Browse > Article
http://dx.doi.org/10.5483/BMBRep.2017.50.5.010

HSV-1 ICP27 represses NF-κB activity by regulating Daxx sumoylation  

Kim, Ji Ae (Department of Microbiology & Molecular Biology, College of Biological Science and Biotechnology, Chungnam National University)
Choi, Mi Sun (Department of predictive toxicology, Korea Institute of Toxicology (KIT))
Min, Jung Sun (Department of Microbiology & Molecular Biology, College of Biological Science and Biotechnology, Chungnam National University)
Kang, Inho (Department of Microbiology & Molecular Biology, College of Biological Science and Biotechnology, Chungnam National University)
Oh, Jeongho (Department of Microbiology & Molecular Biology, College of Biological Science and Biotechnology, Chungnam National University)
Kim, Jin Chul (Division of Biological Sciences, University of California)
Ahn, Jeong Keun (Department of Microbiology & Molecular Biology, College of Biological Science and Biotechnology, Chungnam National University)
Publication Information
BMB Reports / v.50, no.5, 2017 , pp. 275-280 More about this Journal
Abstract
Herpes simplex virus type 1 ICP27 is a multifunctional protein responsible for viral replication, late gene expression, and reactivation from latency. ICP27 interacts with various cellular proteins, including Daxx. However, the role of interaction between ICP27 and Daxx is largely unknown. Since Daxx is known to repress $NF-{\kappa}B$ activity, there is a possibility that ICP27 may influence the inhibitory effect of Daxx on $NF-{\kappa}B$ activity. In this study, we tested whether ICP27 affects the $NF-{\kappa}B$ activity through its interaction with Daxx. Interestingly, ICP27 enhanced the Daxx-mediated repression of $NF-{\kappa}B$ activity. In addition, we found that sumoylation of Daxx regulates its interaction with p65. ICP27 binds to Daxx, inhibits Daxx sumoylation, and enhances p65 deacetylation induced by Daxx. Consequently, ICP27 represses the $NF-{\kappa}B$ activity, by elevating the inhibitory effect of Daxx on $NF-{\kappa}B$ activity through desumoylation of Daxx.
Keywords
Acetylation; Daxx; ICP27; $NF-{\kappa}B$; Sumoylation;
Citations & Related Records
Times Cited By KSCI : 1  (Citation Analysis)
연도 인용수 순위
1 Santoro MG, Rossi A and Amici C (2003) New embo member's review - NF-kappa B and virus infection: who controls whom. EMBO J 22, 2552-2560   DOI
2 Sciortino MT, Medici MA, Marino-Merlo F et al (2008) Involvement of HVEM receptor in activation of nuclear factor kappa B by herpes simplex virus 1 glycoprotein D. Cell Microbiol 10, 2297-2311   DOI
3 Liu XQ, Fitzgerald K, Kurt-Jones E, Finberg R and Knipe DM (2008) Herpesvirus tegument protein activates NFkappa B signaling through the TRAF6 adaptor protein. Proc Natl Acad Sci U S A 105, 11335-11339   DOI
4 Hargett D, Rice S and Bachenheimer SL (2006) Herpes simplex virus type IICP27-Dependent activation of NFkappa B. J Virol 80, 10565-10578   DOI
5 van Lint AL, Murawski MR, Goodbody RE et al (2010) Herpes Simplex Virus Immediate-Early ICP0 Protein Inhibits Toll-Like Receptor 2-Dependent Inflammatory Responses and NF-kappa B Signaling. J Virol 84, 10802-10811   DOI
6 Jang MS, Ryu SW and Kim E (2002) Modification of Daxx by small ubiquitin-related modifier-1. Biochem Biophys Res Commun 295, 495-500   DOI
7 Mo YY, Yu Y, Ee PL and Beck WT (2004) Overexpression of a dominant-negative mutant Ubc9 is associated with increased sensitivity to anticancer drugs. Cancer Res 64, 2793-2798   DOI
8 Schreiner S and Wodrich H (2013) Virion Factors That Target Daxx To Overcome Intrinsic Immunity. J Virol 87, 10412-10422   DOI
9 Chen LF, Mu Y and Greene WC (2002) Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB. EMBO J 21, 6539-6548   DOI
10 McMahan L and Schaffer PA (1990) The repressing and enhancing functions of the herpes simplex virus regulatory protein ICP27 map to C-terminal regions and are required to modulate viral gene expression very early in infection. J Virol 64, 3471-3485
11 Rice SA and Knipe DM (1988) Gene-Specific Transactivation by Herpes-Simplex Virus Type-1 Alpha-Protein-Icp27. J Virol 62, 3814-3823
12 Kuo HY, Chang CC, Jeng JC et al (2005) SUMO modification negatively modulates the transcriptional activity of CREB-binding protein via the recruitment of Daxx. Proc Natl Acad Sci U S A 102, 16973-16978   DOI
13 Shinbo Y, Niki T, Taira T et al (2006) Proper SUMO-1 conjugation is essential to DJ-1 to exert its full activities. Cell Death Differ 13, 96-108   DOI
14 Cook ML and Stevens JG (1973) Pathogenesis of herpetic neuritis and ganglionitis in mice: evidence for intra-axonal transport of infection. Infect Immun 7, 272-288
15 O'Hare P and Goding CR (1988) Herpes simplex virus regulatory elements and the immunoglobulin octamer domain bind a common factor and are both targets for virion transactivation. Cell 52, 435-445   DOI
16 Honess RW and Roizman B (1974) Regulation of herpesvirus macromolecular synthesis. I. Cascade regulation of the synthesis of three groups of viral proteins. J Virol 14, 8-19
17 Sacks WR, Greene CC, Aschman DP and Schaffer PA (1985) Herpes simplex virus type 1 ICP27 is an essential regulatory protein. J Virol 55, 796-805
18 McCarthy AM, McMahan L and Schaffer PA (1989) Herpes simplex virus type 1 ICP27 deletion mutants exhibit altered patterns of transcription and are DNA deficient. J Virol 63, 18-27
19 Hargett D, Rice S and Bachenheimer SL (2006) Herpes simplex virus type 1 ICP27-dependent activation of NFkappaB. J Virol 80, 10565-10578   DOI
20 Gillis PA, Okagaki LH and Rice SA (2009) Herpes simplex virus type 1 ICP27 induces p38 mitogen-activated protein kinase signaling and apoptosis in HeLa cells. J Virol 83, 1767-1777   DOI
21 Melchjorsen J, Siren J, Julkunen I, Paludan SR and Matikainen S (2006) Induction of cytokine expression by herpes simplex virus in human monocyte-derived macrophages and dendritic cells is dependent on virus replication and is counteracted by ICP27 targeting NF-kappaB and IRF-3. J Gen Virol 87, 1099-1108   DOI
22 Hayden MS and Ghosh S (2004) Signaling to NF-kappaB. Genes Dev 18, 2195-2224   DOI
23 Ballard DW, Dixon EP, Peffer NJ et al (1992) The 65-kDa subunit of human NF-kappa B functions as a potent transcriptional activator and a target for v-Rel-mediated repression. Proc Natl Acad Sci U S A 89, 1875-1879   DOI
24 Ghosh S, May MJ and Kopp EB (1998) NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses. Annu Rev Immunol 16, 225-260   DOI
25 Huang B, Yang XD, Lamb A and Chen LF (2010) Posttranslational modifications of NF-kappaB: another layer of regulation for NF-kappaB signaling pathway. Cell Signal 22, 1282-1290   DOI
26 Perkins ND (2006) Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway. Oncogene 25, 6717-6730   DOI
27 Yang X, Khosravi-Far R, Chang HY and Baltimore D (1997) Daxx, a novel Fas-binding protein that activates JNK and apoptosis. Cell 89, 1067-1076   DOI
28 Kiernan R, Bres V, Ng RW et al (2003) Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65. J Biol Chem 278, 2758-2766   DOI
29 Chen L, Fischle W, Verdin E and Greene WC (2001) Duration of nuclear NF-kappaB action regulated by reversible acetylation. Science 293, 1653-1657   DOI
30 Park J, Lee JH, La M et al (2007) Inhibition of NF-kappaB acetylation and its transcriptional activity by Daxx. J Mol Biol 368, 388-397   DOI
31 Salomoni P and Khelifi AF (2006) Daxx: death or survival protein? Trends Cell Biol 16, 97-104   DOI
32 Tang Q, Li L, Ishov AM, Revol V, Epstein AL and Maul GG (2003) Determination of minimum herpes simplex virus type 1 components necessary to localize transcriptionally active DNA to ND10. J Virol 77, 5821-5828   DOI
33 Kim JC, Lee SY, Kim SY et al (2008) HSV-1 ICP27 suppresses NF-kappaB activity by stabilizing IkappaBalpha. FEBS Lett 582, 2371-2376   DOI
34 Muromoto R, Ishida M, Sugiyama K et al (2006) Sumoylation of Daxx regulates IFN-induced growth suppression of B lymphocytes and the hormone receptor-mediated transactivation. J Immunol 177, 1160-1170   DOI
35 Karin M, Cao YX, Greten FR and Li ZW (2002) NF-kappa B in cancer: From innocent bystander to major culprit. Nat Rev Cancer 2, 301-310   DOI
36 Li QT and Verma IM (2002) NF-kappa B regulation in the immune system. Nat Rev Immunol 2, 725-734   DOI
37 Kim SY, Kim JC, Kim JK et al (2008) Hepatitis B virus X protein enhances NFkappaB activity through cooperating with VBP1. BMB Rep 41, 158-163   DOI