메뉴 건너뛰기




Volumn 97, Issue 21, 2013, Pages 9465-9478

A novel cholesterol-producing Pichia pastoris strain is an ideal host for functional expression of human Na,K-ATPase α3β1 isoform

Author keywords

Cholesterol; Lipid engineering; Membrane protein; Na,K ATPase; Pichia pastoris; Protein lipid interaction

Indexed keywords

FUNCTIONAL EXPRESSION; HETEROLOGOUS EXPRESSION; MEMBRANE PROTEINS; PICHIA PASTORIS; PROTEIN LOCALIZATION; PROTEIN-LIPID INTERACTIONS; STRUCTURE-FUNCTION RELATIONSHIP; WESTERN-BLOT ANALYSIS;

EID: 84885955436     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-013-5156-7     Document Type: Article
Times cited : (41)

References (67)
  • 1
    • 79751537491 scopus 로고    scopus 로고
    • Lipid-binding surfaces of membrane proteins: Evidence from evolutionary and structural analysis
    • 10.1016/j.bbamem.2010.12.008 10.1016/j.bbamem.2010.12.008 1:CAS:528:DC%2BC3MXjsVyms7g%3D
    • Adamian L, Naveed H, Liang J (2011) Lipid-binding surfaces of membrane proteins: evidence from evolutionary and structural analysis. Biochim Biophys Acta 1808:1092-1102. doi: 10.1016/j.bbamem.2010.12.008
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 1092-1102
    • Adamian, L.1    Naveed, H.2    Liang, J.3
  • 2
    • 33846011388 scopus 로고    scopus 로고
    • New roles for an old enzyme: Na,K-ATPase emerges as an interesting drug target
    • 10.1111/j.1365-2796.2006.01745.x 10.1111/j.1365-2796.2006.01745.x 1:CAS:528:DC%2BD2sXislWhsbo%3D
    • Aperia A (2007) New roles for an old enzyme: Na,K-ATPase emerges as an interesting drug target. J Intern Med 261:44-52. doi: 10.1111/j.1365-2796.2006. 01745.x
    • (2007) J Intern Med , vol.261 , pp. 44-52
    • Aperia, A.1
  • 4
    • 0029830036 scopus 로고    scopus 로고
    • Degradation and endoplasmic reticulum retention of unassembled α- And β-subunits of Na,K-ATPase correlate with interaction of BiP
    • 10.1074/jbc.271.34.20895 10.1074/jbc.271.34.20895 1:CAS:528: DyaK28Xlt1yntrc%3D
    • Beggah A, Mathews P, Beguin P, Geering K (1996) Degradation and endoplasmic reticulum retention of unassembled α- and β-subunits of Na,K-ATPase correlate with interaction of BiP. J Biol Chem 271:20895-20902. doi: 10.1074/jbc.271.34.20895
    • (1996) J Biol Chem , vol.271 , pp. 20895-20902
    • Beggah, A.1    Mathews, P.2    Beguin, P.3    Geering, K.4
  • 5
    • 0030981919 scopus 로고    scopus 로고
    • Role of glycosylation and disulfide bond formation in the β subunit in the folding and functional expression of Na,K-ATPase
    • 10.1074/jbc.272.15.10318 10.1074/jbc.272.15.10318 1:CAS:528: DyaK2sXisFOksLw%3D
    • Beggah AT, Jaunin P, Geering K (1997) Role of glycosylation and disulfide bond formation in the β subunit in the folding and functional expression of Na,K-ATPase. J Biol Chem 272:10318-10326. doi: 10.1074/jbc.272.15.10318
    • (1997) J Biol Chem , vol.272 , pp. 10318-10326
    • Beggah, A.T.1    Jaunin, P.2    Geering, K.3
  • 6
    • 0032544363 scopus 로고    scopus 로고
    • Membrane integration of Na,K-ATPase α-subunits and β-subunit assembly
    • 10.1074/jbc.273.38.24921 10.1074/jbc.273.38.24921 1:CAS:528: DyaK1cXmtlyqurk%3D
    • Beguin P, Hasler U, Beggah A, Horisberger JD, Geering K (1998) Membrane integration of Na,K-ATPase α-subunits and β-subunit assembly. J Biol Chem 273:24921-24931. doi: 10.1074/jbc.273.38.24921
    • (1998) J Biol Chem , vol.273 , pp. 24921-24931
    • Beguin, P.1    Hasler, U.2    Beggah, A.3    Horisberger, J.D.4    Geering, K.5
  • 7
    • 0035158317 scopus 로고    scopus 로고
    • Yeast - A panacea for the structure-function analysis of membrane proteins?
    • 10.1007/s002940100252 10.1007/s002940100252 1:CAS:528: DC%2BD3MXnvVCkurg%3D
    • Bill R (2001) Yeast - a panacea for the structure-function analysis of membrane proteins? Curr Genet 40:157-171. doi: 10.1007/s002940100252
    • (2001) Curr Genet , vol.40 , pp. 157-171
    • Bill, R.1
  • 8
    • 21344443929 scopus 로고    scopus 로고
    • The Na,K-ATPase and its isozymes: What we have learned using the baculovirus expression system
    • 10.2741/1705 10.2741/1705 1:CAS:528:DC%2BD2MXntFGisrw%3D
    • Blanco G (2005) The Na,K-ATPase and its isozymes: what we have learned using the baculovirus expression system. Front Biosci 10:2397. doi: 10.2741/1705
    • (2005) Front Biosci , vol.10 , pp. 2397
    • Blanco, G.1
  • 9
    • 34447339394 scopus 로고    scopus 로고
    • Expression of 25 human ABC transporters in the yeast Pichia pastoris and characterization of the purified ABCC3 ATPase activity
    • 10.1021/bi700020m 10.1021/bi700020m
    • Chloupková M, Pickert A, Lee JY, Souza S, Trinh YT, Connelly SM, Dumont ME, Dean M, Urbatsch IL (2007) Expression of 25 human ABC transporters in the yeast Pichia pastoris and characterization of the purified ABCC3 ATPase activity. Biochemistry 46:7992-8003. doi: 10.1021/bi700020m
    • (2007) Biochemistry , vol.46 , pp. 7992-8003
    • Chloupková, M.1    Pickert, A.2    Lee, J.Y.3    Souza, S.4    Trinh, Y.T.5    Connelly, S.M.6    Dumont, M.E.7    Dean, M.8    Urbatsch, I.L.9
  • 10
    • 20444489955 scopus 로고    scopus 로고
    • +-ATPase expressed in Pichia pastoris reveals an essential role of phospholipid-protein interactions
    • 10.1074/jbc.M414290200 10.1074/jbc.M414290200 1:CAS:528: DC%2BD2MXjsFOgsrw%3D
    • +-ATPase expressed in Pichia pastoris reveals an essential role of phospholipid-protein interactions. J Biol Chem 280:16610-8. doi: 10.1074/jbc.M414290200
    • (2005) J Biol Chem , vol.280 , pp. 16610-16618
    • Cohen, E.1    Goldshleger, R.2    Shainskaya, A.3    Tal, D.M.4    Ebel, C.5    Le Maire, M.6    Karlish, S.J.D.7
  • 11
    • 0035979370 scopus 로고    scopus 로고
    • Modulation of Na,K-ATPase and Na-ATPase activity by phospholipids and cholesterol. I. Steady-state kinetics
    • 10.1021/bi010541g 10.1021/bi010541g 1:CAS:528:DC%2BD3MXkvVCgt7o%3D
    • Cornelius F (2001) Modulation of Na,K-ATPase and Na-ATPase activity by phospholipids and cholesterol. I. Steady-state kinetics. Biochemistry 40:8842-8851. doi: 10.1021/bi010541g
    • (2001) Biochemistry , vol.40 , pp. 8842-8851
    • Cornelius, F.1
  • 12
    • 0038116611 scopus 로고    scopus 로고
    • Modulation of Na,K-ATPase by phospholipids and cholesterol. II. Steady-state and presteady-state kinetics
    • 10.1021/bi034532e 10.1021/bi034532e 1:CAS:528:DC%2BD3sXkvVaitbs%3D
    • Cornelius F, Turner N, Christensen HRZ (2003) Modulation of Na,K-ATPase by phospholipids and cholesterol. II. Steady-state and presteady-state kinetics. Biochemistry 42:8541-9. doi: 10.1021/bi034532e
    • (2003) Biochemistry , vol.42 , pp. 8541-8549
    • Cornelius, F.1    Turner, N.2    Christensen, H.R.Z.3
  • 13
    • 0034695680 scopus 로고    scopus 로고
    • Transport and pharmacological properties of nine different human Na,K-ATPase isozymes
    • 10.1074/jbc.275.3.1976 10.1074/jbc.275.3.1976 1:CAS:528: DC%2BD3cXotFajtQ%3D%3D
    • Crambert G, Hasler U, Beggah AT, Yu C, Modyanov NN, Horisberger JD, Lelievre L, Geering K (2000) Transport and pharmacological properties of nine different human Na,K-ATPase isozymes. J Biol Chem 275:1976-1986. doi: 10.1074/jbc.275.3.1976
    • (2000) J Biol Chem , vol.275 , pp. 1976-1986
    • Crambert, G.1    Hasler, U.2    Beggah, A.T.3    Yu, C.4    Modyanov, N.N.5    Horisberger, J.D.6    Lelievre, L.7    Geering, K.8
  • 14
    • 74549181271 scopus 로고    scopus 로고
    • Tuning microbial hosts for membrane protein production
    • 10.1186/1475-2859-8-69 10.1186/1475-2859-8-69
    • Freigassner M, Pichler H, Glieder A (2009) Tuning microbial hosts for membrane protein production. Microb Cell Fact 8:69. doi: 10.1186/1475-2859-8-69
    • (2009) Microb Cell Fact , vol.8 , pp. 69
    • Freigassner, M.1    Pichler, H.2    Glieder, A.3
  • 15
    • 14644445240 scopus 로고    scopus 로고
    • Monitoring dynamic expression of nuclear genes in Chlamydomonas reinhardtii by using a synthetic luciferase reporter gene
    • 10.1007/s11103-005-2150-1 1:CAS:528:DC%2BD2MXmtlGksw%3D%3D
    • Fuhrmann M, Hausherr A, Ferbitz L, Schödl T, Heitzer M, Hegemann P (2004) Monitoring dynamic expression of nuclear genes in Chlamydomonas reinhardtii by using a synthetic luciferase reporter gene. Plant Mol Biol 55:869-881. doi: 10.1007/s11103-005-2150-1
    • (2004) Plant Mol Biol , vol.55 , pp. 869-881
    • Fuhrmann, M.1    Hausherr, A.2    Ferbitz, L.3    Schödl, T.4    Heitzer, M.5    Hegemann, P.6
  • 16
    • 0034830988 scopus 로고    scopus 로고
    • +-ATPase in insect cells: Intracellular distribution of pump subunits
    • 1:CAS:528:DC%2BD3MXmvFCgu7k%3D
    • +-ATPase in insect cells: intracellular distribution of pump subunits. Am J Physiol Cell Physiol 281:C982-C992
    • (2001) Am J Physiol Cell Physiol , vol.281
    • Gatto, C.1    McLoud, S.M.2    Kaplan, J.H.3
  • 17
    • 33644870868 scopus 로고    scopus 로고
    • FXYD proteins: New regulators of Na-K-ATPase
    • 10.1152/ajprenal.00126.2005 10.1152/ajprenal.00126.2005 1:CAS:528:DC%2BD28XhsFKit7s%3D
    • Geering K (2006) FXYD proteins: new regulators of Na-K-ATPase. Am J Physiol Renal Physiol 290:F241-F250. doi: 10.1152/ajprenal.00126.2005
    • (2006) Am J Physiol Renal Physiol , vol.290
    • Geering, K.1
  • 18
    • 0034773778 scopus 로고    scopus 로고
    • The functional role of β subunits in oligomeric P-type ATPases
    • 10.1023/A:1010623724749 10.1023/A:1010623724749 1:CAS:528: DC%2BD3MXnsl2ltbc%3D
    • Geering K (2001) The functional role of β subunits in oligomeric P-type ATPases. J Bioenerg Biomembr 33:425-438. doi: 10.1023/A:1010623724749
    • (2001) J Bioenerg Biomembr , vol.33 , pp. 425-438
    • Geering, K.1
  • 19
    • 84858326040 scopus 로고    scopus 로고
    • Regulation of G protein-coupled receptors by palmitoylation and cholesterol
    • 10.1186/1741-7007-10-27 10.1186/1741-7007-10-27 1:CAS:528: DC%2BC38Xlsl2rs70%3D
    • Goddard AD, Watts A (2012) Regulation of G protein-coupled receptors by palmitoylation and cholesterol. BMC Biol 10:27. doi: 10.1186/1741-7007-10-27
    • (2012) BMC Biol , vol.10 , pp. 27
    • Goddard, A.D.1    Watts, A.2
  • 20
    • 0021010421 scopus 로고
    • Immunochemical identification of membrane proteins after sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • 10.1016/S0076-6879(83)96017-2 10.1016/S0076-6879(83)96017-2 1:CAS:528:DyaL2cXhslWis7g%3D
    • Haid A, Suissa M (1983) Immunochemical identification of membrane proteins after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Methods Enzymol 96:192-205. doi: 10.1016/S0076-6879(83)96017-2
    • (1983) Methods Enzymol , vol.96 , pp. 192-205
    • Haid, A.1    Suissa, M.2
  • 21
    • 44649172481 scopus 로고    scopus 로고
    • A specific cholesterol binding site is established by the 2.8 Å structure of the human β2-adrenergic receptor
    • 10.1016/j.str.2008.05.001 10.1016/j.str.2008.05.001 1:CAS:528: DC%2BD1cXmvFertbo%3D
    • Hanson MA, Cherezov V, Griffith MT, Roth CB, Jaakola VP, Chien EYT, Velasquez J, Kuhn P, Stevens RC (2008) A specific cholesterol binding site is established by the 2.8 Å structure of the human β2-adrenergic receptor. Structure 16:897-905. doi: 10.1016/j.str.2008.05.001
    • (2008) Structure , vol.16 , pp. 897-905
    • Hanson, M.A.1    Cherezov, V.2    Griffith, M.T.3    Roth, C.B.4    Jaakola, V.P.5    Chien, E.Y.T.6    Velasquez, J.7    Kuhn, P.8    Stevens, R.C.9
  • 22
    • 0035844306 scopus 로고    scopus 로고
    • Structural and functional features of the transmembrane domain of the Na,K-ATPase β subunit revealed by tryptophan scanning
    • 10.1074/jbc.M008778200 10.1074/jbc.M008778200 1:CAS:528: DC%2BD3MXjvFakurk%3D
    • Hasler U, Crambert G, Horisberger JD, Geering K (2001) Structural and functional features of the transmembrane domain of the Na,K-ATPase β subunit revealed by tryptophan scanning. J Biol Chem 276:16356-16364. doi: 10.1074/jbc.M008778200
    • (2001) J Biol Chem , vol.276 , pp. 16356-16364
    • Hasler, U.1    Crambert, G.2    Horisberger, J.D.3    Geering, K.4
  • 23
    • 0032515054 scopus 로고    scopus 로고
    • Role of β-subunit domains in the assembly, stable expression, intracellular routing, and functional properties of Na,K-ATPase
    • 10.1074/jbc.273.46.30826 10.1074/jbc.273.46.30826 1:CAS:528: DyaK1cXnsVyqsbY%3D
    • Hasler U, Wang X, Crambert G, Beguin P, Jaisser F, Horisberger JD, Geering K (1998) Role of β-subunit domains in the assembly, stable expression, intracellular routing, and functional properties of Na,K-ATPase. J Biol Chem 273:30826-30835. doi: 10.1074/jbc.273.46.30826
    • (1998) J Biol Chem , vol.273 , pp. 30826-30835
    • Hasler, U.1    Wang, X.2    Crambert, G.3    Beguin, P.4    Jaisser, F.5    Horisberger, J.D.6    Geering, K.7
  • 24
    • 35848949327 scopus 로고    scopus 로고
    • +-ATPase purified from Pichia pastoris membranes by specific interactions with lipids
    • 10.1021/bi701248y 10.1021/bi701248y 1:CAS:528:DC%2BD2sXhtFKksrvJ
    • +-ATPase purified from Pichia pastoris membranes by specific interactions with lipids. Biochemistry 46:12855-12867. doi: 10.1021/bi701248y
    • (2007) Biochemistry , vol.46 , pp. 12855-12867
    • Haviv, H.1    Cohen, E.2    Lifshitz, Y.3    Tal, D.M.4    Goldshleger, R.5    Karlish, S.J.D.6
  • 25
    • 84875987246 scopus 로고    scopus 로고
    • Neutral phospholipids stimulate Na,K-ATPase activity: A specific lipid-protein interaction
    • 10.1074/jbc.M112.446997 10.1074/jbc.M112.446997 1:CAS:528: DC%2BC3sXlsVGgurg%3D
    • Haviv H, Habeck M, Kanai R, Toyoshima C, Karlish SJD (2013) Neutral phospholipids stimulate Na,K-ATPase activity: a specific lipid-protein interaction. J Biol Chem 288:10073-81. doi: 10.1074/jbc.M112.446997
    • (2013) J Biol Chem , vol.288 , pp. 10073-10081
    • Haviv, H.1    Habeck, M.2    Kanai, R.3    Toyoshima, C.4    Karlish, S.J.D.5
  • 26
    • 0036678492 scopus 로고    scopus 로고
    • Multiple functions of sterols in yeast endocytosis
    • 10.1091/mbc.E02-04-0186 10.1091/mbc.E02-04-0186 1:CAS:528: DC%2BD38XmsVKls7s%3D
    • Heese-Peck A, Pichler H, Zanolari B, Watanabe R, Daum G, Riezman H (2002) Multiple functions of sterols in yeast endocytosis. Mol Biol Cell 13:2664-80. doi: 10.1091/mbc.E02-04-0186
    • (2002) Mol Biol Cell , vol.13 , pp. 2664-2680
    • Heese-Peck, A.1    Pichler, H.2    Zanolari, B.3    Watanabe, R.4    Daum, G.5    Riezman, H.6
  • 28
    • 3142692722 scopus 로고    scopus 로고
    • +-ATPase: SDS-solubilized enzyme retains partial structure and function
    • 10.1074/jbc.M401986200 10.1074/jbc.M401986200 1:CAS:528: DC%2BD2cXlsVClurg%3D
    • +-ATPase: SDS-solubilized enzyme retains partial structure and function. J Biol Chem 279:29832-29840. doi: 10.1074/jbc.M401986200
    • (2004) J Biol Chem , vol.279 , pp. 29832-29840
    • Ivanov, A.V.1    Gable, M.E.2    Askari, A.3
  • 29
    • 84872965208 scopus 로고    scopus 로고
    • Membrane lipids in the function of serotonin and adrenergic receptors
    • 1:CAS:528:DC%2BC3sXjvFOms7g%3D
    • Jafurulla M, Chattopadhyay A (2013) Membrane lipids in the function of serotonin and adrenergic receptors. Curr Med Chem 20:47-55
    • (2013) Curr Med Chem , vol.20 , pp. 47-55
    • Jafurulla, M.1    Chattopadhyay, A.2
  • 30
    • 0035997378 scopus 로고    scopus 로고
    • Biochemistry of Na,K-ATPase
    • 10.1146/annurev.biochem.71.102201.141218 10.1146/annurev.biochem.71. 102201.141218 1:CAS:528:DC%2BD38Xos1Cltrc%3D
    • Kaplan JH (2002) Biochemistry of Na,K-ATPase. Ann Rev Biochem 71:511-35. doi: 10.1146/annurev.biochem.71.102201.141218
    • (2002) Ann Rev Biochem , vol.71 , pp. 511-535
    • Kaplan, J.H.1
  • 31
    • 83355166924 scopus 로고    scopus 로고
    • Stabilization of the α2 isoform of Na,K-ATPase by mutations in a phospholipid binding pocket
    • 10.1074/jbc.M111.293852 10.1074/jbc.M111.293852 1:CAS:528: DC%2BC3MXhs1ShurrI
    • Kapri-Pardes E, Katz A, Haviv H, Mahmmoud Y, Ilan M, Khalfin-Penigel I, Carmeli S, Yarden O, Karlish SJD (2011) Stabilization of the α2 isoform of Na,K-ATPase by mutations in a phospholipid binding pocket. J Biol Chem 286:42888-99. doi: 10.1074/jbc.M111.293852
    • (2011) J Biol Chem , vol.286 , pp. 42888-42899
    • Kapri-Pardes, E.1    Katz, A.2    Haviv, H.3    Mahmmoud, Y.4    Ilan, M.5    Khalfin-Penigel, I.6    Carmeli, S.7    Yarden, O.8    Karlish, S.J.D.9
  • 32
    • 0035423116 scopus 로고    scopus 로고
    • Ergosterol is required for the Sec18/ATP-dependent priming step of homotypic vacuole fusion
    • 10.1093/emboj/20.15.4035 10.1093/emboj/20.15.4035 1:CAS:528: DC%2BD3MXmtlChtrg%3D
    • Kato M, Wickner W (2001) Ergosterol is required for the Sec18/ATP-dependent priming step of homotypic vacuole fusion. EMBO J 20:4035-40. doi: 10.1093/emboj/20.15.4035
    • (2001) EMBO J , vol.20 , pp. 4035-4040
    • Kato, M.1    Wickner, W.2
  • 33
    • 77953482802 scopus 로고    scopus 로고
    • Selectivity of digitalis glycosides for isoforms of human Na,K-ATPase
    • 10.1074/jbc.M110.119248 10.1074/jbc.M110.119248 1:CAS:528: DC%2BC3cXnt1Cmtb8%3D
    • Katz A, Lifshitz Y, Bab-Dinitz E, Kapri-Pardes E, Goldshleger R, Tal DM, Karlish SJD (2010) Selectivity of digitalis glycosides for isoforms of human Na,K-ATPase. J Biol Chem 285:19582-92. doi: 10.1074/jbc.M110.119248
    • (2010) J Biol Chem , vol.285 , pp. 19582-19592
    • Katz, A.1    Lifshitz, Y.2    Bab-Dinitz, E.3    Kapri-Pardes, E.4    Goldshleger, R.5    Tal, D.M.6    Karlish, S.J.D.7
  • 34
    • 84855984250 scopus 로고    scopus 로고
    • GPCR production in a novel yeast strain that makes cholesterol-like sterols
    • 10.1016/j.ymeth.2011.09.023 10.1016/j.ymeth.2011.09.023 1:CAS:528:DC%2BC38Xht1Wnu7s%3D
    • Kitson SM, Mullen W, Cogdell RJ, Bill RM, Fraser NJ (2011) GPCR production in a novel yeast strain that makes cholesterol-like sterols. Methods 55:287-92. doi: 10.1016/j.ymeth.2011.09.023
    • (2011) Methods , vol.55 , pp. 287-292
    • Kitson, S.M.1    Mullen, W.2    Cogdell, R.J.3    Bill, R.M.4    Fraser, N.J.5
  • 35
    • 0034663844 scopus 로고    scopus 로고
    • +-ATPase modifies the cation binding pocket and thereby generates a high Na + ATPase activity
    • 10.1021/bi0001168 10.1021/bi0001168 1:CAS:528:DC%2BD3cXkvFSjsrg%3D
    • +-ATPase modifies the cation binding pocket and thereby generates a high Na + ATPase activity. Biochemistry 39:9959-9966. doi: 10.1021/bi0001168
    • (2000) Biochemistry , vol.39 , pp. 9959-9966
    • Koenderink, J.B.1    Swarts, H.G.P.2    Hermsen, H.P.H.3    Willems, P.4    De Pont, J.5
  • 36
    • 84872552572 scopus 로고    scopus 로고
    • Expression of GPCRs in Pichia pastoris for structural studies
    • 10.1016/B978-0-12-391861-1.00001-0 10.1016/B978-0-12-391861-1.00001-0 1:CAS:528:DC%2BC3sXotFejtbY%3D
    • Krettler C, Reinhart C, Bevans CG (2013) Expression of GPCRs in Pichia pastoris for structural studies. Methods Enzymol 520:1-29. doi: 10.1016/B978-0-12-391861-1.00001-0
    • (2013) Methods Enzymol , vol.520 , pp. 1-29
    • Krettler, C.1    Reinhart, C.2    Bevans, C.G.3
  • 37
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 10.1038/227680a0 10.1038/227680a0 1:CAS:528:DC%2BD3MXlsFags7s%3D
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-5. doi: 10.1038/227680a0
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 38
    • 33744926463 scopus 로고    scopus 로고
    • +-ATPase. Purification of α1/β1/PLM complexes expressed in Pichia pastoris
    • 10.1074/jbc.M601993200 10.1074/jbc.M601993200 1:CAS:528: DC%2BD28Xlt1CktLw%3D
    • +-ATPase. Purification of α1/β1/PLM complexes expressed in Pichia pastoris. J Biol Chem 281:15790-9. doi: 10.1074/jbc.M601993200
    • (2006) J Biol Chem , vol.281 , pp. 15790-15799
    • Lifshitz, Y.1    Lindzen, M.2    Garty, H.3    Karlish, S.J.D.4
  • 39
    • 37349040730 scopus 로고    scopus 로고
    • Purification of the human α2 Isoform of Na,K-ATPase expressed in Pichia pastoris. Stabilization by lipids and FXYD1
    • 10.1021/bi701812c 10.1021/bi701812c 1:CAS:528:DC%2BD2sXhtlOksrbO
    • Lifshitz Y, Petrovich E, Haviv H, Goldshleger R, Tal DM, Garty H, Karlish SJD (2007) Purification of the human α2 Isoform of Na,K-ATPase expressed in Pichia pastoris. Stabilization by lipids and FXYD1. Biochemistry 46:14937-50. doi: 10.1021/bi701812c
    • (2007) Biochemistry , vol.46 , pp. 14937-14950
    • Lifshitz, Y.1    Petrovich, E.2    Haviv, H.3    Goldshleger, R.4    Tal, D.M.5    Garty, H.6    Karlish, S.J.D.7
  • 41
    • 0030669990 scopus 로고    scopus 로고
    • + ATPase expressed in insect cells
    • 10.1016/S0304-4165(96)00153-5 10.1016/S0304-4165(96)00153-5 1:CAS:528:DyaK2sXmtFKhtL4%3D
    • + ATPase expressed in insect cells. Biochim Biophys Acta 1336:370-386. doi: 10.1016/S0304-4165(96)00153-5
    • (1997) Biochim Biophys Acta , vol.1336 , pp. 370-386
    • Liu, J.Y.1    Guidotti, G.2
  • 42
    • 71849104860 scopus 로고
    • Protein measurement with the Folin phenol reagent
    • 1:CAS:528:DyaG38XhsVyrsw%3D%3D
    • Lowry OH, Rosebrough NJ, Farr LA, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265-276
    • (1951) J Biol Chem , vol.193 , pp. 265-276
    • Lowry, O.H.1    Rosebrough, N.J.2    Farr, L.A.3    Randall, R.J.4
  • 44
    • 3042765579 scopus 로고    scopus 로고
    • Functional expression of the human breast cancer resistance protein in Pichia pastoris
    • 10.1016/j.bbrc.2004.06.012 10.1016/j.bbrc.2004.06.012 1:CAS:528:DC%2BD2cXlsVaru7Y%3D
    • Mao Q, Conseil G, Gupta A, Cole SPC, Unadkat JD (2004) Functional expression of the human breast cancer resistance protein in Pichia pastoris. Biochem Biophys Res Commun 320:730-737. doi: 10.1016/j.bbrc.2004.06.012
    • (2004) Biochem Biophys Res Commun , vol.320 , pp. 730-737
    • Mao, Q.1    Conseil, G.2    Gupta, A.3    Cole, S.P.C.4    Unadkat, J.D.5
  • 45
    • 84885915525 scopus 로고    scopus 로고
    • Effect of sterol composition on the activity of the yeast G-protein-coupled receptor Ste2
    • 10.1007/s00253-012-4470-9 10.1007/s00253-012-4470-9 1:CAS:528: DC%2BC3sXlvV2htLg%3D
    • Morioka S, Shigemori T, Hara K, Morisaka H, Kuroda K, Ueda M (2013) Effect of sterol composition on the activity of the yeast G-protein-coupled receptor Ste2. Appl Microbiol Biotechnol 97:4013-4020. doi: 10.1007/s00253-012- 4470-9
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 4013-4020
    • Morioka, S.1    Shigemori, T.2    Hara, K.3    Morisaka, H.4    Kuroda, K.5    Ueda, M.6
  • 47
    • 0032741066 scopus 로고    scopus 로고
    • Specific sterols required for the internalization step of endocytosis in yeast
    • 10.1091/mbc.10.11.3943 1:CAS:528:DyaK1MXntlyrsbg%3D
    • Munn AL, Heese-Peck A, Stevenson BJ, Pichler H, Riezman H (1999) Specific sterols required for the internalization step of endocytosis in yeast. Mol Biol Cell 10:3943-57
    • (1999) Mol Biol Cell , vol.10 , pp. 3943-3957
    • Munn, A.L.1    Heese-Peck, A.2    Stevenson, B.J.3    Pichler, H.4    Riezman, H.5
  • 48
    • 84863090270 scopus 로고    scopus 로고
    • Deletion of the Pichia pastoris KU70 homologue facilitates platform strain generation for gene expression and synthetic biology
    • 10.1371/journal.pone.0039720 10.1371/journal.pone.0039720
    • Näätsaari L, Mistlberger B, Ruth C, Hajek T, Hartner FS, Glieder A (2012) Deletion of the Pichia pastoris KU70 homologue facilitates platform strain generation for gene expression and synthetic biology. PloS ONE 7:e39720. doi: 10.1371/journal.pone.0039720
    • (2012) PloS ONE , vol.7 , pp. 39720
    • Näätsaari, L.1    Mistlberger, B.2    Ruth, C.3    Hajek, T.4    Hartner, F.S.5    Glieder, A.6
  • 49
    • 80054063178 scopus 로고    scopus 로고
    • Biosynthesis of cholesterol and other sterols
    • 10.1021/cr200021m 10.1021/cr200021m 1:CAS:528:DC%2BC3MXhtFCgsL7F
    • Nes WD (2011) Biosynthesis of cholesterol and other sterols. Chem Rev 111:6423-51. doi: 10.1021/cr200021m
    • (2011) Chem Rev , vol.111 , pp. 6423-6451
    • Nes, W.D.1
  • 50
    • 84861805331 scopus 로고    scopus 로고
    • The role of cholesterol on the activity and stability of neurotensin receptor 1
    • 10.1016/j.bbamem.2012.04.010 10.1016/j.bbamem.2012.04.010 1:CAS:528:DC%2BC38XovVagtr4%3D
    • Oates J, Faust B, Attrill H, Harding P, Orwick M, Watts A (2012) The role of cholesterol on the activity and stability of neurotensin receptor 1. Biochim Biophys Acta 1818:2228-33. doi: 10.1016/j.bbamem.2012.04.010
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 2228-2233
    • Oates, J.1    Faust, B.2    Attrill, H.3    Harding, P.4    Orwick, M.5    Watts, A.6
  • 51
    • 82955248059 scopus 로고    scopus 로고
    • Uncovering the intimate relationship between lipids, cholesterol and GPCR activation
    • 10.1016/j.sbi.2011.09.007 10.1016/j.sbi.2011.09.007 1:CAS:528: DC%2BC3MXhsFOhurvI
    • Oates J, Watts A (2011) Uncovering the intimate relationship between lipids, cholesterol and GPCR activation. Curr Opin Struct Biol 21:802-7. doi: 10.1016/j.sbi.2011.09.007
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 802-807
    • Oates, J.1    Watts, A.2
  • 52
    • 21844472493 scopus 로고    scopus 로고
    • Flux of sterol intermediates in a yeast strain deleted of the lanosterol C-14 demethylase Erg11p
    • 10.1016/j.bbalip.2005.05.003 10.1016/j.bbalip.2005.05.003 1:CAS:528:DC%2BD2MXmtFGhtbw%3D
    • Ott RG, Athenstaedt K, Hrastnik C, Leitner E, Bergler H, Daum G (2005) Flux of sterol intermediates in a yeast strain deleted of the lanosterol C-14 demethylase Erg11p. Biochim Biophys Acta 1735:111-8. doi: 10.1016/j.bbalip.2005. 05.003
    • (2005) Biochim Biophys Acta , vol.1735 , pp. 111-118
    • Ott, R.G.1    Athenstaedt, K.2    Hrastnik, C.3    Leitner, E.4    Bergler, H.5    Daum, G.6
  • 54
    • 0030027897 scopus 로고    scopus 로고
    • Expression in high yield of pig α1β1 Na,K-ATPase and inactive mutants D369N and D807N in Saccharomyces cerevisiae
    • 10.1074/jbc.271.5.2514 10.1074/jbc.271.51.32546 1:CAS:528: DyaK28XptVKltA%3D%3D
    • Pedersen PA, Rasmussen JH, Joergensen PL (1996) Expression in high yield of pig α1β1 Na,K-ATPase and inactive mutants D369N and D807N in Saccharomyces cerevisiae. J Biol Chem 271:2514-2522. doi: 10.1074/jbc.271.5.2514
    • (1996) J Biol Chem , vol.271 , pp. 2514-2522
    • Pedersen, P.A.1    Rasmussen, J.H.2    Joergensen, P.L.3
  • 55
    • 0029692209 scopus 로고    scopus 로고
    • The extraction and analysis of sterols from yeast
    • 10.1385/0-89603-319-8:123 1:CAS:528:DyaK28Xit1Cktbg%3D
    • Quail MA, Kelly SL (1996) The extraction and analysis of sterols from yeast. Methods Mol Biol 53:123-31. doi: 10.1385/0-89603-319-8:123
    • (1996) Methods Mol Biol , vol.53 , pp. 123-131
    • Quail, M.A.1    Kelly, S.L.2
  • 56
    • 34249109987 scopus 로고    scopus 로고
    • Expression of the α3/β1 isoform of human Na,K-ATPase in the methylotrophic yeast Pichia pastoris
    • 10.1111/j.1567-1364.2007.00227.x 10.1111/j.1567-1364.2007.00227.x 1:CAS:528:DC%2BD2sXmt1erurg%3D
    • Reina C, Padoani G, Carotti C, Merico A, Tripodi G, Ferrari P, Popolo L (2007) Expression of the α3/β1 isoform of human Na,K-ATPase in the methylotrophic yeast Pichia pastoris. FEMS Yeast Res 7:585-94. doi: 10.1111/j.1567-1364.2007.00227.x
    • (2007) FEMS Yeast Res , vol.7 , pp. 585-594
    • Reina, C.1    Padoani, G.2    Carotti, C.3    Merico, A.4    Tripodi, G.5    Ferrari, P.6    Popolo, L.7
  • 57
    • 33745400408 scopus 로고    scopus 로고
    • Cholesterol is required for efficient endoplasmic reticulum-to-Golgi transport of secretory membrane proteins
    • 10.1091/mbc.E05-02-0100 10.1091/mbc.E05-02-0100 1:CAS:528: DC%2BD28XltlSqu7k%3D
    • Ridsdale A, Denis M, Gougeon PY, Jk N, Presley JF, Zha X (2006) Cholesterol is required for efficient endoplasmic reticulum-to-Golgi transport of secretory membrane proteins. Mol Biol Cell 17:1593-1605. doi: 10.1091/mbc.E05-02-0100
    • (2006) Mol Biol Cell , vol.17 , pp. 1593-1605
    • Ridsdale, A.1    Denis, M.2    Gougeon, P.Y.3    Jk, N.4    Presley, J.F.5    Zha, X.6
  • 58
    • 0001409028 scopus 로고
    • The influence of some cations on an adenosine triphosphatase from peripheral nerves
    • 10.1016/0006-3002(57)90343-8 1:CAS:528:DyaG2sXjs1aitQ%3D%3D
    • Skou JC (1957) The influence of some cations on an adenosine triphosphatase from peripheral nerves. Biochim Biophys Acta 23:394-401
    • (1957) Biochim Biophys Acta , vol.23 , pp. 394-401
    • Skou, J.C.1
  • 59
    • 80052033032 scopus 로고    scopus 로고
    • A stable yeast strain efficiently producing cholesterol instead of ergosterol is functional for tryptophan uptake, but not weak organic acid resistance
    • 10.1016/j.ymben.2011.06.006 10.1016/j.ymben.2011.06.006 1:CAS:528:DC%2BC3MXhtV2itb%2FK
    • Souza CM, Schwabe TME, Pichler H, Ploier B, Leitner E, Guan XL, Wenk MR, Riezman I, Riezman H (2011) A stable yeast strain efficiently producing cholesterol instead of ergosterol is functional for tryptophan uptake, but not weak organic acid resistance. Metab Eng 13:555-69. doi: 10.1016/j.ymben.2011.06. 006
    • (2011) Metab Eng , vol.13 , pp. 555-569
    • Souza, C.M.1    Schwabe, T.M.E.2    Pichler, H.3    Ploier, B.4    Leitner, E.5    Guan, X.L.6    Wenk, M.R.7    Riezman, I.8    Riezman, H.9
  • 60
    • 0242664242 scopus 로고    scopus 로고
    • +-ATPase in Pichia pastoris: Analysis of wild type and D369N mutant proteins by Fe2 + -catalyzed oxidative cleavage and molecular modeling
    • 10.1074/jbc.M308303200 10.1074/jbc.M308303200 1:CAS:528: DC%2BD3sXosl2itbc%3D
    • +-ATPase in Pichia pastoris: analysis of wild type and D369N mutant proteins by Fe2 + -catalyzed oxidative cleavage and molecular modeling. J Biol Chem 278:46064-73. doi: 10.1074/jbc.M308303200
    • (2003) J Biol Chem , vol.278 , pp. 46064-46073
    • Strugatsky, D.1    Gottschalk, K.E.2    Goldshleger, R.3    Bibi, E.4    Karlish, S.J.D.5
  • 61
    • 82955168417 scopus 로고    scopus 로고
    • +-ATPase: New light on the oldest ion pump
    • 10.1016/j.str.2011.10.016 10.1016/j.str.2011.10.016 1:CAS:528: DC%2BC3MXhs1Sgt73E
    • +-ATPase: new light on the oldest ion pump. Structure 19:1732-8. doi: 10.1016/j.str.2011.10.016
    • (2011) Structure , vol.19 , pp. 1732-1738
    • Toyoshima, C.1    Kanai, R.2    Cornelius, F.3
  • 62
    • 0038491550 scopus 로고    scopus 로고
    • Ergosterol is required for targeting of tryptophan permease to the yeast plasma membrane
    • 10.1083/jcb.200303088 10.1083/jcb.200303088 1:CAS:528: DC%2BD3sXkvFCmsrs%3D
    • Umebayashi K, Nakano A (2003) Ergosterol is required for targeting of tryptophan permease to the yeast plasma membrane. J Cell Biol 161:1117-31. doi: 10.1083/jcb.200303088
    • (2003) J Cell Biol , vol.161 , pp. 1117-1131
    • Umebayashi, K.1    Nakano, A.2
  • 63
    • 84877036789 scopus 로고    scopus 로고
    • Yeast metabolic engineering - Targeting sterol metabolism and terpenoid formation
    • 10.1016/j.plipres.2013.03.001 10.1016/j.plipres.2013.03.001 1:CAS:528:DC%2BC3sXovVCgtbc%3D
    • Wriessnegger T, Pichler H (2013) Yeast metabolic engineering - targeting sterol metabolism and terpenoid formation. Prog Lipid Res 52:277-93. doi: 10.1016/j.plipres.2013.03.001
    • (2013) Prog Lipid Res , vol.52 , pp. 277-293
    • Wriessnegger, T.1    Pichler, H.2
  • 64
    • 0035823586 scopus 로고    scopus 로고
    • Effect of the structure of natural sterols and sphingolipids on the formation of ordered sphingolipid/sterol domains (rafts). Comparison of cholesterol to plant, fungal, and disease-associated sterols and comparison of sphingomyelin, cerebrosides, and ceramide
    • 10.1074/jbc.M104776200 10.1074/jbc.M104776200 1:CAS:528: DC%2BD3MXmslyls70%3D
    • Xu X, Bittman R, Duportail G, Heissler D, Vilcheze C, London E (2001) Effect of the structure of natural sterols and sphingolipids on the formation of ordered sphingolipid/sterol domains (rafts). Comparison of cholesterol to plant, fungal, and disease-associated sterols and comparison of sphingomyelin, cerebrosides, and ceramide. J Biol Chem 276:33540-6. doi: 10.1074/jbc.M104776200
    • (2001) J Biol Chem , vol.276 , pp. 33540-33546
    • Xu, X.1    Bittman, R.2    Duportail, G.3    Heissler, D.4    Vilcheze, C.5    London, E.6
  • 65
    • 33750492961 scopus 로고    scopus 로고
    • Dot-blot immunodetection as a versatile and high-throughput assay to evaluate recombinant GPCRs produced in the yeast Pichia pastoris
    • 10.1016/j.pep.2006.05.017 10.1016/j.pep.2006.05.017 1:CAS:528: DC%2BD28XhtFKmt73P
    • Zeder-Lutz G, Cherouati N, Reinhart C, Pattus F, Wagner R (2006) Dot-blot immunodetection as a versatile and high-throughput assay to evaluate recombinant GPCRs produced in the yeast Pichia pastoris. Protein Expr Purif 50:118-127. doi: 10.1016/j.pep.2006.05.017
    • (2006) Protein Expr Purif , vol.50 , pp. 118-127
    • Zeder-Lutz, G.1    Cherouati, N.2    Reinhart, C.3    Pattus, F.4    Wagner, R.5
  • 66
    • 84858319313 scopus 로고    scopus 로고
    • Palmitoylation and membrane cholesterol stabilize μ-opioid receptor homodimerization and G protein coupling
    • 10.1186/1471-2121-13-6 10.1186/1471-2121-13-6 1:CAS:528: DC%2BC38Xms1Cmurk%3D
    • Zheng H, Pearsall EA, Hurst DP, Zhang Y, Chu J, Zhou Y, Reggio PH, Loh HH, Law PY (2012) Palmitoylation and membrane cholesterol stabilize μ-opioid receptor homodimerization and G protein coupling. BMC Cell Biol 13:6. doi: 10.1186/1471-2121-13-6
    • (2012) BMC Cell Biol , vol.13 , pp. 6
    • Zheng, H.1    Pearsall, E.A.2    Hurst, D.P.3    Zhang, Y.4    Chu, J.5    Zhou, Y.6    Reggio, P.H.7    Loh, H.H.8    Law, P.Y.9
  • 67
    • 0029009125 scopus 로고
    • Isolation and biochemical characterization of organelles from the yeast, Saccharomyces cerevisiae
    • 10.1002/yea.320110602 10.1002/yea.320110602 1:CAS:528:DyaK2MXlvVykurg%3D
    • Zinser E, Daum G (1995) Isolation and biochemical characterization of organelles from the yeast, Saccharomyces cerevisiae. Yeast 11:493-536. doi: 10.1002/yea.320110602
    • (1995) Yeast , vol.11 , pp. 493-536
    • Zinser, E.1    Daum, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.