메뉴 건너뛰기




Volumn 70, Issue 1, 2010, Pages 81-87

Purification and characterization of mammalian glucose transporters expressed in Pichia pastoris

Author keywords

Glucose transporter; GLUT1; GLUT4; Membrane protein purification

Indexed keywords

GLUCOSE TRANSPORTER 1; GLUCOSE TRANSPORTER 2; SLC2A2 PROTEIN, RAT;

EID: 75349092314     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2009.10.011     Document Type: Article
Times cited : (15)

References (49)
  • 2
    • 33845917073 scopus 로고    scopus 로고
    • Energetics of ligand-induced conformational flexibility in the lactose permease of Escherichia coli
    • Nie Y., Smirnova I., Kasho V., and Kaback H.R. Energetics of ligand-induced conformational flexibility in the lactose permease of Escherichia coli. J. Biol. Chem. 281 (2006) 35779-35784
    • (2006) J. Biol. Chem. , vol.281 , pp. 35779-35784
    • Nie, Y.1    Smirnova, I.2    Kasho, V.3    Kaback, H.R.4
  • 3
    • 4444328639 scopus 로고    scopus 로고
    • Lactose permease as a paradigm for membrane transport proteins
    • (Review)
    • Abramson J., Iwata S., and Kaback H.R. Lactose permease as a paradigm for membrane transport proteins. Mol. Membr. Biol. 21 (2004) 227-236 (Review)
    • (2004) Mol. Membr. Biol. , vol.21 , pp. 227-236
    • Abramson, J.1    Iwata, S.2    Kaback, H.R.3
  • 4
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • Abramson J., Smirnova I., Kasho V., Verner G., Kaback H.R., and Iwata S. Structure and mechanism of the lactose permease of Escherichia coli. Science 301 (2003) 610-615
    • (2003) Science , vol.301 , pp. 610-615
    • Abramson, J.1    Smirnova, I.2    Kasho, V.3    Verner, G.4    Kaback, H.R.5    Iwata, S.6
  • 6
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli
    • Huang Y., Lemieux M.J., Song J., Auer M., and Wang D.N. Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli. Science 301 (2003) 616-620
    • (2003) Science , vol.301 , pp. 616-620
    • Huang, Y.1    Lemieux, M.J.2    Song, J.3    Auer, M.4    Wang, D.N.5
  • 7
    • 33646445156 scopus 로고    scopus 로고
    • Structure of the multidrug transporter EmrD from Escherichia coli
    • Yin Y., He X., Szewczyk P., Nguyen T., and Chang G. Structure of the multidrug transporter EmrD from Escherichia coli. Science 312 (2006) 741-744
    • (2006) Science , vol.312 , pp. 741-744
    • Yin, Y.1    He, X.2    Szewczyk, P.3    Nguyen, T.4    Chang, G.5
  • 8
    • 1242317693 scopus 로고    scopus 로고
    • The SLC2 family of facilitated hexose and polyol transporters
    • Uldry M., and Thorens B. The SLC2 family of facilitated hexose and polyol transporters. Pflugers Arch. 447 (2004) 480-489
    • (2004) Pflugers Arch. , vol.447 , pp. 480-489
    • Uldry, M.1    Thorens, B.2
  • 9
    • 0030292743 scopus 로고    scopus 로고
    • Lilly lecture 1995. Glucose transport: pivotal step in insulin action
    • Kahn B.B. Lilly lecture 1995. Glucose transport: pivotal step in insulin action. Diabetes 45 (1996) 1644-1654
    • (1996) Diabetes , vol.45 , pp. 1644-1654
    • Kahn, B.B.1
  • 10
    • 57749111596 scopus 로고    scopus 로고
    • Nutrient transporters in cancer: relevance to Warburg hypothesis and beyond
    • Ganapathy V., Thangaraju M., and Prasad P.D. Nutrient transporters in cancer: relevance to Warburg hypothesis and beyond. Pharmacol. Ther. 121 (2009) 29-40
    • (2009) Pharmacol. Ther. , vol.121 , pp. 29-40
    • Ganapathy, V.1    Thangaraju, M.2    Prasad, P.D.3
  • 12
    • 0031879233 scopus 로고    scopus 로고
    • Fanconi-Bickel syndrome - a congenital defect of the liver-type facilitative glucose transporter. SSIEM Award. Society for the Study of Inborn Errors of Metabolism
    • Santer R., Schneppenheim R., Dombrowski A., Gotze H., Steinmann B., and Schaub J. Fanconi-Bickel syndrome - a congenital defect of the liver-type facilitative glucose transporter. SSIEM Award. Society for the Study of Inborn Errors of Metabolism. J. Inherit. Metab. Dis. 21 (1998) 191-194
    • (1998) J. Inherit. Metab. Dis. , vol.21 , pp. 191-194
    • Santer, R.1    Schneppenheim, R.2    Dombrowski, A.3    Gotze, H.4    Steinmann, B.5    Schaub, J.6
  • 13
    • 0036230647 scopus 로고    scopus 로고
    • Indinavir induces acute and reversible peripheral insulin resistance in rats
    • Hruz P.W., Murata H., Qiu H., and Mueckler M. Indinavir induces acute and reversible peripheral insulin resistance in rats. Diabetes 51 (2002) 937-942
    • (2002) Diabetes , vol.51 , pp. 937-942
    • Hruz, P.W.1    Murata, H.2    Qiu, H.3    Mueckler, M.4
  • 15
    • 0034798447 scopus 로고    scopus 로고
    • Structural analysis of the GLUT1 facilitative glucose transporter
    • (Review)
    • Hruz P.W., and Mueckler M.M. Structural analysis of the GLUT1 facilitative glucose transporter. Mol. Membr. Biol. 18 (2001) 183-193 (Review)
    • (2001) Mol. Membr. Biol. , vol.18 , pp. 183-193
    • Hruz, P.W.1    Mueckler, M.M.2
  • 16
    • 2942726276 scopus 로고    scopus 로고
    • Relative proximity and orientation of helices 4 and 8 of the GLUT1 glucose transporter
    • Alisio A., and Mueckler M. Relative proximity and orientation of helices 4 and 8 of the GLUT1 glucose transporter. J. Biol. Chem. 279 (2004) 26540-26545
    • (2004) J. Biol. Chem. , vol.279 , pp. 26540-26545
    • Alisio, A.1    Mueckler, M.2
  • 17
    • 33845983649 scopus 로고    scopus 로고
    • Transmembrane segment 12 of the Glut1 glucose transporter is an outer helix and is not directly involved in the transport mechanism
    • Mueckler M., and Makepeace C. Transmembrane segment 12 of the Glut1 glucose transporter is an outer helix and is not directly involved in the transport mechanism. J. Biol. Chem. 281 (2006) 11550-11555
    • (2006) J. Biol. Chem. , vol.281 , pp. 11550-11555
    • Mueckler, M.1    Makepeace, C.2
  • 18
    • 67649616342 scopus 로고    scopus 로고
    • Model of the exofacial substrate-binding site and helical folding of the human Glut1 glucose transporter based on scanning mutagenesis
    • Mueckler M., and Makepeace C. Model of the exofacial substrate-binding site and helical folding of the human Glut1 glucose transporter based on scanning mutagenesis. Biochemistry 48 (2009) 5934-5942
    • (2009) Biochemistry , vol.48 , pp. 5934-5942
    • Mueckler, M.1    Makepeace, C.2
  • 19
    • 61349105371 scopus 로고    scopus 로고
    • Analysis of glucose transporter topology and structural dynamics
    • Blodgett D.M., Graybill C., and Carruthers A. Analysis of glucose transporter topology and structural dynamics. J. Biol. Chem. 283 (2008) 36416-36424
    • (2008) J. Biol. Chem. , vol.283 , pp. 36416-36424
    • Blodgett, D.M.1    Graybill, C.2    Carruthers, A.3
  • 20
    • 14044251555 scopus 로고    scopus 로고
    • Quench-flow analysis reveals multiple phases of GluT1-mediated sugar transport
    • Blodgett D.M., and Carruthers A. Quench-flow analysis reveals multiple phases of GluT1-mediated sugar transport. Biochemistry 44 (2005) 2650-2660
    • (2005) Biochemistry , vol.44 , pp. 2650-2660
    • Blodgett, D.M.1    Carruthers, A.2
  • 21
    • 0020354832 scopus 로고
    • Monosaccharide transporter of the human erythrocyte. Characterization of an improved preparation
    • Baldwin S.A., Baldwin J.M., and Lienhard G.E. Monosaccharide transporter of the human erythrocyte. Characterization of an improved preparation. Biochemistry 21 (1982) 3836-3842
    • (1982) Biochemistry , vol.21 , pp. 3836-3842
    • Baldwin, S.A.1    Baldwin, J.M.2    Lienhard, G.E.3
  • 22
    • 0034959596 scopus 로고    scopus 로고
    • Purification and characterization of human erythrocyte glucose transporter in decylmaltoside detergent solution
    • Boulter J.M., and Wang D.N. Purification and characterization of human erythrocyte glucose transporter in decylmaltoside detergent solution. Protein Expr. Purif. 22 (2001) 337-348
    • (2001) Protein Expr. Purif. , vol.22 , pp. 337-348
    • Boulter, J.M.1    Wang, D.N.2
  • 23
    • 0017688926 scopus 로고
    • Reconstitution and purification of the d-glucose transporter from human erythrocytes
    • Kasahara M., and Hinkle P.C. Reconstitution and purification of the d-glucose transporter from human erythrocytes. J. Biol. Chem. 252 (1977) 7384-7390
    • (1977) J. Biol. Chem. , vol.252 , pp. 7384-7390
    • Kasahara, M.1    Hinkle, P.C.2
  • 24
    • 36048934083 scopus 로고    scopus 로고
    • Tissue-specific alterations of glucose transport and molecular mechanisms of intertissue communication in obesity and type 2 diabetes
    • Graham T.E., and Kahn B.B. Tissue-specific alterations of glucose transport and molecular mechanisms of intertissue communication in obesity and type 2 diabetes. Horm. Metab. Res. 39 (2007) 717-721
    • (2007) Horm. Metab. Res. , vol.39 , pp. 717-721
    • Graham, T.E.1    Kahn, B.B.2
  • 25
    • 0034617191 scopus 로고    scopus 로고
    • The mechanism of insulin resistance caused by HIV protease inhibitor therapy
    • Murata H., Hruz P.W., and Mueckler M. The mechanism of insulin resistance caused by HIV protease inhibitor therapy. J. Biol. Chem. 275 (2000) 20251-20254
    • (2000) J. Biol. Chem. , vol.275 , pp. 20251-20254
    • Murata, H.1    Hruz, P.W.2    Mueckler, M.3
  • 27
    • 0024592462 scopus 로고
    • Molecular cloning and characterization of an insulin-regulatable glucose transporter
    • James D.E., Strube M., and Mueckler M. Molecular cloning and characterization of an insulin-regulatable glucose transporter. Nature 338 (1989) 83-87
    • (1989) Nature , vol.338 , pp. 83-87
    • James, D.E.1    Strube, M.2    Mueckler, M.3
  • 28
    • 0027997421 scopus 로고
    • Glutamine 161 of Glut1 glucose transporter is critical for transport activity and exofacial ligand binding
    • Mueckler M., Weng W., and Kruse M. Glutamine 161 of Glut1 glucose transporter is critical for transport activity and exofacial ligand binding. J. Biol. Chem. 269 (1994) 20533-20538
    • (1994) J. Biol. Chem. , vol.269 , pp. 20533-20538
    • Mueckler, M.1    Weng, W.2    Kruse, M.3
  • 29
    • 0027426256 scopus 로고
    • Domains that confer intracellular sequestration of the Glut4 glucose transporter in Xenopus oocytes
    • Marshall B.A., Murata H., Hresko R.C., and Mueckler M. Domains that confer intracellular sequestration of the Glut4 glucose transporter in Xenopus oocytes. J. Biol. Chem. 268 (1993) 26193-26199
    • (1993) J. Biol. Chem. , vol.268 , pp. 26193-26199
    • Marshall, B.A.1    Murata, H.2    Hresko, R.C.3    Mueckler, M.4
  • 30
    • 0024328412 scopus 로고
    • Side-specific photolabelling of the hexose transporter
    • Holman G.D. Side-specific photolabelling of the hexose transporter. Biochem. Soc. Trans. 17 (1989) 438-440
    • (1989) Biochem. Soc. Trans. , vol.17 , pp. 438-440
    • Holman, G.D.1
  • 31
    • 34548852630 scopus 로고    scopus 로고
    • Control of inward rectifier K channel activity by lipid tethering of cytoplasmic domains
    • Enkvetchakul D., Jeliazkova I., Bhattacharyya J., and Nichols C.G. Control of inward rectifier K channel activity by lipid tethering of cytoplasmic domains. J. Gen. Physiol. 130 (2007) 329-334
    • (2007) J. Gen. Physiol. , vol.130 , pp. 329-334
    • Enkvetchakul, D.1    Jeliazkova, I.2    Bhattacharyya, J.3    Nichols, C.G.4
  • 32
    • 36248982122 scopus 로고    scopus 로고
    • Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment
    • Long S.B., Tao X., Campbell E.B., and MacKinnon R. Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment. Nature 450 (2007) 376-382
    • (2007) Nature , vol.450 , pp. 376-382
    • Long, S.B.1    Tao, X.2    Campbell, E.B.3    MacKinnon, R.4
  • 33
    • 0018082681 scopus 로고
    • The monosaccharide transport system of the human erythrocyte. Solubilization and characterization on the basis of cytochalasin B binding
    • Zoccoli M.A., Baldwin S.A., and Lienhard G.E. The monosaccharide transport system of the human erythrocyte. Solubilization and characterization on the basis of cytochalasin B binding. J. Biol. Chem. 253 (1978) 6923-6930
    • (1978) J. Biol. Chem. , vol.253 , pp. 6923-6930
    • Zoccoli, M.A.1    Baldwin, S.A.2    Lienhard, G.E.3
  • 34
    • 0025329803 scopus 로고
    • Human facilitative glucose transporters. Isolation, functional characterization, and gene localization of cDNAs encoding an isoform (GLUT5) expressed in small intestine, kidney, muscle, and adipose tissue and an unusual glucose transporter pseudogene-like sequence (GLUT6)
    • Kayano T., Burant C.F., Fukumoto H., Gould G.W., Fan Y.S., Eddy R.L., Byers M.G., Shows T.B., Seino S., and Bell G.I. Human facilitative glucose transporters. Isolation, functional characterization, and gene localization of cDNAs encoding an isoform (GLUT5) expressed in small intestine, kidney, muscle, and adipose tissue and an unusual glucose transporter pseudogene-like sequence (GLUT6). J. Biol. Chem. 265 (1990) 13276-13282
    • (1990) J. Biol. Chem. , vol.265 , pp. 13276-13282
    • Kayano, T.1    Burant, C.F.2    Fukumoto, H.3    Gould, G.W.4    Fan, Y.S.5    Eddy, R.L.6    Byers, M.G.7    Shows, T.B.8    Seino, S.9    Bell, G.I.10
  • 35
    • 0029160354 scopus 로고
    • From triple cysteine mutants to the cysteine-less glucose transporter GLUT1: a functional analysis
    • Wellner M., Monden I., and Keller K. From triple cysteine mutants to the cysteine-less glucose transporter GLUT1: a functional analysis. FEBS Lett. 370 (1995) 19-22
    • (1995) FEBS Lett. , vol.370 , pp. 19-22
    • Wellner, M.1    Monden, I.2    Keller, K.3
  • 36
    • 0032521442 scopus 로고    scopus 로고
    • Cell-surface biotinylation of GLUT4 using bis-mannose photolabels
    • Koumanov F., Yang J., Jones A.E., Hatanaka Y., and Holman G.D. Cell-surface biotinylation of GLUT4 using bis-mannose photolabels. Biochem. J. 330 Pt. 3 (1998) 1209-1215
    • (1998) Biochem. J. , vol.330 , Issue.PART 3 , pp. 1209-1215
    • Koumanov, F.1    Yang, J.2    Jones, A.E.3    Hatanaka, Y.4    Holman, G.D.5
  • 37
    • 0019039067 scopus 로고
    • The monosaccharide transport system of the human erythrocyte. Orientation upon reconstitution
    • Baldwin J.M., Lienhard G.E., and Baldwin S.A. The monosaccharide transport system of the human erythrocyte. Orientation upon reconstitution. Biochim. Biophys. Acta 599 (1980) 699-714
    • (1980) Biochim. Biophys. Acta , vol.599 , pp. 699-714
    • Baldwin, J.M.1    Lienhard, G.E.2    Baldwin, S.A.3
  • 38
    • 0343945299 scopus 로고
    • Facilitated transfer of hexoses across the human erythrocyte membrane
    • Widdas W.F. Facilitated transfer of hexoses across the human erythrocyte membrane. J. Physiol. 125 (1954) 163-180
    • (1954) J. Physiol. , vol.125 , pp. 163-180
    • Widdas, W.F.1
  • 39
    • 0028152377 scopus 로고
    • Facilitative glucose transporters
    • Mueckler M. Facilitative glucose transporters. Eur. J. Biochem. 219 (1994) 713-725
    • (1994) Eur. J. Biochem. , vol.219 , pp. 713-725
    • Mueckler, M.1
  • 40
    • 0029849743 scopus 로고    scopus 로고
    • Structure, function, and regulation of the mammalian facilitative glucose transporter gene family
    • Olson A.L., and Pessin J.E. Structure, function, and regulation of the mammalian facilitative glucose transporter gene family. Annu. Rev. Nutr. 16 (1996) 235-256
    • (1996) Annu. Rev. Nutr. , vol.16 , pp. 235-256
    • Olson, A.L.1    Pessin, J.E.2
  • 41
    • 34247842999 scopus 로고    scopus 로고
    • Functional properties and genomics of glucose transporters
    • Zhao F.Q., and Keating A.F. Functional properties and genomics of glucose transporters. Curr. Genomics 8 (2007) 113-128
    • (2007) Curr. Genomics , vol.8 , pp. 113-128
    • Zhao, F.Q.1    Keating, A.F.2
  • 42
    • 0037000620 scopus 로고    scopus 로고
    • Glucose transporter 1 deficiency syndrome and other glycolytic defects
    • 3S15-3S23 (discussion 3S24-3S25)
    • De Vivo D.C., Leary L., and Wang D. Glucose transporter 1 deficiency syndrome and other glycolytic defects. J. Child Neurol. 17 Suppl. 3 (2002) 3S15-3S23 (discussion 3S24-3S25)
    • (2002) J. Child Neurol. , vol.17 , Issue.SUPPL. 3
    • De Vivo, D.C.1    Leary, L.2    Wang, D.3
  • 43
    • 0023158728 scopus 로고
    • Elevated levels of glucose transport and transporter messenger RNA are induced by ras or src oncogenes
    • Flier J.S., Mueckler M.M., Usher P., and Lodish H.F. Elevated levels of glucose transport and transporter messenger RNA are induced by ras or src oncogenes. Science 235 (1987) 1492-1495
    • (1987) Science , vol.235 , pp. 1492-1495
    • Flier, J.S.1    Mueckler, M.M.2    Usher, P.3    Lodish, H.F.4
  • 44
    • 34548099721 scopus 로고    scopus 로고
    • Eukaryotic major facilitator superfamily transporter modeling based on the prokaryotic GlpT crystal structure
    • Lemieux M.J. Eukaryotic major facilitator superfamily transporter modeling based on the prokaryotic GlpT crystal structure. Mol. Membr. Biol. 24 (2007) 333-341
    • (2007) Mol. Membr. Biol. , vol.24 , pp. 333-341
    • Lemieux, M.J.1
  • 45
    • 53849119555 scopus 로고    scopus 로고
    • Ins and outs of major facilitator superfamily antiporters
    • Law C.J., Maloney P.C., and Wang D.N. Ins and outs of major facilitator superfamily antiporters. Annu. Rev. Microbiol. 62 (2008) 289-305
    • (2008) Annu. Rev. Microbiol. , vol.62 , pp. 289-305
    • Law, C.J.1    Maloney, P.C.2    Wang, D.N.3
  • 46
    • 55449113709 scopus 로고    scopus 로고
    • Comparative analyses of fundamental differences in membrane transport capabilities in prokaryotes and eukaryotes
    • Ren Q., and Paulsen I.T. Comparative analyses of fundamental differences in membrane transport capabilities in prokaryotes and eukaryotes. PLoS Comput. Biol. 1 (2005) e27
    • (2005) PLoS Comput. Biol. , vol.1
    • Ren, Q.1    Paulsen, I.T.2
  • 47
  • 48
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
    • Long S.B., Campbell E.B., and Mackinnon R. Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science 309 (2005) 897-903
    • (2005) Science , vol.309 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.