Coupled sodium/glucose cotransport by SGLT1 requires a negative charge at position 454

Biochemistry

Volumn 43, Issue 41, 2004, Pages 13175-13184

  Díez Sampedro, Ana ^a,b   Loo, Donald D F ^a   Wright, Ernest M ^a   Zampighi, Guido A ^a   Hirayama, Bruce A ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; ELECTRIC POTENTIAL; MUTAGENESIS; SENSITIVITY ANALYSIS; SODIUM; STOICHIOMETRY;

ELECTROCHEMICAL GRADIENTS; GLUCOSE-BINDING DOMAINS; LIGANDS; PLASMA MEMBRANES;

GLUCOSE;

ASPARAGINE; COTRANSPORTER; CYSTEINE; GLUCOSE; HISTIDINE; SODIUM GLUCOSE COTRANSPORTER 1; SODIUM ION; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; BINDING AFFINITY; BINDING SITE; CELL MEMBRANE; CELL MEMBRANE POTENTIAL; CHEMICAL MUTAGENESIS; CONTROLLED STUDY; ELECTROCHEMISTRY; FLUORESCENCE ANALYSIS; GLUCOSE TRANSPORT; MOLECULAR INTERACTION; NONHUMAN; OOCYTE; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; SODIUM TRANSPORT; SUGAR TRANSPORT; XENOPUS LAEVIS;

ANIMALS; ASPARTIC ACID; CELL MEMBRANE; CYSTEINE; GLUCOSE; HISTIDINE; HUMANS; MEMBRANE GLYCOPROTEINS; METHYLGLUCOSIDES; MONOSACCHARIDE TRANSPORT PROTEINS; MUTAGENESIS, SITE-DIRECTED; OOCYTES; PATCH-CLAMP TECHNIQUES; PROTEIN BINDING; RHODAMINES; SODIUM; SODIUM-GLUCOSE TRANSPORTER 1; SPECTROMETRY, FLUORESCENCE; XENOPUS LAEVIS;

ANIMALIA; XENOPUS LAEVIS;

EID: 5444253054     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048652d     Document Type: Article

References (29)

1. Abramson, J., Smirnova, I., Kasho, V., Verner, G., Kaback, H. R., and Iwata, S. (2003) Structure and mechanism of the lactose permease of Escherichia coli. Science 301, 610-615.
2. +/glucose cotransporters is determined by the carboxyl-terminal half of the protein. J. Biol. Chem. 271, 10029-10034.
3. +/glucose cotransporter. J. Biol. Chem. 272, 20324-20327.
4. Turk E., and Wright, E. M. (1997) Membrane topology motifs in the SGLT cotransporter family. J. Membr. Biol. 159, 1-20.
5. + and voltage dependence of the transporter. J. Biol. Chem. 273, 29341-29351.
6. + channel. J. Biol. Chem. 276, 1728-1734.
7. +/glucose cotransporter. J. Biol. Chem. 276, 49188-49194.
8. Novakova, R., Homerova, D., Kinne, R. K. H., Kinne-Saffran, E., and Lin, J. T (2001) Identification of a region critically involved in the interaction of phlorizin with the rabbit sodium-D-glucose cotransporter SGLT1. J. Membr. Biol. 184, 55-60.
9. +/glucose cotransporter. Biochemistry 40, 11897-11904.
10. +/glucose cotransporter: II. A transport model under nonrapid equilibrium conditions. J. Membr. Biol. 125, 63-79.
11. +/glucose cotransporter cloned from rabbit small intestine. J. Membr. Biol. 110, 87-95.
12. +/glucose cotransporter. Proc. Natl. Acad. Sci. U.S.A. 90, 5767-5771.
13. +/glucose cotransporter (SGLT1) currents and fluxes. J. Membr. Biol. 162, 101-106.
14. +-to-sugar stoichiometry of SGLT3. Am. J. Physiol. Renal Physiol. 49, F278-F282.
15. +/glucose cotransporter. Biochemistry 41, 1250-8.
16. + and glucose transport. Proc. Natl. Acad. Sci. U.S.A. 95, 7789-7794.
17. Zampighi, G. A., Kerman, M., Boorer, K. J., Loo, D. D. F., Bezanilla, F., Chandy, G., Hall, J. E., and Wright, E. M. (1995) A method for determining the unitary functional capacity of cloned channels and transporters expressed in Xenopus laevis oocytes. J. Membr. Biol. 148, 65-78.
18. +-dependent sugar transport. Am. J. Physiol. 248, C498-C509.
19. +-glucose cotransport through the rabbit intestinal SGLT1 protein. J. Membr. Biol. 192, 89-100.
20. +/glucose cotransporter. J. Biol. Chem. 275, 25959-25964.
21. +/glucose cotransporter (SGLT1) trafficking and function cause glucose-galactose malabsorption. Nat. Genet. 12, 216-220.
22. +/glucose cotransporter. J. Biol. Chem. 272, 2110-2115.
23. Díez-Sampedro, A., Hirayama, B. A., Osswald, C., Gorboulev, V., Baumgarten, K., Volk, C., Wright, E. M., and Koepsell, H. (2003) A glucose sensor hiding in a family of cotransporters. Proc. Natl. Acad. Sci. U.S.A. 100, 11753-11758.
24. +/glucose cotransporter expressed in Xenopus oocytes is electrogenic, Biophys. J. 57, 1218-1224.
25. +-glucose cotransporter in Xenopus laevis oocytes. J. Physiol. 520, 359-371.
26. Borre, L., and Kanner, B. I. (2004) Arginine 445 controls the coupling between glutamate and cations in the neuronal transporter EAAC-1. J. Biol. Chem. 279, 2513-2519.
27. Bendahan, A., Armon, A., Madani, N., Kavanaugh, M. P., and Kanner, B. I. (2000) Arginine 447 plays a pivotal role in substrate interactions in a neuronal glutamate transporter. J. Biol. Chem. 275, 37436-37442.
28. Meredith, D. (2004) Site-directed mutation of arginine 282 to glutamate uncouples the movement of peptides and protons by the rabbit proton-peptide cotransporter PepT1. J. Biol. Chem. 279, 15795-15798.
29. +/proline transporter of Escherichia coli. Biochemistry 38, 13523-13529.