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研究生:張珮瑜
研究生(外文):Pei-Yu Chang
論文名稱:探討與大鼠Eag1(Ether-a`-go-go1)鉀離子通道相互作用之蛋白質
論文名稱(外文):Characterization of the Interaction between rEag1 (rat Ether-a`-go-go 1) and rEag1-interacting Proteins
指導教授:鄭瓊娟
指導教授(外文):Chung-Jiuan Jeng
學位類別:碩士
校院名稱:國立陽明大學
系所名稱:解剖暨細胞生物學研究所
學門:醫藥衛生學門
學類:醫學學類
論文種類:學術論文
論文出版年:2009
畢業學年度:97
語文別:中文
論文頁數:59
中文關鍵詞:大鼠Eag1 (Ether-a`-go-go 1) 鉀離子通
外文關鍵詞:rEag1 (rat Ether-a`-go-go 1)
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Eag (ether-`a-go-go) 鉀離子通道屬於神經細胞特有 (neuron-specific) 的電位控制 (voltaged-gated) 鉀離子通道,在大腦中有高度表現,在大鼠Eag鉀離子通道有兩種isoforms:rEag1和rEag2。藉由目前已知與Eag鉀離子通道有相互作用的蛋白質,發現這些蛋白質會去調控Eag鉀離子通道的活性,而也有研究指出Eag會參與調控細胞內訊息傳遞路徑,但對於在神經細胞上,Eag所扮演的角色仍有很多未知。藉由蛋白質與蛋白質之間的作用 (protein-protein interaction) 了解與rEag1有相互作用之蛋白質,並透過這些已知的蛋白質在細胞內所參與之功能,進一步推測rEag1可能參與之角色。本篇論文主要探討我們實驗室經由酵母菌雙雜交系統 (Yeast two-hybrid system) 所發現與rEag1位於細胞質內的N端有相互作用之蛋白質,而我針對138個可能蛋白質,做更進一步篩選,最後經實驗挑選出六個蛋白質:N-ethylmaleimide sensitive factor (NSF)、14-3-3蛋白質、Phocein、Prefoldin 2 (PFD2)、M Phase Phosphoproteins 8 (MPP8)、myosin heavy chain 7b (Myh7b),利用共同免疫沉澱分析實驗、GST pull-dowm實驗與免疫螢光染色等,探討與rEag1是否具有相互作用。
由共同免疫沉澱分析實驗、GST pull-dowm實驗結果顯示,NSF與14-3-3蛋白質能在共同免疫沉澱實驗中,將rEag1沉澱下來,另外,在GST pull-down實驗中,觀察到GST-N207可以將NSF與14-3-3沉澱下來,在這兩個實驗結果顯示rEag1位於細胞質內的N端區域和NSF、14-3-3有相互作用。以免疫螢光染色實驗檢測表達在HEK293T細胞株之14-3-3與rEag1的分佈位置,結果顯示14-3-3與rEag1在細胞膜的部分區域有重疊現象,更進一步證明14-3-3與rEag1之間相互作用的可能性。未來可結合電生理實驗,探討14-3-3或NSF是否會影響rEag1的電生理特性,或者是會影響rEag1表現在細胞膜的運送機制。而其餘的四個蛋白質Phocein、PFD2、MPP8、Myh7b,在共同免疫沉澱實驗中,並無法證實這些蛋白質與rEag1有相互作用關係,未來可經由改善共同免疫沉澱的方式,再次驗證。
The ether-`a-go-go (Eag) potassium channel belongs to the superfamily of voltage-gated potassium channel. Eag is a neuron-specific protein and is widely expressed in various regions of the brain. In the rat brain, there are two isoforms of Eag K+ channel, rat Eag1 (rEag1) and rat Eag2 (rEag2). Eag-interacting proteins identified so far mostly are involved in regulating the gating property of Eag potassium channels. In addition, ectopically expressed Eag in tumor cells has been suggested to modulate signaling pathways related to cell proliferation. So far the physiological role of Eag in neurons remains obscure. We aim to identify rEag1-interacting proteins by performing yeast two-hybrid screening of the rat brain cDNA library, which will lead to more insight into the function of rEag1 potassium channels. Previously our laboratory has identified 138 proteins that can potentially interact with the N-terminus of rEag1 proteins. After bioinformatic analysis, we focused on 6 potential candidates of rEag1-interacting proteins: N-ethylmaleimide sensitive factor (NSF), 14-3-3, Phocein, Prefoldin 2 (PFD2), M Phase Phosphoproteins 8 (MPP8), and myosin heavy chain 7b (Myh7b), for further characterization. We performed experiments of co-immunoprecipitation, GST pull-down assay, and immunofluorescence to verify the interaction between rEag1 and potential candidates of rEag1-interacting proteins.
The results of the co-immunoprecipitation revealed that both NSF and 14-3-3 could be co-immunoprecipitated with rEag1. Moreover, both NSF and 14-3-3 can be pulled down by GST fusion proteins with the N-terminus of rEag1 (GST-N207) in the GST pull-down experiment, suggesting that the N-terminus of rEag1 interacts with NSF and 14-3-3 proteins. Immunofluorescent staining showed that the immunoreactivities of 14-3-3 and rEag1 were co-localized at some portions of the plasma membrane in trasfected HEK293T cells, further supporting the possibility of interaction between rEag1 and 14-3-3 proteins in mammalian cells. In the future, we can use electrophysiological techniques to examine whether 14-3-3 and NSF affects the biophysical properties of rEag1 or involve in the process of the membrane trafficking of rEag1. Although our current co-immunoprecipitation fail to demonstrate a direct interaction between rEag1 and the other 4 candidate proteins (Phocein, PFD2, MPP8, and Myh7b), in the future we may attempt to modify the condition of the co-immunoprecipitation experiment to re-examine this issue.
目錄………………………………………………………………………………… i
圖次………………………………………………………………………………… ii
中文摘要…………………………………………………………………………… iii
英文摘要…………………………………………………………………………… v
第一章 導論 ……………………………………………………………………… 1
第二章 材料與方法 ……………………………………………………………… 10
第三章 結果 ……………………………………………………………………… 20
第四章 圖片與圖片說明 ………………………………………………………… 26
第五章 討論 ……………………………………………………………………… 36
參考文獻…………………………………………………………………………… 43
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Bracey K, Ju M, Tian C, Stevens L, Wray D (2008) Tubulin as a binding partner of the heag2 voltage-gated potassium channel. J Membr Biol 222:115-125.
Broughton SJ, Kitamoto T, Greenspan RJ (2004) Excitatory and inhibitory switches for courtship in the brain of Drosophila melanogaster. Curr Biol 14:538-547.
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Coetzee WA, Amarillo Y, Chiu J, Chow A, Lau D, McCormack T, Moreno H, Nadal MS, Ozaita A, Pountney D, Saganich M, Vega-Saenz de Miera E, Rudy B (1999) Molecular diversity of K+ channels. Ann N Y Acad Sci 868:233-285.
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Kamisago M, Schmitt JP, McNamara D, Seidman C, Seidman JG (2006) Sarcomere protein gene mutations and inherited heart disease: a beta-cardiac myosin heavy chain mutation causing endocardial fibroelastosis and heart failure. Novartis Found Symp 274:176-189; discussion 189-195, 272-176.
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Baillat G, Gaillard S, Castets F, Monneron A (2002) Interactions of phocein with nucleoside-diphosphate kinase, Eps15, and Dynamin I. J Biol Chem 277:18961-18966.
Baillat G, Moqrich A, Castets F, Baude A, Bailly Y, Benmerah A, Monneron A (2001) Molecular cloning and characterization of phocein, a protein found from the Golgi complex to dendritic spines. Mol Biol Cell 12:663-673.
Barinaga M (1999) New clues to how proteins link up to run the cell. Science 283:1247, 1249.
Bauer CK, Schwarz JR (2001) Physiology of EAG K+ channels. J Membr Biol 182:1-15.
Block MR, Glick BS, Wilcox CA, Wieland FT, Rothman JE (1988) Purification of an N-ethylmaleimide-sensitive protein catalyzing vesicular transport. Proc Natl Acad Sci U S A 85:7852-7856.
Borowiec AS, Hague F, Harir N, Guenin S, Guerineau F, Gouilleux F, Roudbaraki M, Lassoued K, Ouadid-Ahidouch H (2007) IGF-1 activates hEAG K(+) channels through an Akt-dependent signaling pathway in breast cancer cells: role in cell proliferation. J Cell Physiol 212:690-701.
Bracey K, Ju M, Tian C, Stevens L, Wray D (2008) Tubulin as a binding partner of the heag2 voltage-gated potassium channel. J Membr Biol 222:115-125.
Broughton SJ, Kitamoto T, Greenspan RJ (2004) Excitatory and inhibitory switches for courtship in the brain of Drosophila melanogaster. Curr Biol 14:538-547.
Chandy KG, Wulff H, Beeton C, Pennington M, Gutman GA, Cahalan MD (2004) K+ channels as targets for specific immunomodulation. Trends Pharmacol Sci 25:280-289.
Choe S (2002) Potassium channel structures. Nat Rev Neurosci 3:115-121.
Coetzee WA, Amarillo Y, Chiu J, Chow A, Lau D, McCormack T, Moreno H, Nadal MS, Ozaita A, Pountney D, Saganich M, Vega-Saenz de Miera E, Rudy B (1999) Molecular diversity of K+ channels. Ann N Y Acad Sci 868:233-285.
Demo SD, Yellen G (1991) The inactivation gate of the Shaker K+ channel behaves like an open-channel blocker. Neuron 7:743-753.
Doyle DA, Morais Cabral J, Pfuetzner RA, Kuo A, Gulbis JM, Cohen SL, Chait BT, MacKinnon R (1998) The structure of the potassium channel: molecular basis of K+ conduction and selectivity. Science 280:69-77.
Fadool DA, Tucker K, Perkins R, Fasciani G, Thompson RN, Parsons AD, Overton JM, Koni PA, Flavell RA, Kaczmarek LK (2004) Kv1.3 channel gene-targeted deletion produces "Super-Smeller Mice" with altered glomeruli, interacting scaffolding proteins, and biophysics. Neuron 41:389-404.
Fanger CM, Ghanshani S, Logsdon NJ, Rauer H, Kalman K, Zhou J, Beckingham K, Chandy KG, Cahalan MD, Aiyar J (1999) Calmodulin mediates calcium-dependent activation of the intermediate conductance KCa channel, IKCa1. J Biol Chem 274:5746-5754.
Flynn GE, Johnson JP, Jr., Zagotta WN (2001) Cyclic nucleotide-gated channels: shedding light on the opening of a channel pore. Nat Rev Neurosci 2:643-651.
Fu H, Subramanian RR, Masters SC (2000) 14-3-3 proteins: structure, function, and regulation. Annu Rev Pharmacol Toxicol 40:617-647.
Ganetzky B, Robertson GA, Wilson GF, Trudeau MC, Titus SA (1999) The eag family of K+ channels in Drosophila and mammals. Ann N Y Acad Sci 868:356-369.
Gilles-Gonzalez MA, Gonzalez G (2004) Signal transduction by heme-containing PAS-domain proteins. J Appl Physiol 96:774-783.
Guy HR, Seetharamulu P (1986) Molecular model of the action potential sodium channel. Proc Natl Acad Sci U S A 83:508-512.
Hegle AP, Marble DD, Wilson GF (2006) A voltage-driven switch for ion-independent signaling by ether-a-go-go K+ channels. Proc Natl Acad Sci U S A 103:2886-2891.
Hille B (2001) Ionic Channels of Excitable Membranes, 2nd Ed.
Hoffman EC, Reyes H, Chu FF, Sander F, Conley LH, Brooks BA, Hankinson O (1991) Cloning of a factor required for activity of the Ah (dioxin) receptor. Science 252:954-958.
Hoglund M, Siden T, Rohme D (1992) The isolation of evolutionarily conserved Eag I end-clones from mouse chromosome 17 using cloned DNA. DNA Cell Biol 11:613-619.
Jeng CJ, Chang CC, Tang CY (2005) Differential localization of rat Eag1 and Eag2 K+ channels in hippocampal neurons. Neuroreport 16:229-233.
Jenke M, Sanchez A, Monje F, Stuhmer W, Weseloh RM, Pardo LA (2003) C-terminal domains implicated in the functional surface expression of potassium channels. Embo J 22:395-403.
Jow GM, Jeng CJ (2008) Differential localization of rat Eag1 and Eag2 potassium channels in the retina. Neurosci Lett 431:12-16.
Kaczmarek LK (2006) Non-conducting functions of voltage-gated ion channels. Nat Rev Neurosci 7:761-771.
Kagan A, Melman YF, Krumerman A, McDonald TV (2002) 14-3-3 amplifies and prolongs adrenergic stimulation of HERG K+ channel activity. Embo J 21:1889-1898.
Kamisago M, Schmitt JP, McNamara D, Seidman C, Seidman JG (2006) Sarcomere protein gene mutations and inherited heart disease: a beta-cardiac myosin heavy chain mutation causing endocardial fibroelastosis and heart failure. Novartis Found Symp 274:176-189; discussion 189-195, 272-176.
Kaplan WD, Trout WE, 3rd (1969) The behavior of four neurological mutants of Drosophila. Genetics 61:399-409.
Lesage F, Reyes R, Fink M, Duprat F, Guillemare E, Lazdunski M (1996) Dimerization of TWIK-1 K+ channel subunits via a disulfide bridge. Embo J 15:6400-6407.
Li Y, Wu Y, Zhou Y (2006) Modulation of inactivation properties of CaV2.2 channels by 14-3-3 proteins. Neuron 51:755-771.
Ludwig J, Owen D, Pongs O (1997) Carboxy-terminal domain mediates assembly of the voltage-gated rat ether-a-go-go potassium channel. Embo J 16:6337-6345.
Ludwig J, Weseloh R, Karschin C, Liu Q, Netzer R, Engeland B, Stansfeld C, Pongs O (2000) Cloning and functional expression of rat eag2, a new member of the ether-a-go-go family of potassium channels and comparison of its distribution with that of eag1. Mol Cell Neurosci 16:59-70.
Marble DD, Hegle AP, Snyder ED, 2nd, Dimitratos S, Bryant PJ, Wilson GF (2005) Camguk/CASK enhances Ether-a-go-go potassium current by a phosphorylation-dependent mechanism. J Neurosci 25:4898-4907.
Martin-Benito J, Boskovic J, Gomez-Puertas P, Carrascosa JL, Simons CT, Lewis SA, Bartolini F, Cowan NJ, Valpuesta JM (2002) Structure of eukaryotic prefoldin and of its complexes with unfolded actin and the cytosolic chaperonin CCT. Embo J 21:6377-6386.
Martin S, Lino de Oliveira C, Mello de Queiroz F, Pardo LA, Stuhmer W, Del Bel E (2008) Eag1 potassium channel immunohistochemistry in the CNS of adult rat and selected regions of human brain. Neuroscience 155:833-844.
Matsumoto-Taniura N, Pirollet F, Monroe R, Gerace L, Westendorf JM (1996) Identification of novel M phase phosphoproteins by expression cloning. Mol Biol Cell 7:1455-1469.
Meyer R, Schonherr R, Gavrilova-Ruch O, Wohlrab W, Heinemann SH (1999) Identification of ether a go-go and calcium-activated potassium channels in human melanoma cells. J Membr Biol 171:107-115.
Napp J, Monje F, Stuhmer W, Pardo LA (2005) Glycosylation of Eag1 (Kv10.1) potassium channels: intracellular trafficking and functional consequences. J Biol Chem 280:29506-29512.
Nishimune A, Isaac JT, Molnar E, Noel J, Nash SR, Tagaya M, Collingridge GL, Nakanishi S, Henley JM (1998) NSF binding to GluR2 regulates synaptic transmission. Neuron 21:87-97.
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