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    題名: 蛋白激酶 CK2 與轉錄因子 SRF 所調控之抗細胞凋亡蛋白 Mcl-1 對 PC12 神經細胞之保護機制的探討
    Anti-apoptotic effects of Mcl-1 through CK2-mediated SRF pathway in PC12 cells
    作者: 曾惠敏
    Tseng, Hui Min
    貢獻者: 趙知章
    Chao, Chih Chang
    曾惠敏
    Tseng, Hui Min
    關鍵詞: 腎上腺髓質嗜鉻細胞瘤細胞株
    蛋白激酶 CK2
    血清反應因子
    骨髓細胞白血病-1
    抗細胞凋亡
    PC12 cells
    protein kinase CK2
    SRF
    Mcl-1
    anti-apoptosis
    日期: 2009
    上傳時間: 2010-12-08 02:00:37 (UTC+8)
    摘要: 蛋白質激酶 CK2 是一種多功能的絲胺酸／蘇胺酸蛋白激酶，且普遍存在於哺乳類動物細胞中，CK2 受質眾多，對於細胞週期的發展、轉錄作用以及抗細胞凋亡等過程中扮演很重要的角色。SRF 是一種哺乳類動物的轉錄因子，它會結合到血清反應元素 SRE 上進而調控一些促進細胞存活的基因轉錄作用。Mcl-1歸類於抗細胞凋亡 Bcl-2 家族，具有促進細胞存活的能力。過去研究顯示 SRF 的 DNA 結合活性會受到蛋白激酶 CK2 的磷酸化而增加，且 SRF 對 Mcl-1 的活性調控作用也被描述在其他的研究中，然而，對於細胞的訊息目前還沒有更詳細的研究。在本實驗中，我們探討是否可以藉由 CK2 調控 SRF 的路徑來影響 Mcl-1 的表現以作為抗細胞凋亡的機制。利用 CK2 抑制劑 TBB 處理的結果顯示，在 4 hr 後，phospho-SRF 蛋白質表現的降低具有劑量相關性。而相似的降低也可以從 Mcl-1 的 mRNA 和蛋白質表現量觀察到。處理 24 hr 後，phospho-SRF 的蛋白質表現量有顯著降低，而 Mcl-1 的 mRNA 表現量相較 Mcl-1 的蛋白質影響層面微弱。另一方面，轉染野生型 CK2α 會增加 phospho-SRF，相反的，轉染抑制催化活性的突變型 CK2αA156 則會顯著降低 phospho-SRF 的表現。更進一步，野生型 CK2α 同時增加 Mcl-1 的 mRNA 及蛋白質層級，而 CK2αA156 則會降低 Mcl-1 的表現。突變型的 SRF99A 轉染作用降低 Mcl-1 的 mRNA 及蛋白質，並經由共同轉染的實驗顯示具有抵抗上游野生型CK2α 對 Mcl-1 蛋白質的影響。綜合這些結果我們認為 CK2α對 SRF 的訊息調控影響包括對 Mcl-1 的表現。且這條訊息路徑所促進的 Mcl-1 蛋白質表現可能對魚藤酮處理所引發的細胞凋亡作用具有保護的效果。
    Protein kinase CK2 is a multifunctional serine/threonine protein kinase with many protein substrates and is ubiquitously expressed in mammalian cells to play an important role in cell cycle progression, transcription, and anti-apoptosis. The serum response factor (SRF) is a mammalian transcription factor which binds to serum response element (SRE) and mediates some gene transcriptions relevent to promote the cell survival. The Myeloid cell leukemia 1 (Mcl-1) belongs to the anti-apoptotic Bcl-2 family and its effect are involved in promoting cell viability. Previous studies have revealed that the DNA-binding activity of SRF is enhanced when it is phosphorylated by protein kinase CK2. The activation regulation of Mcl-1 by SRF has also been reported in other studies. However, the detailed cellular signaling has not been studied well. In the present study, we investigate whether the regulation of Mcl-1 expression through CK2-mediated SRF pathway is involved in its anti-apoptotic effects. The results from CK2 inhibitor TBB revealed that the phosphorylated SRF were reduced in a dose-dependent manner after 4 hr of TBB treatments in PC12 cells. The similar decreases were also observed in the mRNA and protein levels of Mcl-1. After a 24 hr exposure of PC12 cells to TBB, a decreased in phosphorylated SRF and Mcl-1 mRNA were observed; a decreased in Mcl-1 protein level was also detected, albeit to a lesser extent. On the other hand, transfection of the wildtype CK2α increased, whereas transfection of the catalytically inactive CK2αA156 mutant decreased phosphorylated SRF. Further, wildtype CK2α increased, whereas CK2αA156 mutant decreased the mRNA and protein levels of Mcl-1. Furthermore, the mutant SRF99A transfection decreased, the mRNA and protein levels of Mcl-1 and antagonized the up-regulatory effects of wildtype CK2α on Mcl-1 protein level in the co-transfection experiments. These results together suggest that CK2α-mediated SRF signaling is involved in the regulation of Mcl-1 expression, and this signaling pathway may involves the anti-apoptotic effects of Mcl-1 against rotenone treatment.
    參考文獻: Abbott KL, Renfrow MB, Chalmers MJ, Nguyen BD, Marshall AG, Legault P, Omichinski JG (2005) Enhanced binding of RNAP II CTD phosphatase FCP1 to RAP74 following CK2 phosphorylation. Biochemistry 44:2732-2745.
    Adrain C, Martin SJ (2001) The mitochondrial apoptosome: a killer unleashed by the cytochrome seas. Trends Biochem Sci 26:390-397.
    Allende JE, Allende CC (1995) Protein kinases. 4. Protein kinase CK2: an enzyme with multiple substrates and a puzzling regulation. FASEB J 9:313-323.
    Arbour N, Vanderluit JL, Le Grand JN, Jahani-Asl A, Ruzhynsky VA, Cheung EC, Kelly MA, MacKenzie AE, Park DS, Opferman JT, Slack RS (2008) Mcl-1 is a key regulator of apoptosis during CNS development and after DNA damage. J Neurosci 28:6068-6078.
    Arsenian S, Weinhold B, Oelgeschlager M, Ruther U, Nordheim A (1998) Serum response factor is essential for mesoderm formation during mouse embryogenesis. EMBO J 17:6289-6299.
    Bae J, Leo CP, Hsu SY, Hsueh AJ (2000) MCL-1S, a splicing variant of the antiapoptotic BCL-2 family member MCL-1, encodes a proapoptotic protein possessing only the BH3 domain. J Biol Chem 275:25255-25261.
    Belizario JE, Alves J, Garay-Malpartida M, Occhiucci JM (2008) Coupling caspase cleavage and proteasomal degradation of proteins carrying PEST motif. Curr Protein Pept Sci 9:210-220.
    Bingle CD, Craig RW, Swales BM, Singleton V, Zhou P, Whyte MK (2000) Exon skipping in Mcl-1 results in a bcl-2 homology domain 3 only gene product that promotes cell death. J Biol Chem 275:22136-22146.
    Birnbaum MJ, Glover VC (1991) The phosphotransferase activity of casein kinase II is required for its physiological function in vivo. Biochem Biophys Res Commun 181:524-528.
    Blanquet PR (1998) Neurotrophin-induced activation of casein kinase 2 in rat hippocampal slices. Neuroscience 86:739-749.
    Buchou T, Vernet M, Blond O, Jensen HH, Pointu H, Olsen BB, Cochet C, Issinger OG, Boldyreff B (2003) Disruption of the regulatory beta subunit of protein kinase CK2 in mice leads to a cell-autonomous defect and early embryonic lethality. Mol Cell Biol 23:908-915.
    Shi Y, Evans JE, Rock KL (2003) Molecular identification of a danger signal that alerts the immune system to dying cells. Nature 425:516-521.
    Shore P, Sharrocks AD (1995) The ETS-domain transcription factors Elk-1 and SAP-1 exhibit differential DNA binding specificities. Nucleic Acids Res 23:4698-4706.
    Snowden RT, Sun XM, Dyer MJ, Cohen GM (2003) Bisindolylmaleimide IX is a potent inducer of apoptosis in chronic lymphocytic leukaemic cells and activates cleavage of Mcl-1. Leukemia 17:1981-1989.
    Sommer H, Beltran JP, Huijser P, Pape H, Lonnig WE, Saedler H, Schwarz-Sommer Z (1990) Deficiens, a homeotic gene involved in the control of flower morphogenesis in Antirrhinum majus: the protein shows homology to transcription factors. EMBO J 9:605-613.
    Soulez M, Rouviere CG, Chafey P, Hentzen D, Vandromme M, Lautredou N, Lamb N, Kahn A, Tuil D (1996) Growth and differentiation of C2 myogenic cells are dependent on serum response factor. Mol Cell Biol 16:6065-6074.
    Stennicke HR, Salvesen GS (1998) Properties of the caspases. Biochim Biophys Acta 1387:17-31.
    Stennicke HR, Jurgensmeier JM, Shin H, Deveraux Q, Wolf BB, Yang X, Zhou Q, Ellerby HM, Ellerby LM, Bredesen D, Green DR, Reed JC, Froelich CJ, Salvesen GS (1998) Pro-caspase-3 is a major physiologic target of caspase-8. J Biol Chem 273:27084-27090.
    Tapia JC, Torres VA, Rodriguez DA, Leyton L, Quest AF (2006) Casein kinase 2 (CK2) increases survivin expression via enhanced beta-catenin-T cell factor/lymphoid enhancer binding factor-dependent transcription. Proc Natl Acad Sci U S A 103:15079-15084.
    Taylor RC, Cullen SP, Martin SJ (2008) Apoptosis: controlled demolition at the cellular level. Nat Rev Mol Cell Biol 9:231-241.
    Thompson CB (1995) Apoptosis in the pathogenesis and treatment of disease. Science 267:1456-1462.
    Burnett G, Kennedy EP (1954) The enzymatic phosphorylation of proteins. J Biol Chem 211:969-980.
    Timofeeva OA, Plisov S, Evseev AA, Peng S, Jose-Kampfner M, Lovvorn HN, Dome JS, Perantoni AO (2006) Serine-phosphorylated STAT1 is a prosurvival factor in Wilms` tumor pathogenesis. Oncogene 25:7555-7564.
    Townsend KJ, Zhou P, Qian L, Bieszczad CK, Lowrey CH, Yen A, Craig RW (1999) Regulation of MCL1 through a serum response factor/Elk-1-mediated mechanism links expression of a viability-promoting member of the BCL2 family to the induction of hematopoietic cell differentiation. J Biol Chem 274:1801-1813.
    Treisman R (1987) Identification and purification of a polypeptide that binds to the c-fos serum response element. EMBO J 6:2711-2717.
    Trinchieri G, Sher A (2007) Cooperation of Toll-like receptor signals in innate immune defence. Nat Rev Immunol 7:179-190.
    Tyan SW, Tsai MC, Lin CL, Ma YL, Lee EH (2008) Serum- and glucocorticoid-inducible kinase 1 enhances zif268 expression through the mediation of SRF and CREB1 associated with spatial memory formation. J Neurochem 105:820-832.
    Vickers ER, Kasza A, Kurnaz IA, Seifert A, Zeef LA, O`Donnell A, Hayes A, Sharrocks AD (2004) Ternary complex factor-serum response factor complex-regulated gene activity is required for cellular proliferation and inhibition of apoptotic cell death. Mol Cell Biol 24:10340-10351.
    Wang D, Westerheide SD, Hanson JL, Baldwin AS, Jr. (2000) Tumor necrosis factor alpha-induced phosphorylation of RelA/p65 on Ser529 is controlled by casein kinase II. J Biol Chem 275:32592-32597.
    Warr MR, Acoca S, Liu Z, Germain M, Watson M, Blanchette M, Wing SS, Shore GC (2005) BH3-ligand regulates access of MCL-1 to its E3 ligase. FEBS Lett 579:5603-5608.
    Williams JR, Little JB, Shipley WU (1974) Association of mammalian cell death with a specific endonucleolytic degradation of DNA. Nature 252:754-755.
    Willis SN, Adams JM (2005) Life in the balance: how BH3-only proteins induce apoptosis. Curr Opin Cell Biol 17:617-625.
    Cabrejos ME, Allende CC, Maldonado E (2004) Effects of phosphorylation by protein kinase CK2 on the human basal components of the RNA polymerase II transcription machinery. J Cell Biochem 93:2-10.
    Willis SN, Chen L, Dewson G, Wei A, Naik E, Fletcher JI, Adams JM, Huang DC (2005) Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins. Genes Dev 19:1294-1305.
    Wyllie AH, Kerr JF, Currie AR (1980) Cell death: the significance of apoptosis. Int Rev Cytol 68:251-306.
    Xu X, Toselli PA, Russell LD, Seldin DC (1999) Globozoospermia in mice lacking the casein kinase II alpha` catalytic subunit. Nat Genet 23:118-121.
    Yamaguchi Y, Wada T, Suzuki F, Takagi T, Hasegawa J, Handa H (1998) Casein kinase II interacts with the bZIP domains of several transcription factors. Nucleic Acids Res 26:3854-3861.
    Yamane K, Kinsella TJ (2005) CK2 inhibits apoptosis and changes its cellular localization following ionizing radiation. Cancer Res 65:4362-4367.
    Yang-Feng TL, Naiman T, Kopatz I, Eli D, Dafni N, Canaani D (1994) Assignment of the human casein kinase II alpha` subunit gene (CSNK2A1) to chromosome 16p13.2-p13.3. Genomics 19:173.
    Yang T, Kozopas KM, Craig RW (1995) The intracellular distribution and pattern of expression of Mcl-1 overlap with, but are not identical to, those of Bcl-2. J Cell Biol 128:1173-1184.
    Yang T, Buchan HL, Townsend KJ, Craig RW (1996) MCL-1, a member of the BLC-2 family, is induced rapidly in response to signals for cell differentiation or death, but not to signals for cell proliferation. J Cell Physiol 166:523-536.
    Zdunek M, Silbiger S, Lei J, Neugarten J (2001) Protein kinase CK2 mediates TGF-beta1-stimulated type IV collagen gene transcription and its reversal by estradiol. Kidney Int 60:2097-2108.
    Zipp F (2000) Apoptosis in multiple sclerosis. Cell Tissue Res 301:163-171.
    Chai J, Tarnawski AS (2002) Serum response factor: discovery, biochemistry, biological roles and implications for tissue injury healing. J Physiol Pharmacol 53:147-157.
    Chance B, Williams GR, Hollunger G (1963) Inhibition of electron and energy transfer in mitochondria. I. Effects of Amytal, thiopental, rotenone, progesterone, and methylene glycol. J Biol Chem 238:418-431.
    Chang SH, Poser S, Xia Z (2004) A novel role for serum response factor in neuronal survival. J Neurosci 24:2277-2285.
    Chao CC, Ma YL, Lee EH (2007) Protein kinase CK2 impairs spatial memory formation through differential cross talk with PI-3 kinase signaling: activation of Akt and inactivation of SGK1. J Neurosci 27:6243-6248.
    Chao CC, Chiang CH, Ma YL, Lee EH (2006) Molecular mechanism of the neurotrophic effect of GDNF on DA neurons: role of protein kinase CK2. Neurobiol Aging 27:105-118.
    Chao DT, Korsmeyer SJ (1998) BCL-2 family: regulators of cell death. Annu Rev Immunol 16:395-419.
    Chen CJ, Kono H, Golenbock D, Reed G, Akira S, Rock KL (2007) Identification of a key pathway required for the sterile inflammatory response triggered by dying cells. Nat Med 13:851-856.
    Cosmelli D, Antonelli M, Allende CC, Allende JE (1997) An inactive mutant of the alpha subunit of protein kinase CK2 that traps the regulatory CK2beta subunit. FEBS Lett 410:391-396.
    Craig RW (2002) MCL1 provides a window on the role of the BCL2 family in cell proliferation, differentiation and tumorigenesis. Leukemia 16:444-454.
    Creagh EM, Conroy H, Martin SJ (2003) Caspase-activation pathways in apoptosis and immunity. Immunol Rev 193:10-21.
    Cuconati A, Mukherjee C, Perez D, White E (2003) DNA damage response and MCL-1 destruction initiate apoptosis in adenovirus-infected cells. Genes Dev 17:2922-2932.
    Czabotar PE, Lee EF, van Delft MF, Day CL, Smith BJ, Huang DC, Fairlie WD, Hinds MG, Colman PM (2007) Structural insights into the degradation of Mcl-1 induced by BH3 domains. Proc Natl Acad Sci U S A 104:6217-6222.
    De Felice FG, Vieira MN, Bomfim TR, Decker H, Velasco PT, Lambert MP, Viola KL, Zhao WQ, Ferreira ST, Klein WL (2009) Protection of synapses against Alzheimer`s-linked toxins: insulin signaling prevents the pathogenic binding of Abeta oligomers. Proc Natl Acad Sci U S A 106:1971-1976.
    Desagher S, Osen-Sand A, Montessuit S, Magnenat E, Vilbois F, Hochmann A, Journot L, Antonsson B, Martinou JC (2001) Phosphorylation of bid by casein kinases I and II regulates its cleavage by caspase 8. Mol Cell 8:601-611.
    Di Maira G, Brustolon F, Tosoni K, Belli S, Kramer SD, Pinna LA, Ruzzene M (2008) Comparative analysis of CK2 expression and function in tumor cell lines displaying sensitivity vs. resistance to chemical induced apoptosis. Mol Cell Biochem 316:155-161.
    Enari M, Sakahira H, Yokoyama H, Okawa K, Iwamatsu A, Nagata S (1998) A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 391:43-50.
    Fadok VA, Voelker DR, Campbell PA, Cohen JJ, Bratton DL, Henson PM (1992) Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages. J Immunol 148:2207-2216.
    Fan MM, Zhang H, Hayden MR, Pelech SL, Raymond LA (2008) Protective up-regulation of CK2 by mutant huntingtin in cells co-expressing NMDA receptors. J Neurochem 104:790-805.
    Frank S, Gaume B, Bergmann-Leitner ES, Leitner WW, Robert EG, Catez F, Smith CL, Youle RJ (2001) The role of dynamin-related protein 1, a mediator of mitochondrial fission, in apoptosis. Dev Cell 1:515-525.
    Fritz G, Issinger OG, Olsen BB (2009) Selectivity analysis of protein kinase CK2 inhibitors DMAT, TBB and resorufin in cisplatin-induced stress responses. Int J Oncol 35:1151-1157.
    Gallucci S, Lolkema M, Matzinger P (1999) Natural adjuvants: endogenous activators of dendritic cells. Nat Med 5:1249-1255.
    Gauthier-Rouviere C, Vandromme M, Tuil D, Lautredou N, Morris M, Soulez M, Kahn A, Fernandez A, Lamb N (1996) Expression and activity of serum response factor is required for expression of the muscle-determining factor MyoD in both dividing and differentiating mouse C2C12 myoblasts. Mol Biol Cell 7:719-729.
    Gietz RD, Graham KC, Litchfield DW (1995) Interactions between the subunits of casein kinase II. J Biol Chem 270:13017-13021.
    Glover CV, 3rd (1998) On the physiological role of casein kinase II in Saccharomyces cerevisiae. Prog Nucleic Acid Res Mol Biol 59:95-133.
    Gotz C, Wagner P, Issinger OG, Montenarh M (1996) p21WAF1/CIP1 interacts with protein kinase CK2. Oncogene 13:391-398.
    Gotz C, Kartarius S, Scholtes P, Nastainczyk W, Montenarh M (1999) Identification of a CK2 phosphorylation site in mdm2. Eur J Biochem 266:493-501.
    Graham KC, Litchfield DW (2000) The regulatory beta subunit of protein kinase CK2 mediates formation of tetrameric CK2 complexes. J Biol Chem 275:5003-5010.
    Greene LA, Tischler AS (1976) Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor. Proc Natl Acad Sci U S A 73:2424-2428.
    Greenstein S, Ghias K, Krett NL, Rosen ST (2002) Mechanisms of glucocorticoid-mediated apoptosis in hematological malignancies. Clin Cancer Res 8:1681-1694.
    Guo C, Yu S, Davis AT, Wang H, Green JE, Ahmed K (2001) A potential role of nuclear matrix-associated protein kinase CK2 in protection against drug-induced apoptosis in cancer cells. J Biol Chem 276:5992-5999.
    Hebb AL, Moore CS, Bhan V, Campbell T, Fisk JD, Robertson HA, Thorne M, Lacasse E, Holcik M, Gillard J, Crocker SJ, Robertson GS (2008) Expression of the inhibitor of apoptosis protein family in multiple sclerosis reveals a potential immunomodulatory role during autoimmune mediated demyelination. Mult Scler 14:577-594.
    Heidenreich O, Neininger A, Schratt G, Zinck R, Cahill MA, Engel K, Kotlyarov A, Kraft R, Kostka S, Gaestel M, Nordheim A (1999) MAPKAP kinase 2 phosphorylates serum response factor in vitro and in vivo. J Biol Chem 274:14434-14443.
    Homma MK, Homma Y (2008) Cell cycle and activation of CK2. Mol Cell Biochem 316:49-55.
    Izeradjene K, Douglas L, Delaney A, Houghton JA (2004) Influence of casein kinase II in tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis in human rhabdomyosarcoma cells. Clin Cancer Res 10:6650-6660.
    Janknecht R, Nordheim A (1992) Elk-1 protein domains required for direct and SRF-assisted DNA-binding. Nucleic Acids Res 20:3317-3324.
    Johnson SA, Hunter T (2005) Kinomics: methods for deciphering the kinome. Nat Methods 2:17-25.
    Johnston IM, Allison SJ, Morton JP, Schramm L, Scott PH, White RJ (2002) CK2 forms a stable complex with TFIIIB and activates RNA polymerase III transcription in human cells. Mol Cell Biol 22:3757-3768.
    Karbowski M, Norris KL, Cleland MM, Jeong SY, Youle RJ (2006) Role of Bax and Bak in mitochondrial morphogenesis. Nature 443:658-662.
    Kato T, Jr., Delhase M, Hoffmann A, Karin M (2003) CK2 Is a C-Terminal IkappaB Kinase Responsible for NF-kappaB Activation during the UV Response. Mol Cell 12:829-839.
    Kawane K, Fukuyama H, Yoshida H, Nagase H, Ohsawa Y, Uchiyama Y, Okada K, Iida T, Nagata S (2003) Impaired thymic development in mouse embryos deficient in apoptotic DNA degradation. Nat Immunol 4:138-144.
    Keller DM, Lu H (2002) p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex. J Biol Chem 277:50206-50213.
    Kerr JF, Wyllie AH, Currie AR (1972) Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer 26:239-257.
    Kofler R (2000) The molecular basis of glucocorticoid-induced apoptosis of lymphoblastic leukemia cells. Histochem Cell Biol 114:1-7.
    Korn I, Jacob G, Allende CC, Allende JE (2001) The activity of CK2 in the extracts of COS-7 cells transfected with wild type and mutant subunits of protein kinase CK2. Mol Cell Biochem 227:37-44.
    Kozopas KM, Yang T, Buchan HL, Zhou P, Craig RW (1993) MCL1, a gene expressed in programmed myeloid cell differentiation, has sequence similarity to BCL2. Proc Natl Acad Sci U S A 90:3516-3520.
    Krajewski S, Bodrug S, Krajewska M, Shabaik A, Gascoyne R, Berean K, Reed JC (1995) Immunohistochemical analysis of Mcl-1 protein in human tissues. Differential regulation of Mcl-1 and Bcl-2 protein production suggests a unique role for Mcl-1 in control of programmed cell death in vivo. Am J Pathol 146:1309-1319.
    Lane JD, Lucocq J, Pryde J, Barr FA, Woodman PG, Allan VJ, Lowe M (2002) Caspase-mediated cleavage of the stacking protein GRASP65 is required for Golgi fragmentation during apoptosis. J Cell Biol 156:495-509.
    Lang AE, Langston JW, Stoessl AJ, Brodsky M, Brooks DJ, Dhawan V, Elias WJ, Lozano AM, Moro E, Nutt JG, Stacy M, Turner D, Wooten GF (2006) GDNF in treatment of Parkinson`s disease: response to editorial. Lancet Neurol 5:200-202.
    Li PF, Li J, Muller EC, Otto A, Dietz R, von Harsdorf R (2002) Phosphorylation by protein kinase CK2: a signaling switch for the caspase-inhibiting protein ARC. Mol Cell 10:247-258.
    Lin CY, Navarro S, Reddy S, Comai L (2006) CK2-mediated stimulation of Pol I transcription by stabilization of UBF-SL1 interaction. Nucleic Acids Res 34:4752-4766.
    Liu X, Zou H, Slaughter C, Wang X (1997) DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell 89:175-184.
    Livak KJ, Schmittgen TD (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 25:402-408.
    Lorenz P, Pepperkok R, Pyerin W (1994) Requirement of casein kinase 2 for entry into and progression through early phases of the cell cycle. Cell Mol Biol Res 40:519-527.
    Lorenz P, Pepperkok R, Ansorge W, Pyerin W (1993) Cell biological studies with monoclonal and polyclonal antibodies against human casein kinase II subunit beta demonstrate participation of the kinase in mitogenic signaling. J Biol Chem 268:2733-2739.
    Lou DY, Dominguez I, Toselli P, Landesman-Bollag E, O`Brien C, Seldin DC (2008) The alpha catalytic subunit of protein kinase CK2 is required for mouse embryonic development. Mol Cell Biol 28:131-139.
    Lynch JT, Rajendran R, Xenaki G, Berrou I, Demonacos C, Krstic-Demonacos M The role of glucocorticoid receptor phosphorylation in Mcl-1 and NOXA gene expression. Mol Cancer 9:38.
    Manak JR, Prywes R (1993) Phosphorylation of serum response factor by casein kinase II: evidence against a role in growth factor regulation of fos expression. Oncogene 8:703-711.
    Marais RM, Hsuan JJ, McGuigan C, Wynne J, Treisman R (1992) Casein kinase II phosphorylation increases the rate of serum response factor-binding site exchange. EMBO J 11:97-105.
    Martin SJ, Reutelingsperger CP, McGahon AJ, Rader JA, van Schie RC, LaFace DM, Green DR (1995) Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: inhibition by overexpression of Bcl-2 and Abl. J Exp Med 182:1545-1556.
    Masuoka HC, Mott J, Bronk SF, Werneburg NW, Akazawa Y, Kaufmann SH, Gores GJ (2009) Mcl-1 degradation during hepatocyte lipoapoptosis. J Biol Chem 284:30039-30048.
    Meggio F, Pinna LA (2003) One-thousand-and-one substrates of protein kinase CK2? FASEB J 17:349-368.
    Meggio F, Boldyreff B, Issinger OG, Pinna LA (1994) Casein kinase 2 down-regulation and activation by polybasic peptides are mediated by acidic residues in the 55-64 region of the beta-subunit. A study with calmodulin as phosphorylatable substrate. Biochemistry 33:4336-4342.
    Mohun T, Garrett N, Treisman R (1987) Xenopus cytoskeletal actin and human c-fos gene promoters share a conserved protein-binding site. EMBO J 6:667-673.
    Nicholson DW (1999) Caspase structure, proteolytic substrates, and function during apoptotic cell death. Cell Death Differ 6:1028-1042.
    Nijhawan D, Fang M, Traer E, Zhong Q, Gao W, Du F, Wang X (2003) Elimination of Mcl-1 is required for the initiation of apoptosis following ultraviolet irradiation. Genes Dev 17:1475-1486.
    Norman C, Runswick M, Pollock R, Treisman R (1988) Isolation and properties of cDNA clones encoding SRF, a transcription factor that binds to the c-fos serum response element. Cell 55:989-1003.
    Oishi K, Kamakura S, Isazawa Y, Yoshimatsu T, Kuida K, Nakafuku M, Masuyama N, Gotoh Y (2004) Notch promotes survival of neural precursor cells via mechanisms distinct from those regulating neurogenesis. Dev Biol 276:172-184.
    Opferman JT, Letai A, Beard C, Sorcinelli MD, Ong CC, Korsmeyer SJ (2003) Development and maintenance of B and T lymphocytes requires antiapoptotic MCL-1. Nature 426:671-676.
    Opferman JT, Iwasaki H, Ong CC, Suh H, Mizuno S, Akashi K, Korsmeyer SJ (2005) Obligate role of anti-apoptotic MCL-1 in the survival of hematopoietic stem cells. Science 307:1101-1104.
    Oppenheim JJ, Yang D (2005) Alarmins: chemotactic activators of immune responses. Curr Opin Immunol 17:359-365.
    Palancade B, Dubois MF, Bensaude O (2002) FCP1 phosphorylation by casein kinase 2 enhances binding to TFIIF and RNA polymerase II carboxyl-terminal domain phosphatase activity. J Biol Chem 277:36061-36067.
    Panova TB, Panov KI, Russell J, Zomerdijk JC (2006) Casein kinase 2 associates with initiation-competent RNA polymerase I and has multiple roles in ribosomal DNA transcription. Mol Cell Biol 26:5957-5968.
    Pearse RN, Swendeman SL, Li Y, Rafii D, Hempstead BL (2005) A neurotrophin axis in myeloma: TrkB and BDNF promote tumor-cell survival. Blood 105:4429-4436.
    Pelfrey CM, Tranquill LR, Boehme SA, McFarland HF, Lenardo MJ (1995) Two mechanisms of antigen-specific apoptosis of myelin basic protein (MBP)-specific T lymphocytes derived from multiple sclerosis patients and normal individuals. J Immunol 154:6191-6202.
    Pepperkok R, Lorenz P, Ansorge W, Pyerin W (1994) Casein kinase II is required for transition of G0/G1, early G1, and G1/S phases of the cell cycle. J Biol Chem 269:6986-6991.
    Peraldi P, Scimeca JC, Filloux C, Van Obberghen E (1993) Regulation of extracellular signal-regulated protein kinase-1 (ERK-1; pp44/mitogen-activated protein kinase) by epidermal growth factor and nerve growth factor in PC12 cells: implication of ERK1 inhibitory activities. Endocrinology 132:2578-2585.
    Ploner C, Schmidt S, Presul E, Renner K, Schrocksnadel K, Rainer J, Riml S, Kofler R (2005) Glucocorticoid-induced apoptosis and glucocorticoid resistance in acute lymphoblastic leukemia. J Steroid Biochem Mol Biol 93:153-160.
    Puthier D, Derenne S, Barille S, Moreau P, Harousseau JL, Bataille R, Amiot M (1999) Mcl-1 and Bcl-xL are co-regulated by IL-6 in human myeloma cells. Br J Haematol 107:392-395.
    Rinkenberger JL, Horning S, Klocke B, Roth K, Korsmeyer SJ (2000) Mcl-1 deficiency results in peri-implantation embryonic lethality. Genes Dev 14:23-27.
    Rivera VM, Miranti CK, Misra RP, Ginty DD, Chen RH, Blenis J, Greenberg ME (1993) A growth factor-induced kinase phosphorylates the serum response factor at a site that regulates its DNA-binding activity. Mol Cell Biol 13:6260-6273.
    Rollins BJ, Stiles CD (1989) Serum-inducible genes. Adv Cancer Res 53:1-32.
    Rudner J, Elsaesser SJ, Muller AC, Belka C, Jendrossek V Differential effects of anti-apoptotic Bcl-2 family members Mcl-1, Bcl-2, and Bcl-xL on celecoxib-induced apoptosis. Biochem Pharmacol 79:10-20.
    Sakahira H, Enari M, Nagata S (1998) Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis. Nature 391:96-99.
    Sarno S, Reddy H, Meggio F, Ruzzene M, Davies SP, Donella-Deana A, Shugar D, Pinna LA (2001) Selectivity of 4,5,6,7-tetrabromobenzotriazole, an ATP site-directed inhibitor of protein kinase CK2 (`casein kinase-2`). FEBS Lett 496:44-48.
    Scaffidi P, Misteli T, Bianchi ME (2002) Release of chromatin protein HMGB1 by necrotic cells triggers inflammation. Nature 418:191-195.
    Sheng M, Dougan ST, McFadden G, Greenberg ME (1988) Calcium and growth factor pathways of c-fos transcriptional activation require distinct upstream regulatory sequences. Mol Cell Biol 8:2787-2796.
    Sherr CJ, McCormick F (2002) The RB and p53 pathways in cancer. Cancer Cell 2:103-112.
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