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Volumn 96, Issue 1, 2009, Pages 32-37

Structure-function study of the glucose-6-phosphate transporter, an eukaryotic antiporter deficient in glycogen storage disease type Ib

Author keywords

Antiporter; Endoplasmic reticulum; G6P transport; Glycogen storage disease type I; Glycosylation scanning; Phosphate transport

Indexed keywords

AMINO ACID; ANTIPORTER; GLUCOSE 6 PHOSPHATE TRANSPORTER; HEXOSE PHOSPHATE; HEXOSE PHOSPHATE TRANSPORTER UHPT; PHOSPHATE TRANSPORTER; PROTEINASE; UNCLASSIFIED DRUG;

EID: 57649103649     PISSN: 10967192     EISSN: 10967206     Source Type: Journal    
DOI: 10.1016/j.ymgme.2008.10.005     Document Type: Article
Times cited : (21)

References (30)
  • 1
    • 0036086034 scopus 로고    scopus 로고
    • Type I glycogen storage diseases: disorders of the glucose-6-phosphatase complex
    • Chou J.Y., Matern D., Mansfield B.C., and Chen Y.-T. Type I glycogen storage diseases: disorders of the glucose-6-phosphatase complex. Curr. Mol. Med. 2 (2002) 121-143
    • (2002) Curr. Mol. Med. , vol.2 , pp. 121-143
    • Chou, J.Y.1    Matern, D.2    Mansfield, B.C.3    Chen, Y.-T.4
  • 2
    • 32444436610 scopus 로고    scopus 로고
    • Glucose-6-phosphate transporter: the key to glycogen storage disease type Ib
    • Broer S., and Wagner C.A. (Eds), Kluwer Academic/Plenum Publishers, New York
    • Chou J.Y., and Mansfield B.C. Glucose-6-phosphate transporter: the key to glycogen storage disease type Ib. In: Broer S., and Wagner C.A. (Eds). Membrane Transporter Diseases (2003), Kluwer Academic/Plenum Publishers, New York 191-205
    • (2003) Membrane Transporter Diseases , pp. 191-205
    • Chou, J.Y.1    Mansfield, B.C.2
  • 3
    • 0345306587 scopus 로고    scopus 로고
    • Glucose-6-phosphate hydrolase, widely expressed outside the liver, can explain age-dependent resolution of hypoglycemia in glycogen storage disease type Ia
    • Shieh J.-J., Pan C.-J., Mansfield B.C., and Chou J.Y. Glucose-6-phosphate hydrolase, widely expressed outside the liver, can explain age-dependent resolution of hypoglycemia in glycogen storage disease type Ia. J. Biol. Chem. 278 (2003) 47098-47103
    • (2003) J. Biol. Chem. , vol.278 , pp. 47098-47103
    • Shieh, J.-J.1    Pan, C.-J.2    Mansfield, B.C.3    Chou, J.Y.4
  • 4
    • 1842582072 scopus 로고    scopus 로고
    • Histidine-167 is the phosphate acceptor in glucose-6-phosphatase-β forming a phosphohistidine-enzyme intermediate during catalysis
    • Ghosh A., Shieh J.-J., Pan C.-J., and Chou J.Y. Histidine-167 is the phosphate acceptor in glucose-6-phosphatase-β forming a phosphohistidine-enzyme intermediate during catalysis. J. Biol. Chem. 279 (2004) 12479-12483
    • (2004) J. Biol. Chem. , vol.279 , pp. 12479-12483
    • Ghosh, A.1    Shieh, J.-J.2    Pan, C.-J.3    Chou, J.Y.4
  • 6
    • 47049108414 scopus 로고    scopus 로고
    • Neutrophil stress and apoptosis underlie myeloid dysfunction in glycogen storage disease type Ib
    • Kim S.Y., Jun H.S., Mead P.A., Mansfield B.C., and Chou J.Y. Neutrophil stress and apoptosis underlie myeloid dysfunction in glycogen storage disease type Ib. Blood 111 (2008) 5704-5711
    • (2008) Blood , vol.111 , pp. 5704-5711
    • Kim, S.Y.1    Jun, H.S.2    Mead, P.A.3    Mansfield, B.C.4    Chou, J.Y.5
  • 7
    • 0033553477 scopus 로고    scopus 로고
    • Transmembrane topology of human Glucose-6-phosphate transporter
    • Pan C.-J., Lin B., and Chou J.Y. Transmembrane topology of human Glucose-6-phosphate transporter. J. Biol. Chem. 274 (1999) 13865-13869
    • (1999) J. Biol. Chem. , vol.274 , pp. 13865-13869
    • Pan, C.-J.1    Lin, B.2    Chou, J.Y.3
  • 8
    • 0000207681 scopus 로고
    • TMbase-a database of membrane spanning protein segments
    • Hoffman K., and Stoffel W. TMbase-a database of membrane spanning protein segments. Biol. Chem. Hoppe-Seyler 347 (1993) 166-170
    • (1993) Biol. Chem. Hoppe-Seyler , vol.347 , pp. 166-170
    • Hoffman, K.1    Stoffel, W.2
  • 9
    • 0031448837 scopus 로고    scopus 로고
    • Sequence of a putative glucose-6-phosphate translocase, mutated in glycogen storage disease type 1b
    • Gerin I., Veiga-da-Cunha M., Achouri Y., Collet J.-F., and Van Schaftingen E. Sequence of a putative glucose-6-phosphate translocase, mutated in glycogen storage disease type 1b. FEBS Lett. 419 (1997) 235-238
    • (1997) FEBS Lett. , vol.419 , pp. 235-238
    • Gerin, I.1    Veiga-da-Cunha, M.2    Achouri, Y.3    Collet, J.-F.4    Van Schaftingen, E.5
  • 11
    • 0023719174 scopus 로고
    • Nucleotide sequence and transcription start point of the phosphoglycerate transporter gene of Salmonella typhimurium
    • Goldrick D., Yu G.Q., Jiang S.Q., and Hong J.S. Nucleotide sequence and transcription start point of the phosphoglycerate transporter gene of Salmonella typhimurium. J. Bacteriol. 179 (1988) 3421-3426
    • (1988) J. Bacteriol. , vol.179 , pp. 3421-3426
    • Goldrick, D.1    Yu, G.Q.2    Jiang, S.Q.3    Hong, J.S.4
  • 13
    • 0023000305 scopus 로고
    • Reconstitution of sugar phosphate transport systems of Escherichia coli
    • Ambudkar S.V., Larson T.J., and Maloney P.C. Reconstitution of sugar phosphate transport systems of Escherichia coli. J. Biol. Chem. 261 (1986) 9083-9086
    • (1986) J. Biol. Chem. , vol.261 , pp. 9083-9086
    • Ambudkar, S.V.1    Larson, T.J.2    Maloney, P.C.3
  • 14
    • 46749112999 scopus 로고    scopus 로고
    • The glucose-6-phosphate transporter is a phosphate-linked antiporter deficient in glycogen storage disease type Ib and Ic
    • Chen S.Y., Pan C.J., Krishnamachary N., Mansfield B.C., Ambudkar S.V., and Chou J.Y. The glucose-6-phosphate transporter is a phosphate-linked antiporter deficient in glycogen storage disease type Ib and Ic. FASEB J. 22 (2008) 2206-2213
    • (2008) FASEB J. , vol.22 , pp. 2206-2213
    • Chen, S.Y.1    Pan, C.J.2    Krishnamachary, N.3    Mansfield, B.C.4    Ambudkar, S.V.5    Chou, J.Y.6
  • 15
    • 0032528196 scopus 로고    scopus 로고
    • Identification of two essential arginine residues in UhpT, the sugar phosphate antiporter of Escherichia coli
    • Fann M.C., Davies A.H., Varadhachary A., Kuroda T., Sevier C., Tsuchiya T., and Maloney P.C. Identification of two essential arginine residues in UhpT, the sugar phosphate antiporter of Escherichia coli. Membrane Biol. 164 (1998) 187-195
    • (1998) Membrane Biol. , vol.164 , pp. 187-195
    • Fann, M.C.1    Davies, A.H.2    Varadhachary, A.3    Kuroda, T.4    Sevier, C.5    Tsuchiya, T.6    Maloney, P.C.7
  • 16
    • 0033525543 scopus 로고    scopus 로고
    • Altered substrate selectivity in a mutant of an intrahelical salt bridge in UhpT, the sugar phosphate carrier of Escherichia coli
    • Hall J.A., Fann M.C., and Maloney P.C. Altered substrate selectivity in a mutant of an intrahelical salt bridge in UhpT, the sugar phosphate carrier of Escherichia coli. J. Biol. Chem. 274 (1999) 6148-6153
    • (1999) J. Biol. Chem. , vol.274 , pp. 6148-6153
    • Hall, J.A.1    Fann, M.C.2    Maloney, P.C.3
  • 17
    • 0345276579 scopus 로고    scopus 로고
    • Three-dimensional crystallization of the Escherichia coli glycerol-3-phosphate transporter: a member of the major facilitator superfamily
    • Lemieux M.J., Song J., Kim M.J., Huang Y., Villa A., Auer M., Li X.D., and Wang D.N. Three-dimensional crystallization of the Escherichia coli glycerol-3-phosphate transporter: a member of the major facilitator superfamily. Protein Sci. 12 (2003) 2748-2756
    • (2003) Protein Sci. , vol.12 , pp. 2748-2756
    • Lemieux, M.J.1    Song, J.2    Kim, M.J.3    Huang, Y.4    Villa, A.5    Auer, M.6    Li, X.D.7    Wang, D.N.8
  • 18
    • 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
  • 19
    • 3242729357 scopus 로고    scopus 로고
    • Homology modeling of the human microsomal glucose 6-phosphate transporter explains the mutations that cause the glycogen storage disease type Ib
    • Almqvist J., Huang Y., Hovmöller S., and Wang D.N. Homology modeling of the human microsomal glucose 6-phosphate transporter explains the mutations that cause the glycogen storage disease type Ib. Biochemistry 43 (2004) 9289-9297
    • (2004) Biochemistry , vol.43 , pp. 9289-9297
    • Almqvist, J.1    Huang, Y.2    Hovmöller, S.3    Wang, D.N.4
  • 20
    • 0036899098 scopus 로고    scopus 로고
    • Structure-function analysis of the glucose-6-phosphate transporter deficient in glycogen storage disease type Ib
    • Chen L.-Y., Pan C.-J., Shieh J.-J., and Chou J.Y. Structure-function analysis of the glucose-6-phosphate transporter deficient in glycogen storage disease type Ib. Hum. Mol. Genet. 11 (2002) 3199-3207
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 3199-3207
    • Chen, L.-Y.1    Pan, C.-J.2    Shieh, J.-J.3    Chou, J.Y.4
  • 21
    • 0031055468 scopus 로고    scopus 로고
    • Construction of adenovirus vectors through Cre-lox recombination
    • Hardy S., Kitamura M., Harris-Stansil T., Dai Y., and Phipps M.L. Construction of adenovirus vectors through Cre-lox recombination. J. Virol. 71 (1997) 1842-1849
    • (1997) J. Virol. , vol.71 , pp. 1842-1849
    • Hardy, S.1    Kitamura, M.2    Harris-Stansil, T.3    Dai, Y.4    Phipps, M.L.5
  • 22
    • 0037031827 scopus 로고    scopus 로고
    • 176 is the nucleophile forming the phosphohistidine-enzyme intermediate during catalysis
    • 176 is the nucleophile forming the phosphohistidine-enzyme intermediate during catalysis. J. Biol. Chem. 277 (2002) 32837-32842
    • (2002) J. Biol. Chem. , vol.277 , pp. 32837-32842
    • Ghosh, A.1    Shieh, J.-J.2    Pan, C.-J.3    Sun, M.-S.4    Chou, J.Y.5
  • 23
    • 0025991471 scopus 로고
    • Evidence for a membrane exchangeable glucose pool in the functioning of rat liver glucose-6-phosphatase
    • Berteloot A., Vidal H., and van de Werve G. Evidence for a membrane exchangeable glucose pool in the functioning of rat liver glucose-6-phosphatase. J. Biol. Chem. 266 (1991) 5497-5507
    • (1991) J. Biol. Chem. , vol.266 , pp. 5497-5507
    • Berteloot, A.1    Vidal, H.2    van de Werve, G.3
  • 24
    • 0015716692 scopus 로고
    • A rapid, sensitive, and specific method for the determination of protein in dilute solution
    • Schaffner W., and Weissmann C. A rapid, sensitive, and specific method for the determination of protein in dilute solution. Anal. Biochem. 56 (1973) 502-514
    • (1973) Anal. Biochem. , vol.56 , pp. 502-514
    • Schaffner, W.1    Weissmann, C.2
  • 25
    • 0021277078 scopus 로고
    • Calcium efflux from Escherichia coli. Evidence for two systems
    • Ambudkar S.V., Zlotnick G.W., and Rosen B.P. Calcium efflux from Escherichia coli. Evidence for two systems. J. Biol. Chem. 259 (1984) 6142-6146
    • (1984) J. Biol. Chem. , vol.259 , pp. 6142-6146
    • Ambudkar, S.V.1    Zlotnick, G.W.2    Rosen, B.P.3
  • 26
    • 0000102915 scopus 로고
    • Multifunctional glucose-6-phosphatase: a critical review
    • Martonosi A.N. (Ed), Plenum Press, New York
    • Nordlie R.C., and Sukalski K.A. Multifunctional glucose-6-phosphatase: a critical review. In: Martonosi A.N. (Ed). The Enzymes of Biological Membranes. 2rd ed. (1985), Plenum Press, New York 349-398
    • (1985) The Enzymes of Biological Membranes. 2rd ed. , pp. 349-398
    • Nordlie, R.C.1    Sukalski, K.A.2
  • 27
    • 0033782777 scopus 로고    scopus 로고
    • Protein glucosylation and its role in protein folding
    • Parodi A.J. Protein glucosylation and its role in protein folding. Annu. Rev. Biochem. 69 (2000) 69-93
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 69-93
    • Parodi, A.J.1
  • 28
    • 0035979713 scopus 로고    scopus 로고
    • Topogenesis of membrane proteins: determinants and dynamics
    • Goder V., and Spiess M. Topogenesis of membrane proteins: determinants and dynamics. FEBS Lett. 504 (2001) 87-93
    • (2001) FEBS Lett. , vol.504 , pp. 87-93
    • Goder, V.1    Spiess, M.2
  • 29
    • 34248997838 scopus 로고    scopus 로고
    • N-glycan structure dictates extension of protein folding or onset of disposal
    • Molinari M. N-glycan structure dictates extension of protein folding or onset of disposal. Nat. Chem. Biol. 3 (2007) 313-320
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 313-320
    • Molinari, M.1
  • 30
    • 36249022072 scopus 로고    scopus 로고
    • How sugars convey information on protein conformation in the endoplasmic reticulum
    • Caramelo J.J., and Parodi A.J. How sugars convey information on protein conformation in the endoplasmic reticulum. Semin. Cell Dev. Biol. 18 (2007) 732-742
    • (2007) Semin. Cell Dev. Biol. , vol.18 , pp. 732-742
    • Caramelo, J.J.1    Parodi, A.J.2


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