請用此 Handle URI 來引用此文件:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/18117
完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 湯志永(Chih-Yung Tang) | |
dc.contributor.author | Yi-Jheng Peng | en |
dc.contributor.author | 彭怡錚 | zh_TW |
dc.date.accessioned | 2021-06-08T00:51:43Z | - |
dc.date.copyright | 2015-09-25 | |
dc.date.issued | 2014 | |
dc.date.submitted | 2015-06-29 | |
dc.identifier.citation | Alberti S, Bohse K, Arndt V, Schmitz A, Hohfeld J (2004) The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator. Molecular biology of the cell 15:4003-4010. Apaja PM, Foo B, Okiyoneda T, Valinsky WC, Barriere H, Atanasiu R, Ficker E, Lukacs GL, Shrier A (2013) Ubiquitination-dependent quality control of hERG K+ channel with acquired and inherited conformational defect at the plasma membrane. Molecular biology of the cell 24:3787-3804. Araki T, Milbrandt J (2003) ZNRF proteins constitute a family of presynaptic E3 ubiquitin ligases. The Journal of neuroscience : the official journal of the Society for Neuroscience 23:9385-9394. Arias E, Cuervo AM (2011) Chaperone-mediated autophagy in protein quality control. Current opinion in cell biology 23:184-189. Arndt V, Rogon C, Hohfeld J (2007) To be, or not to be--molecular chaperones in protein degradation. Cellular and molecular life sciences : CMLS 64:2525-2541. Arndt V, Daniel C, Nastainczyk W, Alberti S, Hohfeld J (2005) BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP. Molecular biology of the cell 16:5891-5900. Arndt V, Dick N, Tawo R, Dreiseidler M, Wenzel D, Hesse M, Furst DO, Saftig P, Saint R, Fleischmann BK, Hoch M, Hohfeld J (2010) Chaperone-assisted selective autophagy is essential for muscle maintenance. Current biology : CB 20:143-148. Bai X, Ma D, Liu A, Shen X, Wang QJ, Liu Y, Jiang Y (2007) Rheb activates mTOR by antagonizing its endogenous inhibitor, FKBP38. Science 318:977-980. Balch WE, Morimoto RI, Dillin A, Kelly JW (2008) Adapting proteostasis for disease intervention. Science 319:916-919. Banasavadi-Siddegowda YK, Mai J, Fan Y, Bhattacharya S, Giovannucci DR, Sanchez ER, Fischer G, Wang X (2011) FKBP38 peptidylprolyl isomerase promotes the folding of cystic fibrosis transmembrane conductance regulator in the endoplasmic reticulum. The Journal of biological chemistry 286:43071-43080. Barth S, Edlich F, Berchner-Pfannschmidt U, Gneuss S, Jahreis G, Hasgall PA, Fandrey J, Wenger RH, Camenisch G (2009) Hypoxia-inducible factor prolyl-4-hydroxylase PHD2 protein abundance depends on integral membrane anchoring of FKBP38. The Journal of biological chemistry 284:23046-23058. Barth S, Nesper J, Hasgall PA, Wirthner R, Nytko KJ, Edlich F, Katschinski DM, Stiehl DP, Wenger RH, Camenisch G (2007) The peptidyl prolyl cis/trans isomerase FKBP38 determines hypoxia-inducible transcription factor prolyl-4-hydroxylase PHD2 protein stability. Molecular and cellular biology 27:3758-3768. Bretag AH (1987) Muscle chloride channels. Physiological reviews 67:618-724. Buchberger A, Bukau B, Sommer T (2010) Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms. Molecular cell 40:238-252. Bukau B, Horwich AL (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92:351-366. Bulgakov OV, Eggenschwiler JT, Hong DH, Anderson KV, Li T (2004) FKBP8 is a negative regulator of mouse sonic hedgehog signaling in neural tissues. Development (Cambridge, England) 131:2149-2159. Chanoux RA, Robay A, Shubin CB, Kebler C, Suaud L, Rubenstein RC (2012) Hsp70 promotes epithelial sodium channel functional expression by increasing its association with coat complex II and its exit from endoplasmic reticulum. The Journal of biological chemistry 287:19255-19265. Chen MF, Niggeweg R, Iaizzo PA, Lehmann-Horn F, Jockusch H (1997) Chloride conductance in mouse muscle is subject to post-transcriptional compensation of the functional Cl- channel 1 gene dosage. The Journal of physiology 504 ( Pt 1):75-81. Chen S, Smith DF (1998) Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery. The Journal of biological chemistry 273:35194-35200. Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annual review of biochemistry 75:333-366. Cho A, Ko HW, Eggenschwiler JT (2008) FKBP8 cell-autonomously controls neural tube patterning through a Gli2- and Kif3a-dependent mechanism. Developmental biology 321:27-39. Choi BH, Feng L, Yoon HS (2010) FKBP38 protects Bcl-2 from caspase-dependent degradation. The Journal of biological chemistry 285:9770-9779. Cooper G (2000) Protein Degradation. In: The Cell: A Molecular Approach, 2nd Edition. Sunderland (MA): Sinauer Associates. Coppinger JA, Hutt DM, Razvi A, Koulov AV, Pankow S, Yates JR, 3rd, Balch WE (2012) A chaperone trap contributes to the onset of cystic fibrosis. PloS one 7:e37682. Deutsch C (2002) Potassium channel ontogeny. Annual review of physiology 64:19-46. Ditzel L, Lowe J, Stock D, Stetter KO, Huber H, Huber R, Steinbacher S (1998) Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell 93:125-138. Donnelly BF, Needham PG, Snyder AC, Roy A, Khadem S, Brodsky JL, Subramanya AR (2013) Hsp70 and Hsp90 multichaperone complexes sequentially regulate thiazide-sensitive cotransporter endoplasmic reticulum-associated degradation and biogenesis. The Journal of biological chemistry 288:13124-13135. DuBridge RB, Tang P, Hsia HC, Leong PM, Miller JH, Calos MP (1987) Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system. Molecular and cellular biology 7:379-387. Eaton DC, Malik B, Bao HF, Yu L, Jain L (2010) Regulation of epithelial sodium channel trafficking by ubiquitination. Proceedings of the American Thoracic Society 7:54-64. Edlich F, Fischer G (2006) Pharmacological targeting of catalyzed protein folding: the example of peptide bond cis/trans isomerases. Handbook of experimental pharmacology:359-404. Edlich F, Erdmann F, Jarczowski F, Moutty MC, Weiwad M, Fischer G (2007a) The Bcl-2 regulator FKBP38-calmodulin-Ca2+ is inhibited by Hsp90. The Journal of biological chemistry 282:15341-15348. Edlich F, Weiwad M, Erdmann F, Fanghanel J, Jarczowski F, Rahfeld JU, Fischer G (2005) Bcl-2 regulator FKBP38 is activated by Ca2+/calmodulin. The EMBO journal 24:2688-2699. Edlich F, Maestre-Martinez M, Jarczowski F, Weiwad M, Moutty MC, Malesevic M, Jahreis G, Fischer G, Lucke C (2007b) A novel calmodulin-Ca2+ target recognition activates the Bcl-2 regulator FKBP38. The Journal of biological chemistry 282:36496-36504. Ellis RJ, Minton AP (2006) Protein aggregation in crowded environments. Biological chemistry 387:485-497. Erlejman AG, Lagadari M, Toneatto J, Piwien-Pilipuk G, Galigniana MD (2014) Regulatory role of the 90-kDa-heat-shock protein (Hsp90) and associated factors on gene expression. Biochimica et biophysica acta 1839:71-87. Estevez R, Jentsch TJ (2002) CLC chloride channels: correlating structure with function. Current opinion in structural biology 12:531-539. Farinha CM, Nogueira P, Mendes F, Penque D, Amaral MD (2002) The human DnaJ homologue (Hdj)-1/heat-shock protein (Hsp) 40 co-chaperone is required for the in vivo stabilization of the cystic fibrosis transmembrane conductance regulator by Hsp70. The Biochemical journal 366:797-806. Ficker E, Dennis AT, Wang L, Brown AM (2003) Role of the cytosolic chaperones Hsp70 and Hsp90 in maturation of the cardiac potassium channel HERG. Circulation research 92:e87-100. Frydman J (2001) Folding of newly translated proteins in vivo: the role of molecular chaperones. Annual review of biochemistry 70:603-647. Fukuyo Y, Hunt CR, Horikoshi N (2010) Geldanamycin and its anti-cancer activities. Cancer letters 290:24-35. Fuller W, Cuthbert AW (2000) Post-translational disruption of the delta F508 cystic fibrosis transmembrane conductance regulator (CFTR)-molecular chaperone complex with geldanamycin stabilizes delta F508 CFTR in the rabbit reticulocyte lysate. The Journal of biological chemistry 275:37462-37468. Gao Y, Yechikov S, Vazquez AE, Chen D, Nie L (2013a) Impaired surface expression and conductance of the KCNQ4 channel lead to sensorineural hearing loss. Journal of cellular and molecular medicine 17:889-900. Gao Y, Yechikov S, Vazquez AE, Chen D, Nie L (2013b) Distinct roles of molecular chaperones HSP90alpha and HSP90beta in the biogenesis of KCNQ4 channels. PloS one 8:e57282. Goldfarb SB, Kashlan OB, Watkins JN, Suaud L, Yan W, Kleyman TR, Rubenstein RC (2006) Differential effects of Hsc70 and Hsp70 on the intracellular trafficking and functional expression of epithelial sodium channels. Proceedings of the National Academy of Sciences of the United States of America 103:5817-5822. Gong Y, Kakihara Y, Krogan N, Greenblatt J, Emili A, Zhang Z, Houry WA (2009) An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell. Molecular systems biology 5:275. Gothel SF, Marahiel MA (1999) Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts. Cellular and molecular life sciences : CMLS 55:423-436. Guo J, Wang T, Li X, Shallow H, Yang T, Li W, Xu J, Fridman MD, Yang X, Zhang S (2012) Cell surface expression of human ether-a-go-go-related gene (hERG) channels is regulated by caveolin-3 protein via the ubiquitin ligase Nedd4-2. The Journal of biological chemistry 287:33132-33141. Gutsche I, Essen LO, Baumeister W (1999) Group II chaperonins: new TRiC(k)s and turns of a protein folding machine. Journal of molecular biology 293:295-312. Hansen WJ, Cowan NJ, Welch WJ (1999) Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins. The Journal of cell biology 145:265-277. Harst A, Lin H, Obermann WM (2005) Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation. The Biochemical journal 387:789-796. Hartl FU (1996) Molecular chaperones in cellular protein folding. Nature 381:571-579. Hartl FU, Hayer-Hartl M (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295:1852-1858. Hartl FU, Bracher A, Hayer-Hartl M (2011) Molecular chaperones in protein folding and proteostasis. Nature 475:324-332. Hernandez MP, Sullivan WP, Toft DO (2002) The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex. The Journal of biological chemistry 277:38294-38304. Hershko A, Ciechanover A (1998) The ubiquitin system. Annual review of biochemistry 67:425-479. Hessling M, Richter K, Buchner J (2009) Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90. Nature structural molecular biology 16:287-293. High S (1995) Protein translocation at the membrane of the endoplasmic reticulum. Progress in Biophysics and Molecular Biology 63:233-250. Hinzpeter A, Lipecka J, Brouillard F, Baudoin-Legros M, Dadlez M, Edelman A, Fritsch J (2006) Association between Hsp90 and the ClC-2 chloride channel upregulates channel function. American journal of physiology Cell physiology 290:C45-56. Hirota Y, Kurata Y, Kato M, Notsu T, Koshida S, Inoue T, Kawata Y, Miake J, Bahrudin U, Li P, Hoshikawa Y, Yamamoto Y, Igawa O, Shirayoshi Y, Nakai A, Ninomiya H, Higaki K, Hiraoka M, Hisatome I (2008) Functional stabilization of Kv1.5 protein by Hsp70 in mammalian cell lines. Biochemical and biophysical research communications 372:469-474. Horwich AL, Fenton WA, Chapman E, Farr GW (2007) Two families of chaperonin: physiology and mechanism. Annual review of cell and developmental biology 23:115-145. Hutt DM, Roth DM, Chalfant MA, Youker RT, Matteson J, Brodsky JL, Balch WE (2012) FK506 binding protein 8 peptidylprolyl isomerase activity manages a late stage of cystic fibrosis transmembrane conductance regulator (CFTR) folding and stability. The Journal of biological chemistry 287:21914-21925. Jentsch TJ, Stein V, Weinreich F, Zdebik AA (2002) Molecular structure and physiological function of chloride channels. Physiological reviews 82:503-568. Jespersen T, Membrez M, Nicolas CS, Pitard B, Staub O, Olesen SP, Baro I, Abriel H (2007) The KCNQ1 potassium channel is down-regulated by ubiquitylating enzymes of the Nedd4/Nedd4-like family. Cardiovascular research 74:64-74. Jiang J, Maes EG, Taylor AB, Wang L, Hinck AP, Lafer EM, Sousa R (2007) Structural basis of J cochaperone binding and regulation of Hsp70. Molecular cell 28:422-433. Jiao JD, Garg V, Yang B, Hu K (2008) Novel functional role of heat shock protein 90 in ATP-sensitive K+ channel-mediated hypoxic preconditioning. Cardiovascular research 77:126-133. Johnson JL (2012) Evolution and function of diverse Hsp90 homologs and cochaperone proteins. Biochimica et biophysica acta 1823:607-613. Jurkat-Rott K, Lerche H, Lehmann-Horn F (2002) Skeletal muscle channelopathies. Journal of neurology 249:1493-1502. Kamal A, Thao L, Sensintaffar J, Zhang L, Boehm MF, Fritz LC, Burrows FJ (2003) A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature 425:407-410. Kampinga HH, Craig EA (2010) The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nature reviews Molecular cell biology 11:579-592. Kang CB, Feng L, Chia J, Yoon HS (2005) Molecular characterization of FK-506 binding protein 38 and its potential regulatory role on the anti-apoptotic protein Bcl-2. Biochemical and biophysical research communications 337:30-38. Kang CB, Hong Y, Dhe-Paganon S, Yoon HS (2008) FKBP family proteins: immunophilins with versatile biological functions. Neuro-Signals 16:318-325. Kettern N, Dreiseidler M, Tawo R, Hohfeld J (2010) Chaperone-assisted degradation: multiple paths to destruction. Biological chemistry 391:481-489. Kim HR, Kang HS, Kim HD (1999) Geldanamycin induces heat shock protein expression through activation of HSF1 in K562 erythroleukemic cells. IUBMB life 48:429-433. Kim YE, Hipp MS, Bracher A, Hayer-Hartl M, Hartl FU (2013) Molecular chaperone functions in protein folding and proteostasis. Annual review of biochemistry 82:323-355. Koulov AV, LaPointe P, Lu B, Razvi A, Coppinger J, Dong MQ, Matteson J, Laister R, Arrowsmith C, Yates JR, 3rd, Balch WE (2010) Biological and structural basis for Aha1 regulation of Hsp90 ATPase activity in maintaining proteostasis in the human disease cystic fibrosis. Molecular biology of the cell 21:871-884. Kundrat L, Regan L (2010) Balance between folding and degradation for Hsp90-dependent client proteins: a key role for CHIP. Biochemistry 49:7428-7438. Kuo HC, Hsiao KM, Chang LI, You TH, Yeh TH, Huang CC (2006) Novel mutations at carboxyl terminus of CIC-1 channel in myotonia congenita. Acta neurologica Scandinavica 113:342-346. Lam E, Martin M, Wiederrecht G (1995) Isolation of a cDNA encoding a novel human FK506-binding protein homolog containing leucine zipper and tetratricopeptide repeat motifs. Gene 160:297-302. Lee K, Hong TJ, Hahn JS (2012) Roles of 17-AAG-induced molecular chaperones and Rma1 E3 ubiquitin ligase in folding and degradation of Pendrin. FEBS letters 586:2535-2541. Lee TT, Zhang XD, Chuang CC, Chen JJ, Chen YA, Chen SC, Chen TY, Tang CY (2013) Myotonia congenita mutation enhances the degradation of human CLC-1 chloride channels. PloS one 8:e55930. Li J, Soroka J, Buchner J (2012) The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones. Biochimica et biophysica acta 1823:624-635. Li J, Richter K, Reinstein J, Buchner J (2013) Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle. Nature structural molecular biology 20:326-331. Li P, Ninomiya H, Kurata Y, Kato M, Miake J, Yamamoto Y, Igawa O, Nakai A, Higaki K, Toyoda F, Wu J, Horie M, Matsuura H, Yoshida A, Shirayoshi Y, Hiraoka M, Hisatome I (2011) Reciprocal control of hERG stability by Hsp70 and Hsc70 with implication for restoration of LQT2 mutant stability. Circulation research 108:458-468. Lodish H BA, Zipursky SL, et al. (2000) Insertion of Membrane Proteins into the ER Membrane. In: Molecular Cell Biology, 4 Edition. New York: W. H. Freeman. Loo MA, Jensen TJ, Cui L, Hou Y, Chang XB, Riordan JR (1998) Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome. The EMBO journal 17:6879-6887. Lotz GP, Lin H, Harst A, Obermann WM (2003) Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone. The Journal of biological chemistry 278:17228-17235. Lukacs GL, Verkman AS (2012) CFTR: folding, misfolding and correcting the DeltaF508 conformational defect. Trends in molecular medicine 18:81-91. Ma D, Bai X, Guo S, Jiang Y (2008) The switch I region of Rheb is critical for its interaction with FKBP38. The Journal of biological chemistry 283:25963-25970. Macias MJ, Teijido O, Zifarelli G, Martin P, Ramirez-Espain X, Zorzano A, Palacin M, Pusch M, Estevez R (2007) Myotonia-related mutations in the distal C-terminus of ClC-1 and ClC-0 chloride channels affect the structure of a poly-proline helix. The Biochemical journal 403:79-87. Maestre-Martinez M, Haupt K, Edlich F, Neumann P, Parthier C, Stubbs MT, Fischer G, Lucke C (2011) A charge-sensitive loop in the FKBP38 catalytic domain modulates Bcl-2 binding. Journal of molecular recognition : JMR 24:23-34. Marozkina NV, Yemen S, Borowitz M, Liu L, Plapp M, Sun F, Islam R, Erdmann-Gilmore P, Townsend RR, Lichti CF, Mantri S, Clapp PW, Randell SH, Gaston B, Zaman K (2010) Hsp 70/Hsp 90 organizing protein as a nitrosylation target in cystic fibrosis therapy. Proceedings of the National Academy of Sciences of the United States of America 107:11393-11398. Mayer MP (2010) Gymnastics of molecular chaperones. Molecular cell 39:321-331. Mayer MP, Nikolay R, Bukau B (2002) Aha, another regulator for hsp90 chaperones. Molecular cell 10:1255-1256. McLaughlin SH, Sobott F, Yao ZP, Zhang W, Nielsen PR, Grossmann JG, Laue ED, Robinson CV, Jackson SE (2006) The co-chaperone p23 arrests the Hsp90 ATPase cycle to trap client proteins. Journal of molecular biology 356:746-758. Meacham GC, Patterson C, Zhang W, Younger JM, Cyr DM (2001) The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nature cell biology 3:100-105. Meacham GC, Lu Z, King S, Sorscher E, Tousson A, Cyr DM (1999) The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis. The EMBO journal 18:1492-1505. Meyer P, Prodromou C, Liao C, Hu B, Roe SM, Vaughan CK, Vlasic I, Panaretou B, Piper PW, Pearl LH (2004) Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery. The EMBO journal 23:1402-1410. Michnick SW, Rosen MK, Wandless TJ, Karplus M, Schreiber SL (1991) Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin. Science 252:836-839. Miller C (1982) Open-state substructure of single chloride channels from Torpedo electroplax. Philosophical transactions of the Royal Society of London Series B, Biological sciences 299:401-411. Miller C, White MM (1984) Dimeric structure of single chloride channels from Torpedo electroplax. Proceedings of the National Academy of Sciences of the United States of America 81:2772-2775. Mollapour M, Tsutsumi S, Truman Andrew W, Xu W, Vaughan Cara K, Beebe K, Konstantinova A, Vourganti S, Panaretou B, Piper Peter W, Trepel Jane B, Prodromou C, Pearl Laurence H, Neckers L (2011) Threonine 22 Phosphorylation Attenuates Hsp90 Interaction with Cochaperones and Affects Its Chaperone Activity. Molecular cell 41:672-681. Morimoto RI (2008) Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes development 22:1427-1438. Nielsen JV, Mitchelmore C, Pedersen KM, Kjaerulff KM, Finsen B, Jensen NA (2004) Fkbp8: novel isoforms, genomic organization, and characterization of a forebrain promoter in transgenic mice. Genomics 83:181-192. Nilius B, Droogmans G (2003) Amazing chloride channels: an overview. Acta physiologica Scandinavica 177:119-147. Obermann WM, Sondermann H, Russo AA, Pavletich NP, Hartl FU (1998) In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis. The Journal of cell biology 143:901-910. Okamoto T, Nishimura Y, Ichimura T, Suzuki K, Miyamura T, Suzuki T, Moriishi K, Matsuura Y (2006) Hepatitis C virus RNA replication is regulated by FKBP8 and Hsp90. The EMBO journal 25:5015-5025. Okiyoneda T, Apaja PM, Lukacs GL (2011) Protein quality control at the plasma membrane. Current opinion in cell biology 23:483-491. Okiyoneda T, Barriere H, Bagdany M, Rabeh WM, Du K, Hohfeld J, Young JC, Lukacs GL (2010) Peripheral protein quality control removes unfolded CFTR from the plasma membrane. Science 329:805-810. Orr HT, Zoghbi HY (2007) Trinucleotide repeat disorders. Annual review of neuroscience 30:575-621. Palade PT, Barchi RL (1977) Characteristics of the chloride conductance in muscle fibers of the rat diaphragm. The Journal of general physiology 69:325-342. Panaretou B, Siligardi G, Meyer P, Maloney A, Sullivan JK, Singh S, Millson SH, Clarke PA, Naaby-Hansen S, Stein R, Cramer R, Mollapour M, Workman P, Piper PW, Pearl LH, Prodromou C (2002) Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1. Molecular cell 10:1307-1318. Pappenberger G, Wilsher JA, Roe SM, Counsell DJ, Willison KR, Pearl LH (2002) Crystal structure of the CCTgamma apical domain: implications for substrate binding to the eukaryotic cytosolic chaperonin. Journal of molecular biology 318:1367-1379. Papponen H, Nissinen M, Kaisto T, Myllyla VV, Myllyla R, Metsikko K (2008) F413C and A531V but not R894X myotonia congenita mutations cause defective endoplasmic reticulum export of the muscle-specific chloride channel CLC-1. Muscle nerve 37:317-325. Papponen H, Toppinen T, Baumann P, Myllyla V, Leisti J, Kuivaniemi H, Tromp G, Myllyla R (1999) Founder mutations and the high prevalence of myotonia congenita in northern Finland. Neurology 53:297-302. Pearl LH, Prodromou C (2006) Structure and mechanism of the Hsp90 molecular chaperone machinery. Annual review of biochemistry 75:271-294. Peterson LB, Eskew JD, Vielhauer GA, Blagg BS (2012) The hERG channel is dependent upon the Hsp90alpha isoform for maturation and trafficking. Molecular pharmaceutics 9:1841-1846. Powers ET, Morimoto RI, Dillin A, Kelly JW, Balch WE (2009) Biological and chemical approaches to diseases of proteostasis deficiency. Annual review of biochemistry 78:959-991. Pratt WB, Toft DO (2003) Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Experimental biology and medicine (Maywood, NJ) 228:111-133. Preissler S, Deuerling E (2012) Ribosome-associated chaperones as key players in proteostasis. Trends in biochemical sciences 37:274-283. Prodromou C (2012) The 'active life' of Hsp90 complexes. Biochimica et biophysica acta 1823:614-623. Ptacek LJ, Johnson KJ, Griggs RC (1993) Genetics and physiology of the myotonic muscle disorders. The New England journal of medicine 328:482-489. Pusch M (2002) Myotonia caused by mutations in the muscle chloride channel gene CLCN1. Human mutation 19:423-434. Raiborg C, Stenmark H (2009) The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins. Nature 458:445-452. Retzlaff M, Hagn F, Mitschke L, Hessling M, Gugel F, Kessler H, Richter K, Buchner J (2010a) Asymmetric Activation of the Hsp90 Dimer by Its Cochaperone Aha1. Molecular cell 37:344-354. Retzlaff M, Hagn F, Mitschke L, Hessling M, Gugel F, Kessler H, Richter K, Buchner J (2010b) Asymmetric activation of the hsp90 dimer by its cochaperone aha1. Molecular cell 37:344-354. Richter K, Muschler P, Hainzl O, Reinstein J, Buchner J (2003) Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle. The Journal of biological chemistry 278:10328-10333. Rosner M, Hofer K, Kubista M, Hengstschlager M (2003) Cell size regulation by the human TSC tumor suppressor proteins depends on PI3K and FKBP38. Oncogene 22:4786-4798. Saviane C, Conti F, Pusch M (1999) The muscle chloride channel ClC-1 has a double-barreled appearance that is differentially affected in dominant and recessive myotonia. The Journal of general physiology 113:457-468. Saxena A, Banasavadi-Siddegowda YK, Fan Y, Bhattacharya S, Roy G, Giovannucci DR, Frizzell RA, Wang X (2012) Human heat shock protein 105/110 kDa (Hsp105/110) regulates biogenesis and quality control of misfolded cystic fibrosis transmembrane conductance regulator at multiple levels. The Journal of biological chemistry 287:19158-19170. Shirane M, Nakayama KI (2003) Inherent calcineurin inhibitor FKBP38 targets Bcl-2 to mitochondria and inhibits apoptosis. Nature cell biology 5:28-37. Soroka J, Wandinger SK, Mausbacher N, Schreiber T, Richter K, Daub H, Buchner J (2012) Conformational switching of the molecular chaperone Hsp90 via regulated phosphorylation. Molecular cell 45:517-528. Spiess C, Meyer AS, Reissmann S, Frydman J (2004) Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets. Trends in cell biology 14:598-604. Sreedhar AS, Kalmar E, Csermely P, Shen YF (2004) Hsp90 isoforms: functions, expression and clinical importance. FEBS letters 562:11-15. Steinmeyer K, Ortland C, Jentsch TJ (1991) Primary structure and functional expression of a developmentally regulated skeletal muscle chloride channel. Nature 354:301-304. Storer CL, Dickey CA, Galigniana MD, Rein T, Cox MB (2011) FKBP51 and FKBP52 in signaling and disease. Trends in endocrinology and metabolism: TEM 22:481-490. Sun L, Prince T, Manjarrez JR, Scroggins BT, Matts RL (2012) Characterization of the interaction of Aha1 with components of the Hsp90 chaperone machine and client proteins. Biochimica et biophysica acta 1823:1092-1101. Taipale M, Jarosz DF, Lindquist S (2010) HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nature reviews Molecular cell biology 11:515-528. Taipale M, Krykbaeva I, Koeva M, Kayatekin C, Westover KD, Karras GI, Lindquist S (2012) Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition. Cell 150:987-1001. Tang CY, Chen TY (2011) Physiology and pathophysiology of CLC-1: mechanisms of a chloride channel disease, myotonia. Journal of biomedicine biotechnology 2011:685328. Tang YC, Chang HC, Roeben A, Wischnewski D, Wischnewski N, Kerner MJ, Hartl FU, Hayer-Hartl M (2006) Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein. Cell 125:903-914. Tartaglia GG, Dobson CM, Hartl FU, Vendruscolo M (2010) Physicochemical determinants of chaperone requirements. Journal of molecular biology 400:579-588. Theodoraki MA, Caplan AJ (2012) Quality control and fate determination of Hsp90 client proteins. Biochimica et biophysica acta 1823:683-688. Thulasiraman V, Yang CF, Frydman J (1999) In vivo newly translated polypeptides are sequestered in a protected folding environment. The EMBO journal 18:85-95. Turnbull EL, Rosser MF, Cyr DM (2007) The role of the UPS in cystic fibrosis. BMC biochemistry 8 Suppl 1:S11. van Bemmelen MX, Rougier JS, Gavillet B, Apotheloz F, Daidie D, Tateyama M, Rivolta I, Thomas MA, Kass RS, Staub O, Abriel H (2004) Cardiac voltage-gated sodium channel Nav1.5 is regulated by Nedd4-2 mediated ubiquitination. Circulation research 95:284-291. Walker VE, Atanasiu R, Lam H, Shrier A (2007) Co-chaperone FKBP38 promotes HERG trafficking. The Journal of biological chemistry 282:23509-23516. Walker VE, Wong MJ, Atanasiu R, Hantouche C, Young JC, Shrier A (2010) Hsp40 chaperones promote degradation of the HERG potassium channel. The Journal of biological chemistry 285:3319-3329. Wang X, Venable J, LaPointe P, Hutt DM, Koulov AV, Coppinger J, Gurkan C, Kellner W, Matteson J, Plutner H, Riordan JR, Kelly JW, Yates JR, 3rd, Balch WE (2006) Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis. Cell 127:803-815. Wang Z, Hou Y, Guo X, van der Voet M, Boxem M, Dixon JE, Chisholm AD, Jin Y (2013) The EBAX-type Cullin-RING E3 ligase and Hsp90 guard the protein quality of the SAX-3/Robo receptor in developing neurons. Neuron 79:903-916. Ward CL, Omura S, Kopito RR (1995) Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83:121-127. Wiedmann B, Sakai H, Davis TA, Wiedmann M (1994) A protein complex required for signal-sequence-specific sorting and translocation. Nature 370:434-440. Xu X, Sarikas A, Dias-Santagata DC, Dolios G, Lafontant PJ, Tsai SC, Zhu W, Nakajima H, Nakajima HO, Field LJ, Wang R, Pan ZQ (2008) The CUL7 E3 ubiquitin ligase targets insulin receptor substrate 1 for ubiquitin-dependent degradation. Molecular cell 30:403-414. Yamamoto YH, Kimura T, Momohara S, Takeuchi M, Tani T, Kimata Y, Kadokura H, Kohno K (2010) A novel ER J-protein DNAJB12 accelerates ER-associated degradation of membrane proteins including CFTR. Cell structure and function 35:107-116. Yan FF, Pratt EB, Chen PC, Wang F, Skach WR, David LL, Shyng SL (2010) Role of Hsp90 in biogenesis of the beta-cell ATP-sensitive potassium channel complex. Molecular biology of the cell 21:1945-1954. Young JC (2014) The role of the cytosolic HSP70 chaperone system in diseases caused by misfolding and aberrant trafficking of ion channels. Disease models mechanisms 7:319-329. Young JC, Moarefi I, Hartl FU (2001) Hsp90: a specialized but essential protein-folding tool. The Journal of cell biology 154:267-273. Young JC, Barral JM, Ulrich Hartl F (2003) More than folding: localized functions of cytosolic chaperones. Trends in biochemical sciences 28:541-547. Young JC, Agashe VR, Siegers K, Hartl FU (2004) Pathways of chaperone-mediated protein folding in the cytosol. Nature reviews Molecular cell biology 5:781-791. Younger JM, Chen L, Ren H-Y, Rosser MFN, Turnbull EL, Fan C-Y, Patterson C, Cyr DM (2006) Sequential Quality-Control Checkpoints Triage Misfolded Cystic Fibrosis Transmembrane Conductance Regulator. Cell 126:571-582. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/18117 | - |
dc.description.abstract | 先天性肌肉強直症 (myotonia congenita) 是一種遺傳性肌肉疾病,是由於電壓敏感性氯離子通道CLC-1基因發生突變所造成。A531V是一種先天性肌肉強直症的突變型,其開關特性 (gating property) 與野生型 (wild-type) 並無明顯差別;但A531V蛋白質的表現量卻明顯較少,此表現減少的原因之一是由於蛋白酶體降解增加。本實驗室先前的研究發現A531V與伴護蛋白Hsp90的輔助伴護蛋白Aha1以及帶有PPIase功能的伴護蛋白 FKBP8有交互作用。分子伴護蛋白可協助蛋白質的折疊,以及將不具功能、錯誤摺疊的蛋白經由降解途徑移除。本篇論文目的為檢測可能調控CLC-1的chaperon,並且了解 CLC-1 WT和A531V是否經由Hsp70-Hsp90伴護蛋白系統來調控其蛋白質的品質控管。 我們發現大量表現Aha1可增加CLC-1 WT與A531V的穩定性,而利用shRNA壓制內生性Aha1的表現則降低了CLC-1 WT與A531V的表現;這個現象顯示加速Hsp90 ATPase cycling的速率可協助CLC-1的摺疊。此外,我們觀察到大量表現FKBP8後同樣也可增加CLC-1 WT與A531V的穩定性,並且增加了CLC-1在細胞膜上的表現,同時還可減短A531V的半衰期。從上述結果暗示CLC-1很有可能會經由Hsp70-Hsp90進行品質控管,接著我們大量表現Hsc70以及Hsp90α/β,並發現Hsc70以及Hsp90β同樣的增加了CLC-1的穩定性,但Hsp90α則對CLC-1沒有影響。當我們壓制了內生性的Hsc70之後,發現CLC-1 A531V表現量下降。我們也使用了Hsp90的抑制劑17-AAG,並發現CLC-1 WT和A531V的表現皆上升,此現象可能與17-AAG活化了Hsf1並造成其他伴護蛋白增加有關。 從我們的研究結果推測, Hsc70-Hsp90-FKBP8摺疊路徑可能是調控CLC-1蛋白質平衡的關鍵步驟。對於與肌強直症相關的圖變A531V而言,或許經由調控這些相關伴護蛋白的表現可以達成改善其不穩定缺陷的效果。 | zh_TW |
dc.description.abstract | Myotonia congenita is a hereditary muscle disorder caused by mutations in the human voltage-gated chloride (Cl-) channel CLC-1. A531V is a myotonia-related mutant with a gating property similar to that of wild-type (WT) channels. The protein expression of A531V, however, is significantly lower, which is partly attributed to an enhanced proteasomal degradation. Previous studies from our lab demonstrated that CLC-1 may interact with the Hsp90 cochaperone Aha1, as well as with the PPIase chaperone FKBP8. Molecular chaperones are known to assist protein folding and to remove nonfunctional, misfolded, or aggregated proteins via degradation pathways. In this study, we aim to identify CLC-1-associated molecular chaperones, and to examine whether the chaperones and cochaperones of the Hsp70-Hsp90 system may contribute to the protein quality control of CLC-1 WT and A531V. Overexpression of Aha1 promoted protein expression of both WT and A531V, whereas knockdown of Aha1 reduced the protein expression of both WT and A531V. These observations suggest that the rate of Hsp90 ATPase cycling may be important for the correct folding of CLC-1. Overexpression of FKBP8 also promoted total and surface protein expression of WT and A531V, although only A531V displayed a significant increase in protein half-life. We then investigated the role of Hsp70 and Hsp90 in CLC-1 quality control by overexpressing Hsc70, Hsp90α, or Hsp90β. We found that both Hsc70 and Hsp90β, but not Hsp90α, increased the protein expression of WT and A531V. In addition, knockdown of Hsc70 decreased the expression of A531V. Surprisingly, treatment with 17-AAG, an Hsp90 inhibitor, also led to an increase in the expression of both WT and A531V, which may result from 17-AAG –induced expression of heat shock transcription factor 1 (Hsf1). Together, our data suggest that the Hsc70-Hsp90β-FKBP8 chaperone pathway may play a key role in controlling the protein homeostasis of CLC-1. Our findings also imply that manipulation of the expression/activity of these chaperones/cochaperones may partially correct the protein expression deficit of the myotonia-related mutant A531V. | en |
dc.description.provenance | Made available in DSpace on 2021-06-08T00:51:43Z (GMT). No. of bitstreams: 1 ntu-103-R00441014-1.pdf: 3900364 bytes, checksum: 63c3863dd131481a63f41a74ceb235df (MD5) Previous issue date: 2014 | en |
dc.description.tableofcontents | 中文摘要 i Abstract ii 目錄 iv 圖目錄 vii 第一章 導論 1 1.1 氯離子通道 (Chloride channel) 1 1.2 CLC-1在骨骼肌細胞之生理功能 1 1.3 CLC-1的結構與特性 2 1.4 先天性肌肉強直症 (myotonia congenita) 2 1.5 Myotonia mutant: A531V 3 1.6 蛋白質的摺疊 4 1.7 分子伴護蛋白之基本概念 4 1.8 伴護蛋白在細胞內之作用途徑 5 1.9 The Hsp70 System 6 1.10 The Chaperonin System 7 1.11 The Hsp90 system 7 1.12 伴護蛋白調控蛋白質體平衡 9 1.13 離子通道蛋白受伴護蛋白之調控 10 1.14 研究目的 12 第二章 材料與方法 13 2.1 DNA construct 13 2.2 Cell culture 13 2.3 DNA transfection 14 2.4 Immunoblotting 14 2.5 Biotinylation of Cell Surface Proteins 15 2.6 Cycloheximide treatment 15 2.7 Lentivirus production and infection 16 2.8 17-AAG treatment 16 2.9 CLC-1 stable cell line generation 17 2.10 統計分析 17 第三章 結果 18 3.1 Transient expression system 18 3.1.1 Aha1 18 3.1.2 FKBP8 19 3.1.3 Hsp90β和Hsp90α 19 3.1.4 Hsc70 20 3.1.5 同時大量表現兩種chaperone 20 3.1.6 17-AAG 21 3.1.7 Hsp40s 21 3.1.8 HOP 21 3.1.9 E3 ubiuitin ligase 22 3.2 Stable cell line 22 3.2.1 Chapeorne protein 22 3.2.2 17-AAG 23 第四章 討論 24 4.1 Aha1調控Hsp90 chaperone cycle對CLC-1穩定性之影響 24 4.2 FKBP8參與調控CLC-1 WT及A531V之穩定性 25 4.3 Hsp90α以及Hsp90β對CLC-1 WT及A531V具有不同的影響 27 4.4 Hsc70及其cochaperone對CLC-1表現之影響 28 4.5 Hsp90抑制劑17-AAG使CLC-1之影響 30 4.6 同時大量表現兩種chaperone對CLC-1的影響 30 4.7 Chaperone參與CLC-1 WT與A531V的摺疊路徑之可能模式 31 4.8 CLC-1 stable cell line與transient transfection結果之比較 32 4.9 Chaperone對CLC-1品質控管的病生理意義 32 4.10 未解決的問題與未來的實驗方向 32 結論 34 圖表 36 附圖 67 參考資料 70 | |
dc.language.iso | zh-TW | |
dc.title | 分子伴護蛋白調控人類第一型氯離子通道蛋白之品質控管 | zh_TW |
dc.title | Molecular chaperone-mediated protein quality control of human CLC-1 chloride channel | en |
dc.type | Thesis | |
dc.date.schoolyear | 103-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 胡孟君,鄭瓊娟,吳君泰 | |
dc.subject.keyword | 分子伴護蛋白,人類第一型氯離子通道, | zh_TW |
dc.subject.keyword | Molecular chaperone,human CLC-1 chloride channel, | en |
dc.relation.page | 81 | |
dc.rights.note | 未授權 | |
dc.date.accepted | 2015-06-29 | |
dc.contributor.author-college | 醫學院 | zh_TW |
dc.contributor.author-dept | 生理學研究所 | zh_TW |
顯示於系所單位: | 生理學科所 |
文件中的檔案:
檔案 | 大小 | 格式 | |
---|---|---|---|
ntu-103-1.pdf 目前未授權公開取用 | 3.81 MB | Adobe PDF |
系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。