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Volumn 113, Issue 17, 2016, Pages 4711-4716

Mechanism of inhibition of human glucose transporter GLUT1 is conserved between cytochalasin B and phenylalanine amides

Author keywords

Cytochalasin B; Glucose facilitator; GLUT inhibitor; Human MFS transporter; X ray structure

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMIDE; BROMINE; CYTOCHALASIN B; GLUCOSE; GLUCOSE TRANSPORTER 1; HYDROGEN; LUCIFERIN; PHENYLALANINE; CYTOCHALASIN; CYTOCHALASIN A; PHENYLALANINE AMIDE; PROTEIN BINDING; SLC2A1 PROTEIN, HUMAN;

EID: 84964725539     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1603735113     Document Type: Article
Times cited : (168)

References (38)
  • 1
    • 0025716308 scopus 로고
    • Homologous sugar transport proteins in Escherichia coli and their relatives in both prokaryotes and eukaryotes
    • Henderson PJ, Maiden MC (1990) Homologous sugar transport proteins in Escherichia coli and their relatives in both prokaryotes and eukaryotes. Philos Trans R Soc Lond B Biol Sci 326(1236):391-410.
    • (1990) Philos Trans R Soc Lond B Biol Sci , vol.326 , Issue.1236 , pp. 391-410
    • Henderson, P.J.1    Maiden, M.C.2
  • 2
    • 0022360064 scopus 로고
    • Sequence and structure of a human glucose transporter
    • Mueckler M, et al. (1985) Sequence and structure of a human glucose transporter. Science 229(4717):941-945.
    • (1985) Science , vol.229 , Issue.4717 , pp. 941-945
    • Mueckler, M.1
  • 3
    • 0029849743 scopus 로고    scopus 로고
    • Structure, function, and regulation of the mammalian facilitative glucose transporter gene family
    • Olson AL, Pessin JE (1996) Structure, function, and regulation of the mammalian facilitative glucose transporter gene family. Annu Rev Nutr 16:235-256.
    • (1996) Annu Rev Nutr , vol.16 , pp. 235-256
    • Olson, A.L.1    Pessin, J.E.2
  • 4
    • 84956673642 scopus 로고    scopus 로고
    • Disorders of glucose transport
    • eds Saudubray JM, van den Berghe G, Walter JH Springer New York
    • Santer R, Klepper J (2011) Disorders of glucose transport. Inborn Metabolic Diseases: Diagnosis and Treatment, eds Saudubray JM, van den Berghe G, Walter JH (Springer, New York), pp 175-181.
    • (2011) Inborn Metabolic Diseases: Diagnosis and Treatment , pp. 175-181
    • Santer, R.1    Klepper, J.2
  • 5
    • 12944262229 scopus 로고    scopus 로고
    • Molecular and cellular regulation of glucose transporter (GLUT) proteins in cancer
    • Macheda ML, Rogers S, Best JD (2005) Molecular and cellular regulation of glucose transporter (GLUT) proteins in cancer. J Cell Physiol 202(3):654-662.
    • (2005) J Cell Physiol , vol.202 , Issue.3 , pp. 654-662
    • Macheda, M.L.1    Rogers, S.2    Best, J.D.3
  • 6
    • 12444279265 scopus 로고
    • On the origin of cancer cells
    • Warburg O (1956) On the origin of cancer cells. Science 123(3191):309-314.
    • (1956) Science , vol.123 , Issue.3191 , pp. 309-314
    • Warburg, O.1
  • 7
    • 75349106751 scopus 로고    scopus 로고
    • GLUT1 as a therapeutic target in hepatocellular carcinoma
    • Amann T, Hellerbrand C (2009) GLUT1 as a therapeutic target in hepatocellular carcinoma. Expert Opin Ther Targets 13(12):1411-1427.
    • (2009) Expert Opin Ther Targets , vol.13 , Issue.12 , pp. 1411-1427
    • Amann, T.1    Hellerbrand, C.2
  • 8
    • 84879463466 scopus 로고    scopus 로고
    • Glucose transporter 1 (GLUT1) of anaerobic glycolysis as predictive and prognostic values in neoadjuvant chemoradiotherapy and laparoscopic surgery for locally advanced rectal cancer
    • Shim BY, et al. (2013) Glucose transporter 1 (GLUT1) of anaerobic glycolysis as predictive and prognostic values in neoadjuvant chemoradiotherapy and laparoscopic surgery for locally advanced rectal cancer. Int J Colorectal Dis 28(3):375-383.
    • (2013) Int J Colorectal Dis , vol.28 , Issue.3 , pp. 375-383
    • Shim, B.Y.1
  • 9
    • 84877133364 scopus 로고    scopus 로고
    • GLUT1 protein expression correlates with unfavourable histologic category and high risk in patients with neuroblastic tumours
    • Ramani P, Headford A, May MT (2013) GLUT1 protein expression correlates with unfavourable histologic category and high risk in patients with neuroblastic tumours. Virchows Arch 462(2):203-209.
    • (2013) Virchows Arch , vol.462 , Issue.2 , pp. 203-209
    • Ramani, P.1    Headford, A.2    May, M.T.3
  • 10
    • 34447513075 scopus 로고    scopus 로고
    • Hypoxic regulation of glucose transport, anaerobic metabolism and angiogenesis in cancer: Novel pathways and targets for anticancer therapeutics
    • Airley RE, Mobasheri A (2007) Hypoxic regulation of glucose transport, anaerobic metabolism and angiogenesis in cancer: Novel pathways and targets for anticancer therapeutics. Chemotherapy 53(4):233-256.
    • (2007) Chemotherapy , vol.53 , Issue.4 , pp. 233-256
    • Airley, R.E.1    Mobasheri, A.2
  • 11
    • 0022375120 scopus 로고
    • Inhibition of 3-O-methylglucose transport in human erythrocytes by forskolin
    • Sergeant S, Kim HD (1985) Inhibition of 3-O-methylglucose transport in human erythrocytes by forskolin. J Biol Chem 260(27):14677-14682.
    • (1985) J Biol Chem , vol.260 , Issue.27 , pp. 14677-14682
    • Sergeant, S.1    Kim, H.D.2
  • 12
    • 0025732373 scopus 로고
    • Inhibitions of sugar transport produced by ligands binding at opposite sides of the membrane Evidence for simultaneous occupation of the carrier by maltose and cytochalasin B
    • Carruthers A, Helgerson AL (1991) Inhibitions of sugar transport produced by ligands binding at opposite sides of the membrane. Evidence for simultaneous occupation of the carrier by maltose and cytochalasin B. Biochemistry 30(16):3907-3915.
    • (1991) Biochemistry , vol.30 , Issue.16 , pp. 3907-3915
    • Carruthers, A.1    Helgerson, A.L.2
  • 13
    • 84902002905 scopus 로고    scopus 로고
    • Crystal structure of the human glucose transporter GLUT1
    • Deng D, et al. (2014) Crystal structure of the human glucose transporter GLUT1. Nature 510(7503):121-125.
    • (2014) Nature , vol.510 , Issue.7503 , pp. 121-125
    • Deng, D.1
  • 14
    • 84938299834 scopus 로고    scopus 로고
    • Molecular basis of ligand recognition and transport by glucose transporters
    • Deng D, et al. (2015) Molecular basis of ligand recognition and transport by glucose transporters. Nature 526(7573):391-396.
    • (2015) Nature , vol.526 , Issue.7573 , pp. 391-396
    • Deng, D.1
  • 15
    • 0017399443 scopus 로고
    • Cytochalasin B binding sites and glucose transport carrier in human erythrocyte ghosts
    • Jung CY, Rampal AL (1977) Cytochalasin B binding sites and glucose transport carrier in human erythrocyte ghosts. J Biol Chem 252(15):5456-5463.
    • (1977) J Biol Chem , vol.252 , Issue.15 , pp. 5456-5463
    • Jung, C.Y.1    Rampal, A.L.2
  • 16
    • 77955984864 scopus 로고    scopus 로고
    • Overexpression and purification of integral membrane proteins in yeast
    • Hays FA, Roe-Zurz Z, Stroud RM (2010) Overexpression and purification of integral membrane proteins in yeast. Methods Enzymol 470:695-707.
    • (2010) Methods Enzymol , vol.470 , pp. 695-707
    • Hays, F.A.1    Roe-Zurz, Z.2    Stroud, R.M.3
  • 17
    • 0028043145 scopus 로고
    • Replacement of both tryptophan residues at 388 and 412 completely abolished cytochalasin B photolabelling of the GLUT1 glucose transporter
    • Inukai K, et al. (1994) Replacement of both tryptophan residues at 388 and 412 completely abolished cytochalasin B photolabelling of the GLUT1 glucose transporter. Biochem J 302(Pt 2):355-361.
    • (1994) Biochem J , vol.302 , pp. 355-361
    • Inukai, K.1
  • 18
    • 0025835070 scopus 로고
    • Substitution of leucine for tryptophan 412 does not abolish cytochalasin B labeling but markedly decreases the intrinsic activity of GLUT1 glucose transporter
    • Katagiri H, et al. (1991) Substitution of leucine for tryptophan 412 does not abolish cytochalasin B labeling but markedly decreases the intrinsic activity of GLUT1 glucose transporter. J Biol Chem 266(12):7769-7773.
    • (1991) J Biol Chem , vol.266 , Issue.12 , pp. 7769-7773
    • Katagiri, H.1
  • 19
    • 77953598589 scopus 로고    scopus 로고
    • The protein family of glucose transport facilitators: It's not only about glucose after all
    • Augustin R (2010) The protein family of glucose transport facilitators: It's not only about glucose after all. IUBMB Life 62(5):315-333.
    • (2010) IUBMB Life , vol.62 , Issue.5 , pp. 315-333
    • Augustin, R.1
  • 20
    • 0035831170 scopus 로고    scopus 로고
    • Adenosine and adenosine triphosphate modulate the substrate binding affinity of glucose transporter GLUT1 in vitro
    • Lachaal M, Spangler RA, Jung CY (2001) Adenosine and adenosine triphosphate modulate the substrate binding affinity of glucose transporter GLUT1 in vitro. Biochim Biophys Acta 1511(1):123-133.
    • (2001) Biochim Biophys Acta , vol.1511 , Issue.1 , pp. 123-133
    • Lachaal, M.1    Spangler, R.A.2    Jung, C.Y.3
  • 21
    • 0029557683 scopus 로고
    • The role of tryptophans 371 and 395 in the binding of antibiotics and the transport of sugars by the D-galactose-H+ symport protein (GalP) from Escherichia coli
    • McDonald TP, Walmsley AR, Martin GE, Henderson PJ (1995) The role of tryptophans 371 and 395 in the binding of antibiotics and the transport of sugars by the D-galactose-H+ symport protein (GalP) from Escherichia coli. J Biol Chem 270(51):30359-30370.
    • (1995) J Biol Chem , vol.270 , Issue.51 , pp. 30359-30370
    • McDonald, T.P.1    Walmsley, A.R.2    Martin, G.E.3    Henderson, P.J.4
  • 22
    • 0030943846 scopus 로고    scopus 로고
    • Asparagine 394 in putative helix 11 of the galactose-H+ symport protein (GalP) from Escherichia coli is associated with the internal binding site for cytochalasin B and sugar
    • McDonald TP, Walmsley AR, Henderson PJ (1997) Asparagine 394 in putative helix 11 of the galactose-H+ symport protein (GalP) from Escherichia coli is associated with the internal binding site for cytochalasin B and sugar. J Biol Chem 272(24):15189-15199.
    • (1997) J Biol Chem , vol.272 , Issue.24 , pp. 15189-15199
    • McDonald, T.P.1    Walmsley, A.R.2    Henderson, P.J.3
  • 23
    • 33644874235 scopus 로고    scopus 로고
    • The integration of macromolecular diffraction data
    • Leslie AG (2006) The integration of macromolecular diffraction data. Acta Crystallogr D Biol Crystallogr 62(Pt 1):48-57.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 48-57
    • Leslie, A.G.1
  • 24
    • 79953737180 scopus 로고    scopus 로고
    • Overview of the CCP4 suite and current developments
    • Winn MD, et al. (2011) Overview of the CCP4 suite and current developments. Acta Crystallogr D Biol Crystallogr 67(Pt 4):235-242.
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , pp. 235-242
    • Winn, M.D.1
  • 25
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • Evans P (2006) Scaling and assessment of data quality. Acta Crystallogr D Biol Crystallogr 62(Pt 1):72-82.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 72-82
    • Evans, P.1
  • 26
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • eds Abelson JN, Simon MI, Carter CW, Jr, Sweet RM (Academic, New York
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods in Enzymology, eds Abelson JN, Simon MI, Carter CW, Jr, Sweet RM (Academic, New York), Vol 276, pp 307-326.
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 27
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • Karplus PA, Diederichs K (2012) Linking crystallographic model and data quality. Science 336(6084):1030-1033.
    • (2012) Science , vol.336 , Issue.6084 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2
  • 28
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66(Pt 2):213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 29
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60(Pt 12 Pt 1):2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 30
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • Web Server issue
    • Davis IW, et al. (2007) MolProbity: All-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 35(Web Server issue):W375-W383.
    • (2007) Nucleic Acids Res , vol.35 , pp. 375-383
    • Davis, I.W.1
  • 31
    • 67650358909 scopus 로고    scopus 로고
    • QMEAN server for protein model quality estimation
    • Web Server issue
    • Benkert P, Kunzli M, Schwede T (2009) QMEAN server for protein model quality estimation. Nucleic Acids Res 37(Web Server issue):W510-W514.
    • (2009) Nucleic Acids Res , vol.37 , pp. 510-514
    • Benkert, P.1    Kunzli, M.2    Schwede, T.3
  • 33
    • 12144289984 scopus 로고    scopus 로고
    • Glide: A new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy
    • Friesner RA, et al. (2004) Glide: A new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy. J Med Chem 47(7):1739-1749.
    • (2004) J Med Chem , vol.47 , Issue.7 , pp. 1739-1749
    • Friesner, R.A.1
  • 34
    • 84860390215 scopus 로고    scopus 로고
    • The VSGB 2.0 model: A next generation energy model for high resolution protein structure modeling
    • Li J, et al. (2011) The VSGB 2.0 model: A next generation energy model for high resolution protein structure modeling. Proteins 79(10):2794-2812.
    • (2011) Proteins , vol.79 , Issue.10 , pp. 2794-2812
    • Li, J.1
  • 35
    • 79951815565 scopus 로고    scopus 로고
    • A pairwise chemical genetic screen identifies new inhibitors of glucose transport
    • Ulanovskaya OA, Cui J, Kron SJ, Kozmin SA (2011) A pairwise chemical genetic screen identifies new inhibitors of glucose transport. Chem Biol 18(2):222-230.
    • (2011) Chem Biol , vol.18 , Issue.2 , pp. 222-230
    • Ulanovskaya, O.A.1    Cui, J.2    Kron, S.J.3    Kozmin, S.A.4
  • 36
    • 45549099845 scopus 로고    scopus 로고
    • Synthesis enables identification of the cellular target of leucascandrolide A and neopeltolide
    • Ulanovskaya OA, et al. (2008) Synthesis enables identification of the cellular target of leucascandrolide A and neopeltolide. Nat Chem Biol 4(7):418-424.
    • (2008) Nat Chem Biol , vol.4 , Issue.7 , pp. 418-424
    • Ulanovskaya, O.A.1
  • 37
    • 0025872644 scopus 로고
    • Membrane-permeable luciferin esters for assay of firefly luciferase in live intact cells
    • Craig FF, Simmonds AC, Watmore D, McCapra F, White MR (1991) Membrane-permeable luciferin esters for assay of firefly luciferase in live intact cells. Biochem J 276(Pt 3):637-641.
    • (1991) Biochem J , vol.276 , pp. 637-641
    • Craig, F.F.1    Simmonds, A.C.2    Watmore, D.3    McCapra, F.4    White, M.R.5
  • 38
    • 0035066836 scopus 로고    scopus 로고
    • Global indicators of X-ray data quality
    • Weiss MS (2001) Global indicators of X-ray data quality. J Appl Crystallog 34:130-135.
    • (2001) J Appl Crystallog , vol.34 , pp. 130-135
    • Weiss, M.S.1


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