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http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/77518完整後設資料紀錄
| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 陳美如(Mei-Ru Chen) | |
| dc.contributor.author | Ssu-Hua Chen | en |
| dc.contributor.author | 陳思樺 | zh_TW |
| dc.date.accessioned | 2021-07-10T22:06:36Z | - |
| dc.date.available | 2021-07-10T22:06:36Z | - |
| dc.date.copyright | 2021-02-25 | |
| dc.date.issued | 2020 | |
| dc.date.submitted | 2020-12-22 | |
| dc.identifier.citation | Ahmad, S.S., J. Glatzle, K. Bajaeifer, S. Buhler, T. Lehmann, I. Konigsrainer, J.P. Vollmer, B. Sipos, S.S. Ahmad, H. Northoff, A. Konigsrainer, and D. Zieker. 2013. Phosphoglycerate kinase 1 as a promoter of metastasis in colon cancer. Int J Oncol. 43:586-590.
Ai, J., H. Huang, X. Lv, Z. Tang, M. Chen, T. Chen, W. Duan, H. Sun, Q. Li, R. Tan, Y. Liu, J. Duan, Y. Yang, Y. Wei, Y. Li, and Q. Zhou. 2011. FLNA and PGK1 are two potential markers for progression in hepatocellular carcinoma. Cell Physiol Biochem. 27:207-216. Alwine, J.C. 2012. The Human Cytomegalovirus Assembly Compartment: A Masterpiece of Viral Manipulation of Cellular Processes That Facilitates Assembly and Egress. PLOS Pathogens. 8:e1002878. Baer, R., A.T. Bankier, M.D. Biggin, P.L. Deininger, P.J. Farrell, T.J. Gibson, G. Hatfull, G.S. Hudson, S.C. Satchwell, C. Séguin, P.S. Tuffnell, and B.G. Barrell. 1984. DNA sequence and expression of the B95-8 Epstein—Barr virus genome. Nature. 310:207-211. Bailey, R.E. 1994. Diagnosis and treatment of infectious mononucleosis. Am Fam Physician. 49:879-888. Banks, R.D., C.C. Blake, P.R. Evans, R. Haser, D.W. Rice, G.W. Hardy, M. Merrett, and A.W. Phillips. 1979. Sequence, structure and activity of phosphoglycerate kinase: a possible hinge-bending enzyme. Nature. 279:773-777. Berger, K.H., L.F. Sogo, and M.P. Yaffe. 1997. Mdm12p, a component required for mitochondrial inheritance that is conserved between budding and fission yeast. J Cell Biol. 136:545-553. Bernstein, B.E., and W.G. Hol. 1998. Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism. Biochemistry. 37:4429-4436. Briggs, M.W., and D.B. Sacks. 2003a. IQGAP1 as signal integrator: Ca2+, calmodulin, Cdc42 and the cytoskeleton. FEBS Lett. 542:7-11. Briggs, M.W., and D.B. Sacks. 2003b. IQGAP proteins are integral components of cytoskeletal regulation. EMBO Rep. 4:571-574. Burgess, S.M., M. Delannoy, and R.E. Jensen. 1994. MMM1 encodes a mitochondrial outer membrane protein essential for establishing and maintaining the structure of yeast mitochondria. J Cell Biol. 126:1375-1391. Chang, C.W., C.P. Lee, M.T. Su, C.H. Tsai, and M.R. Chen. 2015. BGLF4 kinase modulates the structure and transport preference of the nuclear pore complex to facilitate nuclear import of Epstein-Barr virus lytic proteins. J Virol. 89:1703-1718. 63 Chang, L.S., J.T. Wang, S.L. Doong, C.P. Lee, C.W. Chang, C.H. Tsai, S.W. Yeh, C.Y. Hsieh, and M.R. Chen. 2012a. Epstein-Barr virus BGLF4 kinase downregulates NF-kappaB transactivation through phosphorylation of coactivator UXT. J Virol. 86:12176-12186. Chang, Y.-H., C.-P. Lee, M.-T. Su, J.-T. Wang, J.-Y. Chen, S.-F. Lin, C.-H. Tsai, M.-J. Hsieh, K. Takada, and M.-R. Chen. 2012b. Epstein-Barr virus BGLF4 kinase retards cellular S-phase progression and induces chromosomal abnormality. PLoS One. 7:e39217-e39217. Chang, Y., C.H. Tung, Y.T. Huang, J. Lu, J.Y. Chen, and C.H. Tsai. 1999. Requirement for cell-to-cell contact in Epstein-Barr virus infection of nasopharyngeal carcinoma cells and keratinocytes. J Virol. 73:8857-8866. Chau, C.M., X.Y. Zhang, S.B. McMahon, and P.M. Lieberman. 2006. Regulation of Epstein-Barr virus latency type by the chromatin boundary factor CTCF. J Virol. 80:5723-5732. Chen, M.R., S.J. Chang, H. Huang, and J.Y. Chen. 2000. A protein kinase activity associated with Epstein-Barr virus BGLF4 phosphorylates the viral early antigen EA-D in vitro. J Virol. 74:3093-3104. Chen, Z., W. Zhuang, Z. Wang, W. Xiao, W. Don, X. Li, and X. Chen. 2019. MicroRNA-450b-3p inhibits cell growth by targeting phosphoglycerate kinase 1 in hepatocellular carcinoma. J Cell Biochem. 120:18805-18815. Combs, J.A., E.B. Norton, Z.R. Saifudeen, K.H.Z. Bentrup, P.V. Katakam, C.A. Morris, L. Myers, A. Kaur, D.E. Sullivan, and K.J. Zwezdaryk. 2020. Human Cytomegalovirus Alters Host Cell Mitochondrial Function during Acute Infection. Journal of Virology. 94:e01183-01119. Dong, W., H. Li, and X. Wu. 2019. Rab11-FIP2 suppressed tumor growth via regulation of PGK1 ubiquitination in non-small cell lung cancer. Biochem Biophys Res Commun. 508:60-65. Duleh, S.N., and M.D. Welch. 2010. WASH and the Arp2/3 complex regulate endosome shape and trafficking. Cytoskeleton (Hoboken). 67:193-206. Fehrenbacher, K.L., I.R. Boldogh, and L.A. Pon. 2005. A role for Jsn1p in recruiting the Arp2/3 complex to mitochondria in budding yeast. Mol Biol Cell. 16:5094-5102. Fehrenbacher, K.L., H.C. Yang, A.C. Gay, T.M. Huckaba, and L.A. Pon. 2004. Live cell imaging of mitochondrial movement along actin cables in budding yeast. Curr Biol. 14:1996-2004. Fujii, K., N. Yokoyama, T. Kiyono, K. Kuzushima, M. Homma, Y. Nishiyama, M. Fujita, and T. Tsurumi. 2000. The Epstein-Barr virus pol catalytic subunit physically interacts with the BBLF4-BSLF1-BBLF2/3 complex. Journal of virology. 74:2550-2557. Fukata, M., S. Kuroda, K. Fujii, T. Nakamura, I. Shoji, Y. Matsuura, K. Okawa, A. Iwamatsu, A. Kikuchi, and K. Kaibuchi. 1997. Regulation of cross-linking of actin filament by IQGAP1, a target for Cdc42. J Biol Chem. 272:29579-29583. Fukata, M., S. Kuroda, M. Nakagawa, A. Kawajiri, N. Itoh, I. Shoji, Y. Matsuura, S. Yonehara, H. Fujisawa, A. Kikuchi, and K. Kaibuchi. 1999. Cdc42 and Rac1 regulate the interaction of IQGAP1 with beta-catenin. J Biol Chem. 274:26044-26050. Fukata, M., T. Watanabe, J. Noritake, M. Nakagawa, M. Yamaga, S. Kuroda, Y. Matsuura, A. Iwamatsu, F. Perez, and K. Kaibuchi. 2002. Rac1 and Cdc42 capture microtubules through IQGAP1 and CLIP-170. Cell. 109:873-885. Ge, J., J. Li, S. Na, P. Wang, G. Zhao, and X. Zhang. 2019. miR-548c-5p inhibits colorectal cancer cell proliferation by targeting PGK1. J Cell Physiol. 234:18872-18878. Gershburg, E., M. Marschall, K. Hong, and J.S. Pagano. 2004. Expression and localization of the Epstein-Barr virus-encoded protein kinase. J Virol. 78:12140-12146. Gonnella, R., A. Farina, R. Santarelli, S. Raffa, R. Feederle, R. Bei, M. Granato, A. Modesti, L. Frati, H.J. Delecluse, M.R. Torrisi, A. Angeloni, and A. Faggioni. 2005. Characterization and intracellular localization of the Epstein-Barr virus protein BFLF2: interactions with BFRF1 and with the nuclear lamina. J Virol. 79:3713-3727. Grogan, E., H. Jenson, J. Countryman, L. Heston, L. Gradoville, and G. Miller. 1987. Transfection of a rearranged viral DNA fragment, WZhet, stably converts latent Epstein-Barr viral infection to productive infection in lymphoid cells. Proc Natl Acad Sci U S A. 84:1332-1336. He, Y., Y. Luo, D. Zhang, X. Wang, P. Zhang, H. Li, S. Ejaz, and S. Liang. 2019. PGK1-mediated cancer progression and drug resistance. Am J Cancer Res. 9:2280-2302. Henaff, D., K. Radtke, and R. Lippé. 2012. Herpesviruses exploit several host compartments for envelopment. Traffic. 13:1443-1449. Ho, M.Y., S.J. Tang, W.V. Ng, W. Yang, S.J. Leu, Y.C. Lin, C.K. Feng, J.S. Sung, and K.H. Sun. 2010. Nucleotide-binding domain of phosphoglycerate kinase 1 reduces tumor growth by suppressing COX-2 expression. Cancer Sci. 101:2411-2416. Hobbs, A.E., M. Srinivasan, J.M. McCaffery, and R.E. Jensen. 2001. Mmm1p, a mitochondrial outer membrane protein, is connected to mitochondrial DNA (mtDNA) nucleoids and required for mtDNA stability. J Cell Biol. 152:401-410. Hu, H., W. Zhu, J. Qin, M. Chen, L. Gong, L. Li, X. Liu, Y. Tao, H. Yin, H. Zhou, L. Zhou, D. Ye, Q. Ye, and D. Gao. 2017. Acetylation of PGK1 promotes liver cancer cell proliferation and tumorigenesis. Hepatology. 65:515-528. Huang, W.-H. 2018. Characterization of viral proteins and cellular factors involved in EBV cytoplasmic assembly compartment. In Graduate Institute of Microbiology. National Taiwan University, College of Medicine. Huckaba, T.M., A.C. Gay, L.F. Pantalena, H.-C. Yang, and L.A. Pon. 2004. Live cell imaging of the assembly, disassembly, and actin cable-dependent movement of endosomes and actin patches in the budding yeast, Saccharomyces cerevisiae. J Cell Biol. 167:519-530. Hudewentz, J., G.W. Bornkamm, and H. Zur Hausen. 1980. Effect of the diterpene ester TPA on Epstein-Barr virus antigen- and DNA synthesis in producer and nonproducer cell lines. Virology. 100:175-178. Imamura, H., K.P. Nhat, H. Togawa, K. Saito, R. Iino, Y. Kato-Yamada, T. Nagai, and H. Noji. 2009. Visualization of ATP levels inside single living cells with fluorescence resonance energy transfer-based genetically encoded indicators. Proc Natl Acad Sci U S A. 106:15651-15656. Janke, C., and G. Montagnac. 2017. Causes and Consequences of Microtubule Acetylation. Curr Biol. 27:R1287-r1292. Johnson, M., M. Sharma, and B.R. Henderson. 2009. IQGAP1 regulation and roles in cancer. Cell Signal. 21:1471-1478. Küppers, R. 2009. The biology of Hodgkin's lymphoma. Nat Rev Cancer. 9:15-27. Kudoh, A., T. Daikoku, Y. Ishimi, Y. Kawaguchi, N. Shirata, S. Iwahori, H. Isomura, and T. Tsurumi. 2006. Phosphorylation of MCM4 at Sites Inactivating DNA Helicase Activity of the MCM4-MCM6-MCM7 Complex during Epstein-Barr Virus Productive Replication. Journal of Virology. 80:10064-10072. Kuroda, S., M. Fukata, M. Nakagawa, K. Fujii, T. Nakamura, T. Ookubo, I. Izawa, T. Nagase, N. Nomura, H. Tani, I. Shoji, Y. Matsuura, S. Yonehara, and K. Kaibuchi. 1998. Role of IQGAP1, a target of the small GTPases Cdc42 and Rac1, in regulation of E-cadherin- mediated cell-cell adhesion. Science. 281:832-835. Lay, A.J., X.-M. Jiang, O. Kisker, E. Flynn, A. Underwood, R. Condron, and P.J. Hogg. 2000. Phosphoglycerate kinase acts in tumour angiogenesis as a disulphide reductase. Nature. 408:869-873. Lee, C.-P., Y.-H. Huang, S.-F. Lin, Y. Chang, Y.-H. Chang, K. Takada, and M.-R. Chen. 2008. Epstein-Barr Virus BGLF4 Kinase Induces Disassembly of the Nuclear Lamina To Facilitate Virion Production. Journal of Virology. 82:11913-11926. Lee, C.P., J.Y. Chen, J.T. Wang, K. Kimura, A. Takemoto, C.C. Lu, and M.R. Chen. 2007. Epstein-Barr virus BGLF4 kinase induces premature chromosome condensation through activation of condensin and topoisomerase II. J Virol. 81:5166-5180. Lee, M.-A., M.E. Diamond, and J.L. Yates. 1999. Genetic Evidence that EBNA-1 Is Needed for Efficient, Stable Latent Infection by Epstein-Barr Virus. Journal of Virology. 73:2974-2982. Li, D., W. Fu, and S. Swaminathan. 2018a. Continuous DNA replication is required for late gene transcription and maintenance of replication compartments in gammaherpesviruses. PLoS Pathog. 14:e1007070. Li, H., S. Liu, J. Hu, X. Luo, N. Li, A. M Bode, and Y. Cao. 2016a. Epstein-Barr virus lytic reactivation regulation and its pathogenic role in carcinogenesis. Int J Biol Sci. 12:1309-1318. Li, L., Y. Liang, L. Kang, Y. Liu, S. Gao, S. Chen, Y. Li, W. You, Q. Dong, T. Hong, Z. Yan, S. Jin, T. Wang, W. Zhao, H. Mai, J. Huang, X. Han, Q. Ji, Q. Song, C. Yang, S. Zhao, X. Xu, and Q. Ye. 2018b. Transcriptional Regulation of the Warburg Effect in Cancer by SIX1. Cancer Cell. 33:368-385.e367. Li, X., Y. Jiang, J. Meisenhelder, W. Yang, D.H. Hawke, Y. Zheng, Y. Xia, K. Aldape, J. He, T. Hunter, L. Wang, and Z. Lu. 2016b. Mitochondria-Translocated PGK1 Functions as a Protein Kinase to Coordinate Glycolysis and the TCA Cycle in Tumorigenesis. Mol Cell. 61:705-719. Li, X., S.V. Kozlov, A. El-Guindy, and S. Bhaduri-McIntosh. 2019. Retrograde Regulation by the Viral Protein Kinase Epigenetically Sustains the Epstein-Barr Virus Latency-to-Lytic Switch To Augment Virus Production. Journal of virology. 93:e00572-00519. Lin, C.T., W.Y. Chan, W. Chen, H.M. Huang, H.C. Wu, M.M. Hsu, S.M. Chuang, and C.C. Wang. 1993. Characterization of seven newly established nasopharyngeal carcinoma cell lines. Lab Invest. 68:716-727. Luka, J., B. Kallin, and G. Klein. 1979. Induction of the Epstein-Barr virus (EBV) cycle in latently infected cells by n-butyrate. Virology. 94:228-231. Lyu, X., J. Wang, X. Guo, G. Wu, Y. Jiao, O.D. Faleti, P. Liu, T. Liu, Y. Long, T. Chong, X. Yang, J. Huang, M. He, C.M. Tsang, S.W. Tsao, Q. Wang, Q. Jiang, and X. Li. 2018. EBV-miR-BART1-5P activates AMPK/mTOR/HIF1 pathway via a PTEN independent manner to promote glycolysis and angiogenesis in nasopharyngeal carcinoma. PLoS Pathog. 14:e1007484. Mateer, S.C., A.E. McDaniel, V. Nicolas, G.M. Habermacher, M.J. Lin, D.A. Cromer, M.E. King, and G.S. Bloom. 2002. The mechanism for regulation of the F-actin binding activity of IQGAP1 by calcium/calmodulin. J Biol Chem. 277:12324-12333. Mettenleiter, T.C., B.G. Klupp, and H. Granzow. 2009. Herpesvirus assembly: an update. Virus Res. 143:222-234. Moar, M.H., and G. Klein. 1978. Detection of Epstein-Barr virus (EBV) DNA sequences using in situ hybridization. Biochim Biophys Acta. 519:49-64. Nie, H., H. Ju, J. Fan, X. Shi, Y. Cheng, X. Cang, Z. Zheng, X. Duan, and W. Yi. 2020. O-GlcNAcylation of PGK1 coordinates glycolysis and TCA cycle to promote tumor growth. Nature Communications. 11:36. Niederman, J.C., A.S. Evans, L. Subrahmanyan, and R.W. McCollum. 1970. Prevalence, incidence and persistence of EB virus antibody in young adults. N Engl J Med. 282:361-365. Noritake, J., T. Watanabe, K. Sato, S. Wang, and K. Kaibuchi. 2005. IQGAP1: a key regulator of adhesion and migration. J Cell Sci. 118:2085-2092. Owen, D., L.J. Campbell, K. Littlefield, K.A. Evetts, Z. Li, D.B. Sacks, P.N. Lowe, and H.R. Mott. 2008. The IQGAP1-Rac1 and IQGAP1-Cdc42 interactions: interfaces differ between the complexes. J Biol Chem. 283:1692-1704. Pal, A.D., N.P. Basak, A.S. Banerjee, and S. Banerjee. 2014. Epstein-Barr virus latent membrane protein-2A alters mitochondrial dynamics promoting cellular migration mediated by Notch signaling pathway. Carcinogenesis. 35:1592-1601. Pattle, S.B., and P.J. Farrell. 2006. The role of Epstein-Barr virus in cancer. Expert Opin Biol Ther. 6:1193-1205. Pelikan-Conchaudron, A., C. Le Clainche, D. Didry, and M.-F. Carlier. 2011. The IQGAP1 protein is a calmodulin-regulated barbed end capper of actin filaments: possible implications in its function in cell migration. The Journal of biological chemistry. 286:35119-35128. Prasanth, K.R., C. Chuang, and P.D. Nagy. 2017. Co-opting ATP-generating glycolytic enzyme PGK1 phosphoglycerate kinase facilitates the assembly of viral replicase complexes. PLoS pathogens. 13:e1006689-e1006689. Procter, D.J., A. Banerjee, M. Nukui, K. Kruse, V. Gaponenko, E.A. Murphy, Y. Komarova, and D. Walsh. 2018. The HCMV Assembly Compartment Is a Dynamic Golgi-Derived MTOC that Controls Nuclear Rotation and Virus Spread. Dev Cell. 45:83- 100.e107. Qian, X., X. Li, Q. Cai, C. Zhang, Q. Yu, Y. Jiang, J.H. Lee, D. Hawke, Y. Wang, Y. Xia, Y. Zheng, B.H. Jiang, D.X. Liu, T. Jiang, and Z. Lu. 2017. Phosphoglycerate Kinase 1 Phosphorylates Beclin1 to Induce Autophagy. Mol Cell. 65:917-931 e916. Ragoczy, T., L. Heston, and G. Miller. 1998. The Epstein-Barr virus Rta protein activates lytic cycle genes and can disrupt latency in B lymphocytes. Journal of virology. 72:7978-7984. Roy, M., Z. Li, and D.B. Sacks. 2004. IQGAP1 binds ERK2 and modulates its activity. J Biol Chem. 279:17329-17337. Samson, E.B., D.S. Tsao, J. Zimak, R.T. McLaughlin, N.J. Trenton, E.M. Mace, J.S. Orange, V. Schweikhard, and M.R. Diehl. 2017. The coordinating role of IQGAP1 in the regulation of local, endosome-specific actin networks. Biol Open. 6:785-799. Seo, J.S., N.Y. Cho, H.R. Kim, T. Tsurumi, Y.S. Jang, W.K. Lee, and S.K. Lee. 2008. Cell cycle arrest and lytic induction of EBV-transformed B lymphoblastoid cells by a histone deacetylase inhibitor, Trichostatin A. Oncol Rep. 19:93-98. Shetty, S., M. Ganachari, M.C. Liu, A. Azghani, H. Muniyappa, and S. Idell. 2005. Regulation of urokinase receptor expression by phosphoglycerate kinase is independent of its catalytic activity. Am J Physiol Lung Cell Mol Physiol. 289:L591-598. Sogo, L.F., and M.P. Yaffe. 1994. Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane. J Cell Biol. 126:1361-1373. Su, M.T., Y.T. Wang, Y.J. Chen, S.F. Lin, C.H. Tsai, and M.R. Chen. 2017. The SWI/SNF Chromatin Regulator BRG1 Modulates the Transcriptional Regulatory Activity of the Epstein-Barr Virus DNA Polymerase Processivity Factor BMRF1. J Virol. 91. Sugimoto, A., Y. Sato, T. Kanda, T. Murata, Y. Narita, D. Kawashima, H. Kimura, and T. Tsurumi. 2013. Different distributions of Epstein-Barr virus early and late gene transcripts within viral replication compartments. Journal of virology. 87:6693- 6699. Takada, K. 1984. Cross-linking of cell surface immunoglobulins induces Epstein-Barr virus in Burkitt lymphoma lines. Int J Cancer. 33:27-32. Valentini, G., M. Maggi, and A.L. Pey. 2013. Protein Stability, Folding and Misfolding in Human PGK1 Deficiency. Biomolecules. 3:1030-1052. Wang, J., W. Guo, C. Long, H. Zhou, H. Wang, and X. Sun. 2016. The split Renilla luciferase complementation assay is useful for identifying the interaction of Epstein-Barr virus protein kinase BGLF4 and a heat shock protein Hsp90. Acta Virol. 60:62-70. Wang, J.T., S.L. Doong, S.C. Teng, C.P. Lee, C.H. Tsai, and M.R. Chen. 2009. Epstein-Barr virus BGLF4 kinase suppresses the interferon regulatory factor 3 signaling pathway. J Virol. 83:1856-1869. Wang, J.T., P.W. Yang, C.P. Lee, C.H. Han, C.H. Tsai, and M.R. Chen. 2005. Detection of Epstein-Barr virus BGLF4 protein kinase in virus replication compartments and virus particles. J Gen Virol. 86:3215-3225. Wang, S., B. Jiang, T. Zhang, L. Liu, Y. Wang, Y. Wang, X. Chen, H. Lin, L. Zhou, Y. Xia, L. Chen, C. Yang, Y. Xiong, D. Ye, and K.-L. Guan. 2015. Insulin and mTOR Pathway Regulate HDAC3-Mediated Deacetylation and Activation of PGK1. PLOS Biology. 13:e1002243. Westermann, B. 2010. Mitochondrial fusion and fission in cell life and death. Nat Rev Mol Cell Biol. 11:872-884. Xie, H., G. Tong, Y. Zhang, S. Liang, K. Tang, and Q. Yang. 2017. PGK1 Drives Hepatocellular Carcinoma Metastasis by Enhancing Metabolic Process. 18:1630. Yang, T.-Y. 2013. EBV BGLF4 Induces Formation of Viral Cytoplasmic Assembly Compartment Through Rearrangement of Cytoskeleton. In Graduate Institute of Microbiology. National Taiwan University., College of Medicine. Yu, T., Y. Zhao, Z. Hu, J. Li, D. Chu, J. Zhang, Z. Li, B. Chen, X. Zhang, H. Pan, S. Li, H. Lin, L. Liu, M. Yan, X. He, and M. Yao. 2017. MetaLnc9 Facilitates Lung Cancer Metastasis via a PGK1-Activated AKT/mTOR Pathway. 77:5782-5794. Yuan, S.X., F. Yang, Y. Yang, Q.F. Tao, J. Zhang, G. Huang, Y. Yang, R.Y. Wang, S. Yang, X.S. Huo, L. Zhang, F. Wang, S.H. Sun, and W.P. Zhou. 2012. Long noncoding RNA associated with microvascular invasion in hepatocellular carcinoma promotes angiogenesis and serves as a predictor for hepatocellular carcinoma patients' poor recurrence-free survival after hepatectomy. Hepatology. 56:2231-2241. Zhang, D., L.K. Tai, L.L. Wong, L.L. Chiu, S.K. Sethi, and E.S. Koay. 2005. Proteomic study reveals that proteins involved in metabolic and detoxification pathways are highly expressed in HER-2/neu-positive breast cancer. Mol Cell Proteomics. 4:1686-1696. Zhang, K., D.W. Lv, and R. Li. 2019. Conserved Herpesvirus Protein Kinases Target SAMHD1 to Facilitate Virus Replication. Cell Rep. 28:449-459.e445. Zhang, Y., H. Cai, Y. Liao, Y. Zhu, F. Wang, and J. Hou. 2020. Activation of PGK1 under hypoxic conditions promotes glycolysis and increases stem cell - like properties and the epithelial - mesenchymal transition in oral squamous cell carcinoma cells via the AKT signalling pathway. Int J Oncol. 57:743-755. Zhang, Y., G. Yu, H. Chu, X. Wang, L. Xiong, G. Cai, R. Liu, H. Gao, B. Tao, W. Li, G. Li, J. Liang, and W. Yang. 2018. Macrophage-Associated PGK1 Phosphorylation Promotes Aerobic Glycolysis and Tumorigenesis. Mol Cell. 71:201-215.e207. Zieker, D., I. Königsrainer, I. Tritschler, M. Löffler, S. Beckert, F. Traub, K. Nieselt, S. Bühler, M. Weller, J. Gaedcke, R.S. Taichman, H. Northoff, B.L. Brücher, and A. Königsrainer. 2010. Phosphoglycerate kinase 1 a promoting enzyme for peritoneal dissemination in gastric cancer. Int J Cancer. 126:1513-1520. | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/77518 | - |
| dc.description.abstract | 疱疹病毒基因體在細胞核複製後,帶著病毒 DNA 的核殼體 (nucleocapsid) 會被運送到細胞質中進行膜蛋白包覆 (tegumentation),加上細胞蛋白質和病毒蛋白質以及病毒披膜蛋白的套膜完成病毒組裝。EB 病毒蛋白激酶 BGLF4 是一個具有與 CDK1 功能相似的蛋白酶,可以促使微管組織中心(microtubule organization center, MTOC) 的形成。在先前的研究發現,除了在細胞核之外,BGLF4 會有小部分聚集至病毒組裝區域 (assembly compartment),並且與 IQGAP1 有共定位的現象。IQGAP1 可以透過調控細胞骨架影響細胞附著以及移動能力。我們認為在表現 BGLF4 的情況下,IQGAP1 會將許多蛋白質帶到病毒組裝區域。在之前實驗室的共同免疫沉澱質譜儀分析結果中,發現在表現 BGLF4 的情況下磷酸甘油酸激酶 1 (PGK1) 與 IQGAP1 有相互作用。PGK1 在細胞中主要參與在糖解作用,PGK1 會將 1,3BPG 轉換成 3PG,同時產生一個 ATP。在本研究中,我們發現 PGK1 會聚集在病毒組裝區域,並且與粒線體有共定位的現象,然而目前的實驗方法無法觀察到在粒線體中的 PGK1。另一方面,我們想要知道剔除 PGK1 是否會影響病毒的複製以及病毒顆粒的組裝,因此我們利用 QPCR 的方式偵測細胞內外的病毒量,發現抑制 PGK1 蛋白質在 48 小時的時候對病毒 DNA 複製影響較小只會抑制病毒顆粒釋出細胞,而在 72 小時則會減少病毒 DNA 的複製以及病毒顆粒釋出細胞。我們也探討 PGK1 是否會影響到病毒組裝區域的蛋白質,而我們發現抑制 PGK1 後會些微影響到病毒蛋白酶 BGLF4 聚集至病毒組裝區域。我們認為 PGK1 可能在病毒組裝區域中扮演提供 ATP 的角色, 因此我們利用螢光共振能量轉移系統 (FRET) 觀察發現在病毒組裝區域中,ATP 的含量會上升,代表 PGK1 確實有可能在病毒組裝區域中提供許多 ATP。綜上所述,PGK1 聚集至病毒組裝區域在病毒成熟過程中扮演一個重要的角色,值得未來再進一步探討。 | zh_TW |
| dc.description.abstract | After EBV genome replication in the nucleus, nucleocapsids translocated into the cytoplasm through the nucleus egress process. Herpesviruses recruit several viral proteins and cellular components to complete the tegumentation and assembly in the cytoplasm, to facilitate the next round infection. BGLF4 is a CDK1-like protein kinase that can induces microtubule organization center (MTOC) redistribution. In EBV replicating epithelial NA cells, BGLF4 is partially distributed to viral cytoplasmic assembly compartment (AC) and co-localizes with IQ motif containing GTPase Activating Protein (IQGAP1), which is a cytoskeleton hub protein that can modulate cell adhesion and motility. We suggest that IQGAP1 may recruit certain host proteins to the AC to promote EBV in the presence of BGLF4. In the Mass analysis, phosphoglycerate kinase 1 (PGK1), which is an ATP-generating enzyme in the glycolytic pathway, was identified to interact with IQGAP1 in the presence of BGLF4. The appropriate formation of EBV AC may require additional energy for cytoskeleton rearrangement and protein trafficking. In this study, we demonstrated that PGK1 accumulated to the EBV AC and co-localizes with mitochondria. Knockdown of PGK1 causes the decrease of virion secretion at 48, 72 hours post-transfection and the virus DNA replication was reduced at 72 hours post-transfection. Moreover, we found that knockdown of PGK1 interferes with the accumulation of BGLF4 at AC. The ATP concentration at AC is increased after EBV reactivation. Overall, our data suggest PGK1 plays an important role in the EBV assembly and secretion. | en |
| dc.description.provenance | Made available in DSpace on 2021-07-10T22:06:36Z (GMT). No. of bitstreams: 1 U0001-2112202011014600.pdf: 3932914 bytes, checksum: 18bb17dda10c43f1ef4cf70d449eaf46 (MD5) Previous issue date: 2020 | en |
| dc.description.tableofcontents | 口委審定書 I 誌謝 II 中文摘要 III Abstract IV 1. Introduction ................................................................................... 1 1.1. Epstein-Barr Virus ................................................................................... 1 1.1.1. The virus structure and characterization of EBV ........................... 1 1.1.2. The life cycle of EBV ................................................................................... 2 1.1.3. The assembly compartment of human Herpesviruses ........................... 4 1.1.4. EBV protein kinase BGLF4 ................................................................................... 5 1.2. The functions of the cytoskeleton hub protein IQGAP1 ................................................................................... 7 1.3. Mitochondria movement and cytoskeleton rearrangement ........................ 8 1.4. The ATP generating enzyme PGK1 ................................................................................... 9 1.4.1. PGK1 structure and functional domains ................................................................................... 9 1.4.2. The characteristics of PGK1 in cancers. ................................................................................... 9 1.4.3. PGK1 participates in the several signaling pathway. ...................... 10 1.4.4. The post-translation of PGK1 in the tumor cells. ......................... 11 1.4.5. The participation of PGK1 in virus replication ........................... 13 1.5. Specific aims .................................................................................. 13 2. Materials and methods .................................................................................. 15 2.1. Cells culture .................................................................................. 15 2.2. Lentivirus and Plasmid construction .................................................................................. 16 2.3. Plasmids .................................................................................. 17 2.4. Cell transfection .................................................................................. 18 2.5. shPGK1 lentivirus production .................................................................................. 18 2.6. shRNA lentivirus infection .................................................................................. 19 2.7. Mitochondria fractionation .................................................................................. 19 2.8. Western blot analysis .................................................................................. 20 2.9. Immunofluorescence assay (IFA) .................................................................................. 21 2.10. MitoTracker® Red CMXRos staining .................................................................................. 22 2.11. Quantitative real-time PCR (q-PCR) analysis .................................................................................. 22 2.11.1. EBV intracellular DNA extraction .................................................................................. 22 2.11.2. EBV extracellular DNA extraction .................................................................................. 23 2.11.3. Quantitative real-time PCR .................................................................................. 23 3. Results .................................................................................. 25 3.1. PGK1 colocalizes with YFP-mitochondria and BGLF4 in NA cells affect lytic reactivation .................................................................................. 25 3.2. PGK1 colocalizes with mitochondria and BGLF4 at 24, 36, 48 hours post transfection in NA cells .................................................................................. 26 3.3. Expression of BGLF4 changes the distribution of IQGAP1 and PGK1 in HeLa cells .................................................................................. 27 3.4. Expression of BGLF4-DsRed changes the distribution of IQGAP1-YFP in TW01 cells. .................................................................................. 28 3.5. Expression of BGLF4 induces the accumulation of mitochondria to the nuclear concave region in HeLa cells .................................................................................. 29 3.6. BGLF4 changes the distribution of transiently transfected HA-PGK1 in HeLa cells .................................................................................. 31 3.7. PGK1 was not detected in the mitochondria fraction in the presence of BGLF4 in the current protocol .................................................................................. 32 3.8. PGK1 was not detected in the mitochondria fraction after EBV reactivation in the current protocol ..................................................................................33 3.9. ATP concentration is increased within the cytoplasmic assembly compartment upon EBV reactivation .................................................................................. 33 3.10. Knockdown of PGK1 interferes with the distribution of BGLF4 to the perinuclear concave region .................................................................................. 34 3.11. Knockdown of PGK1 affects virus replication and virion secretion in VIII NA cells .................................................................................. 35 4. Discussion .................................................................................. 37 4.1. The possible role of mitochondria in virus replication....................................................................... 37 4.2. BGLF4 regulates the distribution of mitochondria .................................................................................. 38 4.3. PGK1 was not detected in the mitochondria fraction in the current protocol .................................................................................. 40 4.4. PGK1 kinase activity in signaling pathways. .................................................................................. 41 4.5. The energy provider in the assembly compartment .................................................................................. 42 5. Figures .................................................................................. 45 Fig. 1. EBV reactivation induces the redistribution of PGK1 and mitochondria to the perinuclear concave region in NA cells ....................... 44 Fig. 2. EBV reactivation induces the redistribution of PGK1 and mitochondria to the perinuclear concave region in NA cells ....................... 46 Fig. 3. Expression of BGLF4 changes the distribution of IQGAP1 and PGK1 in HeLa cells. .................................................................................. 48 Fig. 4. Expression of BGLF4 induces the redistribution of IQGAP1 in TW01 cells. ........................................................................... 49 Fig. 5. Expression of BGLF4 induces the redistribution of mitochondria to the perinuclear concave region in HeLa cells. .................................................................................. 51 Fig. 6. Expression of BGLF4 changes the distribution of overexpressed PGK1 in HeLa cells. .............................................................. 53 Fig. 7. Mitochondria fractionation protocol did not detect mitochondria- targeted PGK1 in the presence of BGLF4 in HeLa cells. .................................................................................. 55 Fig. 8. Mitochondria fractionation protocol did not detect mitochondria- targeted PGK1 upon EBV reactivation in NA cells. .................................................................................. 57 Fig. 9. ATP concentration is increased upon EBV reactivation ..................... 58 Fig. 10. Knockdown of PGK1 affects the distribution of BGLF4 to assembly compartment in NA cells. .................................................................................. 59 Fig. 11. The presence of PGK1 affects virus replication and virion secretion in NA cells. .................................................................................. 60 6. Reference .................................................................................. 62 | |
| dc.language.iso | en | |
| dc.subject | 磷酸甘油酸激酶1 | zh_TW |
| dc.subject | EB病毒蛋白激酶 | zh_TW |
| dc.subject | 磷酸甘油酸激酶1 | zh_TW |
| dc.subject | 人類皰疹病毒第四型 | zh_TW |
| dc.subject | EB病毒蛋白激酶 | zh_TW |
| dc.subject | 人類皰疹病毒第四型 | zh_TW |
| dc.subject | EBV | en |
| dc.subject | BGLF4 | en |
| dc.subject | BGLF4 | en |
| dc.subject | PGK1 | en |
| dc.subject | PGK1 | en |
| dc.subject | EBV | en |
| dc.title | 細胞蛋白質磷酸甘油酸激酶1 (PGK1) 在EB病毒複製過程中所扮演之角色 | zh_TW |
| dc.title | The role of phosphoglycerate kinase 1 (PGK1) in the Epstein-Barr virus replication | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 109-1 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 徐立中(Li-Chung Hsu),林靜宜(Jing-Yi Lin),李重霈(Chung-Pei Lee),蔡明翰(Ming-Han Tsai) | |
| dc.subject.keyword | 人類皰疹病毒第四型,磷酸甘油酸激酶1,EB病毒蛋白激酶, | zh_TW |
| dc.subject.keyword | EBV,PGK1,BGLF4, | en |
| dc.relation.page | 69 | |
| dc.identifier.doi | 10.6342/NTU202004436 | |
| dc.rights.note | 未授權 | |
| dc.date.accepted | 2020-12-22 | |
| dc.contributor.author-college | 醫學院 | zh_TW |
| dc.contributor.author-dept | 微生物學研究所 | zh_TW |
| 顯示於系所單位: | 微生物學科所 | |
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