. Mod Pathol 2008, 21:609-616
    • (2008) Mod Pathol , vol.21 , pp. 609-616
    • Hsu, M.C.1    Chai, C.Y.2    Hou, M.F.3    Chang, H.C.4    Chen, W.T.5    Hung, W.C.6
  • 53
    • 35948984762 scopus 로고    scopus 로고
    • HER-2/neu transcriptionally activates Jab1 expression via the AKT/beta-catenin pathway in breast cancer cells
    • Hsu MC, Chang HC, Hung WC: HER-2/neu transcriptionally activates Jab1 expression via the AKT/beta-catenin pathway in breast cancer cells. Endocr Relat Cancer 2007, 14:655-667
    • (2007) Endocr Relat Cancer , vol.14 , pp. 655-667
    • Hsu, M.C.1    Chang, H.C.2    Hung, W.C.3
  • 55
    • 33745309536 scopus 로고    scopus 로고
    • Overexpression of Jun activation domain- binding protein 1 in nonsmall cell lung cancer and its significance in p27 expression and clinical features
    • Osoegawa A, Yoshino I, Kometani T, Yamaguchi M, Kameyama T, Yohena T, Maehara Y: Overexpression of Jun activation domain- binding protein 1 in nonsmall cell lung cancer and its significance in p27 expression and clinical features. Cancer 2006, 107:154-161
    • (2006) Cancer , vol.107 , pp. 154-161
    • Osoegawa, A.1    Yoshino, I.2    Kometani, T.3    Yamaguchi, M.4    Kameyama, T.5    Yohena, T.6    Maehara, Y.7
  • 56
    • 33645824561 scopus 로고    scopus 로고
    • High expression of Jun activation domain-binding protein 1 (Jab1) is a strong prognostic marker in oral squamous cell carcinoma patients treated by UFT in combination with radiation
    • Harada K, Kawashima Y, Yoshida H, Sato M: High expression of Jun activation domain-binding protein 1 (Jab1) is a strong prognostic marker in oral squamous cell carcinoma patients treated by UFT in combination with radiation. Anticancer Res 2006, 26:1615-1619
    • (2006) Anticancer Res , vol.26 , pp. 1615-1619
    • Harada, K.1    Kawashima, Y.2    Yoshida, H.3    Sato, M.4
  • 57
    • 33746451838 scopus 로고    scopus 로고
    • Clinical significance of Skp2 expression, alone and combined with Jab1 and p27 in epithelial ovarian tumors
    • Sui L, Dong Y, Watanabe Y, Yamaguchi F, Sugimoto K, Tokuda M: Clinical significance of Skp2 expression, alone and combined with Jab1 and p27 in epithelial ovarian tumors. Oncol Rep 2006, 15:765-771
    • (2006) Oncol Rep , vol.15 , pp. 765-771
    • Sui, L.1    Dong, Y.2    Watanabe, Y.3    Yamaguchi, F.4    Sugimoto, K.5    Tokuda, M.6
  • 58
    • 11344272136 scopus 로고    scopus 로고
    • Prognostic significance of Jab1 expression in laryngeal squamous cell carcinomas
    • Dong Y, Sui L, Watanabe Y, Yamaguchi F, Hatano N, Tokuda M: Prognostic significance of Jab1 expression in laryngeal squamous cell carcinomas. Clin Cancer Res 2005, 11:259-266
    • (2005) Clin Cancer Res , vol.11 , pp. 259-266
    • Dong, Y.1    Sui, L.2    Watanabe, Y.3    Yamaguchi, F.4    Hatano, N.5    Tokuda, M.6
  • 61
    • 31144445302 scopus 로고    scopus 로고
    • Pregnancy-associated exo- somes and their modulation of T cell signaling
    • Taylor DD, Akyol S, Gercel-Taylor C: Pregnancy-associated exo- somes and their modulation of T cell signaling. J Immunol 2006, 176:1534-1542
    • (2006) J Immunol , vol.176 , pp. 1534-1542
    • Taylor, D.D.1    Akyol, S.2    Gercel-Taylor, C.3


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