메뉴 건너뛰기




Volumn 25, Issue 17, 2006, Pages 4120-4130

PRA1 promotes the intracellular trafficking and NF-κB signaling of EBV latent membrane protein 1

Author keywords

EBV; Intracellular trafficking; LMP1; NF B; PRA1

Indexed keywords

BREFELDIN A; CD40 LIGAND; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LATENT MEMBRANE PROTEIN 1; NOCODAZOLE; PROTEIN PRA1; RAB PROTEIN; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR; UNCLASSIFIED DRUG;

EID: 33748340652     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/sj.emboj.7601282     Document Type: Article
Times cited : (38)

References (46)
  • 2
    • 0032938469 scopus 로고    scopus 로고
    • Evidence of LMP1-TRAF3 interactions in glycosphingolipid-rich complexes of lymphoblastoid and nasopharyngeal carcinoma cells
    • Ardila-Osorio H, Clausse B, Mishal Z, Wiels J, Tursz T, Busson P (1999) Evidence of LMP1-TRAF3 interactions in glycosphingolipid-rich complexes of lymphoblastoid and nasopharyngeal carcinoma cells. Int J Cancer 81: 645-649
    • (1999) Int J Cancer , vol.81 , pp. 645-649
    • Ardila-Osorio, H.1    Clausse, B.2    Mishal, Z.3    Wiels, J.4    Tursz, T.5    Busson, P.6
  • 3
    • 0037683407 scopus 로고    scopus 로고
    • Signals for COPII-dependent export from the ER: What's the ticket out?
    • Barlowe C (2003) Signals for COPII-dependent export from the ER: what's the ticket out? Trends Cell Biol 13: 295-300
    • (2003) Trends Cell Biol , vol.13 , pp. 295-300
    • Barlowe, C.1
  • 5
    • 0842324801 scopus 로고    scopus 로고
    • The mechanisms of vesicle budding and fusion
    • Bonifacino JS, Glick BS (2004) The mechanisms of vesicle budding and fusion. Cell 116: 153-166
    • (2004) Cell , vol.116 , pp. 153-166
    • Bonifacino, J.S.1    Glick, B.S.2
  • 6
    • 0037134020 scopus 로고    scopus 로고
    • A system for stable expression of short interfering RNAs in mammalian cells
    • Brummelkamp TR, Bernards R, Agami R (2002) A system for stable expression of short interfering RNAs in mammalian cells. Science 296: 550-553
    • (2002) Science , vol.296 , pp. 550-553
    • Brummelkamp, T.R.1    Bernards, R.2    Agami, R.3
  • 7
    • 0033583815 scopus 로고    scopus 로고
    • Interaction cloning and characterization of the cDNA encoding the human prenylated rab acceptor (PRA1)
    • Bucci C, Chiariello M, Lattero D, Maiorano M, Bruni CB (1999) Interaction cloning and characterization of the cDNA encoding the human prenylated rab acceptor (PRA1). Biochem Biophys Res Commun 258: 657-662
    • (1999) Biochem Biophys Res Commun , vol.258 , pp. 657-662
    • Bucci, C.1    Chiariello, M.2    Lattero, D.3    Maiorano, M.4    Bruni, C.B.5
  • 8
    • 0037333399 scopus 로고    scopus 로고
    • Transmembrane domains 1 and 2 of the latent membrane protein 1 of Epstein-Barr virus contain a lipid raft targeting signal and play a critical role in cytostasis
    • Coffin III WF, Geiger TR, Martin JM (2003) Transmembrane domains 1 and 2 of the latent membrane protein 1 of Epstein-Barr virus contain a lipid raft targeting signal and play a critical role in cytostasis. J Virol 77: 3749-3758
    • (2003) J Virol , vol.77 , pp. 3749-3758
    • Coffin III, W.F.1    Geiger, T.R.2    Martin, J.M.3
  • 9
    • 0041315472 scopus 로고    scopus 로고
    • Reconstitution of sterol-regulated endoplasmic reticulum-to-Golgi transport of SREBP-2 in insect cells by co-expression of mammalian SCAP and Insigs
    • Dobrosotskaya IY, Goldstein JL, Brown MS, Rawson RB (2003) Reconstitution of sterol-regulated endoplasmic reticulum-to-Golgi transport of SREBP-2 in insect cells by co-expression of mammalian SCAP and Insigs. J Biol Chem 278: 35837-35843
    • (2003) J Biol Chem , vol.278 , pp. 35837-35843
    • Dobrosotskaya, I.Y.1    Goldstein, J.L.2    Brown, M.S.3    Rawson, R.B.4
  • 10
    • 0036223564 scopus 로고    scopus 로고
    • The oncogenic protein kinase Tpl-2/Cot contributes to Epstein-Barr virus-encoded latent infection membrane protein 1-induced NF-κB signaling downstream of TRAF2
    • Eliopoulos AG, Davies C, Blake SS, Murray P, Najafipour S, Tsichlis PN, Young LS (2002) The oncogenic protein kinase Tpl-2/Cot contributes to Epstein-Barr virus-encoded latent infection membrane protein 1-induced NF-κB signaling downstream of TRAF2. J Virol 76: 4567-4579
    • (2002) J Virol , vol.76 , pp. 4567-4579
    • Eliopoulos, A.G.1    Davies, C.2    Blake, S.S.3    Murray, P.4    Najafipour, S.5    Tsichlis, P.N.6    Young, L.S.7
  • 11
    • 0032510393 scopus 로고    scopus 로고
    • Epstein-Barr virus: LMP1 masquerades as an active receptor
    • Eliopoulos AG, Rickinson AB (1998) Epstein-Barr virus: LMP1 masquerades as an active receptor. Curr Biol 8: 196-198
    • (1998) Curr Biol , vol.8 , pp. 196-198
    • Eliopoulos, A.G.1    Rickinson, A.B.2
  • 12
    • 0035958898 scopus 로고    scopus 로고
    • Prenylated Rab acceptor protein is a receptor for prenylated small GTPases
    • Figueroa C, Taylor J, Vojtek AB (2001) Prenylated Rab acceptor protein is a receptor for prenylated small GTPases. J Biol Chem 276: 28219-28225
    • (2001) J Biol Chem , vol.276 , pp. 28219-28225
    • Figueroa, C.1    Taylor, J.2    Vojtek, A.B.3
  • 13
    • 0037813157 scopus 로고    scopus 로고
    • Localization of the Epstein-Barr virus protein LMP1 to exosomes
    • Flanagan J, Middeldorp J, Sculley T (2003) Localization of the Epstein-Barr virus protein LMP1 to exosomes. J Gen Virol 84: 1871-1879
    • (2003) J Gen Virol , vol.84 , pp. 1871-1879
    • Flanagan, J.1    Middeldorp, J.2    Sculley, T.3
  • 15
    • 0037184055 scopus 로고    scopus 로고
    • Disruption of Golgi morphology and trafficking in cells expressing mutant prenylated rab acceptor-1
    • Gougeon PY, Prosser DC, Da Silva LF, Ngsee JK (2002) Disruption of Golgi morphology and trafficking in cells expressing mutant prenylated rab acceptor-1. J Biol Chem 277: 36408-36414
    • (2002) J Biol Chem , vol.277 , pp. 36408-36414
    • Gougeon, P.Y.1    Prosser, D.C.2    Da Silva, L.F.3    Ngsee, J.K.4
  • 16
    • 0034493602 scopus 로고    scopus 로고
    • Dynamics of transitional endoplasmic reticulum sites in vertebrate cells
    • Hammond AT, Glick BS (2000) Dynamics of transitional endoplasmic reticulum sites in vertebrate cells. Mol Biol Cell 11: 3013-3030
    • (2000) Mol Biol Cell , vol.11 , pp. 3013-3030
    • Hammond, A.T.1    Glick, B.S.2
  • 17
    • 0034682501 scopus 로고    scopus 로고
    • Dissecting the role of the Golgi complex and lipid rafts in biosynthetic transport of cholesterol to the cell surface
    • Heino S, Lusa S, Somerharju P, Ehnholm C, Olkkonen VM, Ikonen E (2000) Dissecting the role of the Golgi complex and lipid rafts in biosynthetic transport of cholesterol to the cell surface. Proc Natl Acad Sci USA 97: 8375-8380
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8375-8380
    • Heino, S.1    Lusa, S.2    Somerharju, P.3    Ehnholm, C.4    Olkkonen, V.M.5    Ikonen, E.6
  • 18
    • 0035836746 scopus 로고    scopus 로고
    • Epstein-Barr virus latent-infection membrane proteins are palmitoylated and raft-associated: Protein 1 binds to the cytoskeleton through TNF receptor cytoplasmic factors
    • Higuchi M, Izumi KM, Kieff E (2001) Epstein-Barr virus latent-infection membrane proteins are palmitoylated and raft-associated: protein 1 binds to the cytoskeleton through TNF receptor cytoplasmic factors. Proc Natl Acad Sci USA 98: 4675-4680
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4675-4680
    • Higuchi, M.1    Izumi, K.M.2    Kieff, E.3
  • 20
    • 0032517767 scopus 로고    scopus 로고
    • Kinetic analysis of secretory protein traffic and characterization of Golgi to plasma membrane transport intermediates in living cells
    • Hirschberg K, Miller CM, Ellenberg J, Presley JF, Siggia ED, Phair RD, Lippincott-Schwartz J (1998) Kinetic analysis of secretory protein traffic and characterization of Golgi to plasma membrane transport intermediates in living cells. J Cell Biol 143: 1485-1503
    • (1998) J Cell Biol , vol.143 , pp. 1485-1503
    • Hirschberg, K.1    Miller, C.M.2    Ellenberg, J.3    Presley, J.F.4    Siggia, E.D.5    Phair, R.D.6    Lippincott-Schwartz, J.7
  • 21
    • 0034663173 scopus 로고    scopus 로고
    • Association of latent membrane protein 1 and matrix metalloproteinase 9 with metastasis in nasopharyngeal carcinoma
    • Horikawa T, Yoshizaki T, Sheen TS, Lee SY, Furukawa M (2000) Association of latent membrane protein 1 and matrix metalloproteinase 9 with metastasis in nasopharyngeal carcinoma. Cancer 89: 715-723
    • (2000) Cancer , vol.89 , pp. 715-723
    • Horikawa, T.1    Yoshizaki, T.2    Sheen, T.S.3    Lee, S.Y.4    Furukawa, M.5
  • 23
    • 0035423556 scopus 로고    scopus 로고
    • Roles of lipid rafts in membrane transport
    • Ikonen E (2001) Roles of lipid rafts in membrane transport. Curr Opin Cell Biol 13: 470-477
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 470-477
    • Ikonen, E.1
  • 24
    • 2942640590 scopus 로고    scopus 로고
    • Trafficking of Lyn through the Golgi caveolin involves the charged residues on alpha E and alpha I helices in the kinase domain
    • Kasahara K, Nakayama Y, Ikeda K, Fukushima Y, Matsuda D, Horimoto S, Yamaguchi N (2004) Trafficking of Lyn through the Golgi caveolin involves the charged residues on alpha E and alpha I helices in the kinase domain. J Cell Biol 165: 641-652
    • (2004) J Cell Biol , vol.165 , pp. 641-652
    • Kasahara, K.1    Nakayama, Y.2    Ikeda, K.3    Fukushima, Y.4    Matsuda, D.5    Horimoto, S.6    Yamaguchi, N.7
  • 25
    • 0035355202 scopus 로고    scopus 로고
    • CD40 and LMP-1 both signal from lipid rafts but LMP-1 assembles a distinct, more efficient signaling complex
    • Kaykas A, Worringer K, Sugden B (2001) CD40 and LMP-1 both signal from lipid rafts but LMP-1 assembles a distinct, more efficient signaling complex. EMBO J 20: 2641-2654
    • (2001) EMBO J , vol.20 , pp. 2641-2654
    • Kaykas, A.1    Worringer, K.2    Sugden, B.3
  • 26
    • 0032536860 scopus 로고    scopus 로고
    • Epstein-Barr virus-mediated B-cell proliferation is dependent upon latent membrane protein 1, which simulates an activated CD40 receptor
    • Kilger E, Kieser A, Baumann M, Hammerschmidt W (1998) Epstein-Barr virus-mediated B-cell proliferation is dependent upon latent membrane protein 1, which simulates an activated CD40 receptor. EMBO J 17: 1700-1709
    • (1998) EMBO J , vol.17 , pp. 1700-1709
    • Kilger, E.1    Kieser, A.2    Baumann, M.3    Hammerschmidt, W.4
  • 27
    • 0026561901 scopus 로고
    • Brefeldin A: Insights into the control of membrane traffic and organelle structure
    • Klausner RD, Donaldson JG, Lippincott-Schwartz J (1992) Brefeldin A: insights into the control of membrane traffic and organelle structure. J Cell Biol 116: 1071-1080
    • (1992) J Cell Biol , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 28
    • 0037938602 scopus 로고    scopus 로고
    • LMP1, a viral relative of the TNF receptor family, signals principally from intracellular compartments
    • Lam N, Sugden B (2003) LMP1, a viral relative of the TNF receptor family, signals principally from intracellular compartments. EMBO J 22: 3027-3038
    • (2003) EMBO J , vol.22 , pp. 3027-3038
    • Lam, N.1    Sugden, B.2
  • 29
    • 0035920120 scopus 로고    scopus 로고
    • The cellular protein PRA1 modulates the anti-apoptotic activity of Epstein-Barr virus BHRF1, a homologue of Bcl-2, through direct interaction
    • Li LY, Shih HM, Liu MY, Chen JY (2001) The cellular protein PRA1 modulates the anti-apoptotic activity of Epstein-Barr virus BHRF1, a homologue of Bcl-2, through direct interaction. J Biol Chem 276: 27354-27362
    • (2001) J Biol Chem , vol.276 , pp. 27354-27362
    • Li, L.Y.1    Shih, H.M.2    Liu, M.Y.3    Chen, J.Y.4
  • 30
    • 0035834687 scopus 로고    scopus 로고
    • Membrane topography and topogenesis of prenylated Rab acceptor (PRA1)
    • Lin J, Liang Z, Zhang Z, Li G (2001) Membrane topography and topogenesis of prenylated Rab acceptor (PRA1). J Biol Chem 276: 41733-41741
    • (2001) J Biol Chem , vol.276 , pp. 41733-41741
    • Lin, J.1    Liang, Z.2    Zhang, Z.3    Li, G.4
  • 32
    • 2442486341 scopus 로고    scopus 로고
    • Phenotypic alterations induced by the Hong Kong-prevalent Epstein-Barr virus-encoded LMP1 variant (2117-LMP1) in nasopharyngeal epithelial cells
    • Lo AK, Huang DP, Lo KW, Chui YL, Li HM, Pang JC, Tsao SW (2004) Phenotypic alterations induced by the Hong Kong-prevalent Epstein-Barr virus-encoded LMP1 variant (2117-LMP1) in nasopharyngeal epithelial cells. Int J Cancer 109: 919-925
    • (2004) Int J Cancer , vol.109 , pp. 919-925
    • Lo, A.K.1    Huang, D.P.2    Lo, K.W.3    Chui, Y.L.4    Li, H.M.5    Pang, J.C.6    Tsao, S.W.7
  • 33
    • 0030732268 scopus 로고    scopus 로고
    • A SNARE involved in protein transport through the Golgi apparatus
    • Lowe SL, Peter F, Subramaniam VN, Wong SH, Hong W (1997) A SNARE involved in protein transport through the Golgi apparatus. Nature 389: 881-884
    • (1997) Nature , vol.389 , pp. 881-884
    • Lowe, S.L.1    Peter, F.2    Subramaniam, V.N.3    Wong, S.H.4    Hong, W.5
  • 34
    • 0021354880 scopus 로고
    • Monensin prevents terminal glycosylation of the N- and O-linked oligosaccharides of the HLA-DR-associated invariant chain and inhibits its dissociation from the alpha-beta chain complex
    • Machamer CE, Cresswell P (1984) Monensin prevents terminal glycosylation of the N- and O-linked oligosaccharides of the HLA-DR-associated invariant chain and inhibits its dissociation from the alpha-beta chain complex. Proc Natl Acad Sci USA 81: 1287-1291
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 1287-1291
    • Machamer, C.E.1    Cresswell, P.2
  • 35
    • 0030783121 scopus 로고    scopus 로고
    • Isolation and characterization of a dual prenylated Rab and VAMP2 receptor
    • Martincic I, Peralta ME, Ngsee JK (1997) Isolation and characterization of a dual prenylated Rab and VAMP2 receptor. J Biol Chem 272: 26991-26998
    • (1997) J Biol Chem , vol.272 , pp. 26991-26998
    • Martincic, I.1    Peralta, M.E.2    Ngsee, J.K.3
  • 36
    • 0032865424 scopus 로고    scopus 로고
    • Palmitoylation of GAP-43 by the ER-Golgi intermediate compartment and Golgi apparatus
    • McLaughlin RE, Denny JB (1999) Palmitoylation of GAP-43 by the ER-Golgi intermediate compartment and Golgi apparatus. Biochim Biophys Acta 1451: 82-92
    • (1999) Biochim Biophys Acta , vol.1451 , pp. 82-92
    • McLaughlin, R.E.1    Denny, J.B.2
  • 37
    • 0842309131 scopus 로고    scopus 로고
    • ER-to-Golgi transport and cytoskeletal interactions in animal cells
    • Murshid A, Presley JF (2004) ER-to-Golgi transport and cytoskeletal interactions in animal cells. Cell Mol Life Sci 61: 133-145
    • (2004) Cell Mol Life Sci , vol.61 , pp. 133-145
    • Murshid, A.1    Presley, J.F.2
  • 39
    • 0036159169 scopus 로고    scopus 로고
    • Association of the Epstein-Barr virus latent membrane protein 1 with lipid rafts is mediated through its N-terminal region
    • Rothenberger S, Rousseaux M, Knecht H, Bender FC, Legler DF, Bron C (2002) Association of the Epstein-Barr virus latent membrane protein 1 with lipid rafts is mediated through its N-terminal region. Cell Mol Life Sci 59: 171-180
    • (2002) Cell Mol Life Sci , vol.59 , pp. 171-180
    • Rothenberger, S.1    Rousseaux, M.2    Knecht, H.3    Bender, F.C.4    Legler, D.F.5    Bron, C.6
  • 40
    • 0030925641 scopus 로고    scopus 로고
    • Characterization of LMP-1's association with TRAF1, TRAF2, and TRAF3
    • Sandberg M, Hammerschmidt W, Sugden B (1997) Characterization of LMP-1's association with TRAF1, TRAF2, and TRAF3. J Virol 71: 4649-4656
    • (1997) J Virol , vol.71 , pp. 4649-4656
    • Sandberg, M.1    Hammerschmidt, W.2    Sugden, B.3
  • 41
    • 0242363237 scopus 로고    scopus 로고
    • Yip3 catalyses the dissociation of endosomal Rab-GDI complexes
    • Sivars U, Aivazian D, Pfeffer SR (2003) Yip3 catalyses the dissociation of endosomal Rab-GDI complexes. Nature 425: 856-859
    • (2003) Nature , vol.425 , pp. 856-859
    • Sivars, U.1    Aivazian, D.2    Pfeffer, S.R.3
  • 42
    • 0032517823 scopus 로고    scopus 로고
    • Recycling of Golgi-resident glycosyltransferases through the ER reveals a novel pathway and provides an explanation for nocodazole-induced Golgi scattering
    • Storrie B, White J, Rottger S, Stelzer EH, Suganuma T, Nilsson T (1998) Recycling of Golgi-resident glycosyltransferases through the ER reveals a novel pathway and provides an explanation for nocodazole-induced Golgi scattering. J Cell Biol 143: 1505-1521
    • (1998) J Cell Biol , vol.143 , pp. 1505-1521
    • Storrie, B.1    White, J.2    Rottger, S.3    Stelzer, E.H.4    Suganuma, T.5    Nilsson, T.6
  • 44
    • 0036800355 scopus 로고    scopus 로고
    • GS15 Forms a SNARE complex with syntaxin 5, GS28, and Ykt6 and is implicated in traffic in the early cisternae of the Golgi apparatus
    • Xu Y, Martin S, James DE, Hong W (2002) GS15 Forms a SNARE complex with syntaxin 5, GS28, and Ykt6 and is implicated in traffic in the early cisternae of the Golgi apparatus. Mol Biol Cell 13: 3493-3507
    • (2002) Mol Biol Cell , vol.13 , pp. 3493-3507
    • Xu, Y.1    Martin, S.2    James, D.E.3    Hong, W.4
  • 45
    • 0032555572 scopus 로고    scopus 로고
    • A 29-kilodalton Golgi soluble N-ethylmaleimide-sensitive factor attachment protein receptor (Vti1-rp2) implicated in protein trafficking in the secretory pathway
    • Xu Y, Wong SH, Tang BL, Subramaniam VN, Zhang T, Hong W (1998) A 29-kilodalton Golgi soluble N-ethylmaleimide-sensitive factor attachment protein receptor (Vti1-rp2) implicated in protein trafficking in the secretory pathway. J Biol Chem 273: 21783-21789
    • (1998) J Biol Chem , vol.273 , pp. 21783-21789
    • Xu, Y.1    Wong, S.H.2    Tang, B.L.3    Subramaniam, V.N.4    Zhang, T.5    Hong, W.6
  • 46
    • 0347088997 scopus 로고    scopus 로고
    • Latent infection membrane protein transmembrane FWLY is critical for intermolecular interaction, raft localization, and signaling
    • Yasui T, Luftig M, Soni V, Kieff E (2004) Latent infection membrane protein transmembrane FWLY is critical for intermolecular interaction, raft localization, and signaling. Proc Natl Acad Sci USA 101: 278-283
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 278-283
    • Yasui, T.1    Luftig, M.2    Soni, V.3    Kieff, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.