Sodium cotransporters

Current Opinion in Cell Biology

Volumn 8, Issue 4, 1996, Pages 468-473

  Wright, Ernest M ^a   Loo, Donald D F ^a   Turk, Eric ^a   Hirayama, Bruce A ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHIMERIC PROTEIN; MEMBRANE PROTEIN; PROTEIN KINASE;

ENDOCYTOSIS; EXOCYTOSIS; LIGAND BINDING; MOLECULAR CLONING; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; REVIEW; SITE DIRECTED MUTAGENESIS; SODIUM TRANSPORT; WATER TRANSPORT;

MAMMALIA;

EID: 0030222111     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(96)80022-6     Document Type: Article

References (49)

1. 1. Reizer J, Reizer A, Saier MH Jr: A functional superfamily of sodium/solute symporters. BBA - Biomembranes 1994, 1197:133-166.
2. 2. Wright EM, Hager KM, Turk E: Sodium cotransport proteins. Curr Opin Cell Biol 1992, 4:696-702.
3. +/glucose co-transporter. Nature 1987, 330:379-381.
4. 4. Wong MH, Oelkers P, Craddock AL, Dawson PA: Expression cloning and characterization of the hamster ileal sodium-dependent bile acid transporter. J Biol Chem 1994, 269:1340-1347.
5. +/sulphate cotransporter.
6. +/glucose cotransporter (SGLT1) gene family.
7. + binding and the conformational states of the unloaded carrier. The transport of napthyl-glucoside shows that large conformational changes occur in the cotransporter during the transport cycle.
8. +/glucose stoichiometry of SGLT1.
9. +/GABA cotransporter can operate in the reverse direction.
10. 10. Kanai Y, Nussberger S, Romero MF, Boron WF, Hebert SC, Hediger MA: Electrogenic properties of the epithelial and neuronal high affinity glutamate transporter. J Biol Chem 1995, 270:16561-16568. The stoichiometry of EAAC1 (EAAT3) was determined using current, radiotracer, and pH measurements.
11. 11. Galli A, DeFelice LJ, Duke BJ, Moore KR, Blakely RD: Sodium-dependent norepinephrine-induced currents in norepinephrine-transporter-transfected HEK-293 cells blocked by cocaine and antidepressants. J Exp Biol 1995, 198:2197-2212. On the basis of transport and binding assays, and transient charge movements, the authors concluded that the norepinephrine transporter functions as an ion-gated ligand channel.
12. +/glucose cotransporter (SGLT1). J Biol Chem 1994, 269:21407-21410.
13. 13. Cammack JN, Rakhilin SV, Schwartz EA: A GABA transporter operates asymmetrically and with variable stoichiometry. Neuron 1994, 13:949-960.
14. 14. Vandenberg RJ, Arriza JL, Amara SG, Kavanaugh MP: Constitutive ion fluxes and substrate binding domains of human glutamate transporters. J Biol Chem 1995, 270:17668-17671. Describes substrate-independent ion transport through a EAAT1-EAAT2 chimera, and identifies the structural domain influencing kainate binding.
15. +/glucose cotransporter and not an amino acid transporter. A reinterprelation. J Biol Chem 1994, 269:22488-22491.
16. +/hexose cotransporter (STP1) from Arabidopsis thaliana expressed in Xenopus oocytes. J Biol Chem 1994, 269:20417-20424.
17. + amino acid transporter from Arabidopsis thaliana. J Biol Chem 1996, 271:2213-2220. The turnover number of this plant cotransporter is at least an order of magnitude greater than that of the animal cotransporters.
18. +/dipeptide cotransporter.
19. +/glucose cotransport stoichiometry is predicted by the model.
20. 20. Mager S, Min C, Henry DJ, Chavkin C, Hoffman BJ, Davidson N, Lester HA: Conducting states of a mammalian serotonin transporter. Neuron 1994, 12:845-859.
21. + and GABA.
22. 22. Fairman WA, Vandenberg RJ, Arriza JL, Kavanaugh MP, Amara SG: An excitatory amino-acid transporter with properties of a ligand-gated chloride channel. Nature 1995, 375:599-603. Current and flux measurements associated with the expression of EAAT4 in oocytes are used to show that this cotransporter also contains a chloride-conductance pathway.
23. +/glutamate transport.
24. +/glutamate cotransporter channel.
25. -3).
26. 26. Zampighi GA, Kreman M, Boorer KJ, Loo DDF, Bezanilla F, Chandy G, Hall JE, Wright EM: A method for determining the unitary functional capacity of cloned channels and transporters expressed in Xenopus laevis oocytes. J Membr Biol 1995, 148:65-78. A freeze-fracture analysis of oocytes expressing cotransporters and channels. The results show that charge measurements can be used to quantitate the number of cotransporters and ion channels in oocyte plasma membranes, and that the combination of physiological and freeze-fracture electron microscopy on the same oocyte can be used to determine functional properties of single transporters and channels.
27. 27. Fiévet B, Gabillat N, Borgese F, Motais R: Expression of band 3 anion exchanger induces chloride current and taurine transport: structure-function analysis. EMBO J 1995, 14:5158-5169. A study showing that an exchanger, trout anion exchanger 1, is also an ion channel and a taurine transporter.
28. 28. Wadiche JI, Arriza JL, Amara SF, Kavanaugh MP: Kinetics of a human glutamate transporter. Neuron 1995, 14:1019-1027. A study of pre-steady-state kinetics of the human EAAT2 cotransporter. Establishes that carrier currents are common to voltage-dependent cotransporters.
29. +/glucose cotransporter. II. A transport model under nonrapid equilibrium conditions. J Membr Biol 1992, 125:63-79.
30. 30. Su A, Mager S, Mayo SL, Lester HA: A multi-substrate single-file model for ion-coupled transporters. Biophys J 1996, 70:762-777. A three-site ion channel model is proposed to account for ion leaks, nonlinear current/voltage curves, and variable flux ratios of cotransporters. The model differs from carrier models in that it does not explicitly allow conformational changes that change the compartmentalization of the substrates.
31. +/glucose cotransporter (SGLT1): analysis of interactions. J Membr Biol 1994, 142:161-170.
32. +/myo-inositol cotransporter expressed in Xenopus oocytes. J Membr Biol 1995, 143:103-113. Extends the carrier model for SGLT1 to the myo-inositol cotransporter.
33. +/lactose cotransporter.
34. 34. Turk E, Kerner CJ, Lostao MP, Wright EM: Membrane topology of the human Na+/glucose cotransporter SGLT1. J Biol Chem 1996, 271:1925-1934. An experimental study using N-glycosylation scanning mutagenesis to test secondary structure models, and a theoretical analysis of structure using Predict Protein neural network, MEMSAT (membrane structure and topology), and IFH/RT (interfacial hydrophobicity/reverse turn) algorithms. It is concluded that the eukaryotic homologs of SGLT1 are composed of 14 transmembranes helices, and that the bacterial homologs lack the 14th putative transmembrane helix.
35. 35. Bruss M, Hammermann R, Brimijoin S, Bonisch H: Antipeptide antibodies confirm the topology of the human norepinephrine transporter. J Biol Chem 1995, 270:9197-9201. Describes an important experimental approach to the secondary structure of cotransporters.
36. +/glucose cotransporter, the number of cotransporters in the plasma membrane, and the total membrane area before and after activation of PKA or PKC. It is demonstrated that kinase activation regulates transport by regulating the number of cotransporters in the membrane, by exocytosis and endocytosis, and that the sequence of the expressed cotransporter determines the effect of a protein kinase.
37. 37. Poolman B, Knol J, Van der Does C, Henderson PJF, Liang WJ, Leblanc G, Pourcher T, Mus-Veteau I: Cation and sugar selectivity determinants in a novel family of transport proteins. Mol Microbiol 1996, 19:911-922. A review of site-directed mutagenesis studies of a family of bacterial cation/sugar cotransporters.
38. + glucose cotransporter (SGLT1) trafficking and function cause glucose-galactose malabsorption. Nat Genet 1996, 12:216-220. A study of the structure and function of SGLT1, using the natural mutations causing glucose-galactose malabsorption in patients.
39. +/glucose cotransporter (SGLT1) is involved in trafficking to the plasma membrane. FEBS Lett 1995, 377:181-184. A study of the molecular pathology of a SGLT1 mutant in oocytes using radioactive tracer uptakes, steady-state and pre-steady-state current measurements, Western blotting, immunofluorescence, and freeze-fracture electronmicroscopy. The results show that a single point mutation can impair the trafficking of SGLT1 between the endoplasmic reticulum and the plasma membrane.
40. 40. Hirayama BA, Lostao MP, Panayotova-Heiermann M, Loo DDF, Turk E, Wright EM: Kinetic and specificity differences between rat, human and rabbit Na+-glucose cotransporters (SGLT-1). Am J Physiol - Cell Physiol 1996, 270:G919-G926. Residues and domains involved in determining differences in the kinetics and substrate specificity of the three SGLT1 isoforms have been identified by sequence alignments.
41. 41. Panayotova-Heiermann M, Loo DDF, Kong C, Lever JE, Wright EM: Sugar binding to Na+/glucose cotransporters is determined by the carboxyl-terminal half of the protein. J Biol Chem 1996, 271:10029-10034. Using a chimera composed of the amino-terminal half of SGLT1 and the carboxy-terminal half of SGLT2, it was determined that the carboxy-terminal half determines the sugar affinity and selectivity of the cotransporter. Sequence alignments of the homologs and isoforms suggest residues and domains that account for these observations.
42. +)-coupled glutamate transporter from rat brain. J Biol Chem 1995, 270:17093-17097. An analysis of conserved Hydrophobic charged residues in the glutamate cotransporters has identified a residue that is involved in determining the amino acid substrate specificity.
43. +-dependent glutamate transporter GLAST-1 by site-directed mutagenesis. J Biol Chem 1995, 270:25207-25212. Mutations of polar residues that are conserved in glutamate cotransporters, but are not conserved in the related neutral amino acid cotransporter ASCT1 (alanine, serine, cysteine transporter 1 ), have identified two residues that may be involved in the binding of negatively charged substrates.
44. 44. Calonge MJ, Gasparini P, Chillaron J, Chillon M, Gallucci M, Rousaud F, Zelante L, Testar X, Dallapiccola B, Di Silverio F et al.: Cystinuria caused by mutations in rBAT, a gene involved in the transport of cystine. Nat Genet 1994, 6:420-425.
45. 45. Miyamoto K, Katai K, Tatsumi S, Sone K, Segawa H, Yamamoto H, Taketani Y, Takada K, Morita K, Kanayama H et al.: Mutations of the basic amino acid transporter gene associated with cystinuria. Biochem J 1995, 310:951-955. A compound heterozygote with mutations in the rat basic amino acid transporter gene suffers from cystinuria.
46. 46. Sato K, Adams R, Betz H, Schloss P: Modulation of a recombinant glycine transporter (GLYT1b) by activation of protein kinase C. J Neurochem 1995, 65:1967-1973. Shows that regulation of glycine transport by PKC is not due to phosphorylation of GLYT1b (a recominbinant glycine transporter) at a consensus phosphorylation site of the cotransporter.
47. 47. Corey JL, Davidson N, Lester HA, Brecha N, Quick MW: Protein kinase C modulates the activity of a cloned γ-aminobutyric acid transporter expressed in Xenopus oocytes via regulated subcellular redistribution of the transporter. J Biol Chem 1994, 269:14759-14767.
48. +/phosphate cotransporter.
49. 49. Zerangue N, Arriza JL, Amara SG, Kavanaugh MP: Differential modulation of human glutamate transporter subtypes by arachidonic acid. J Biol Chem 1995, 270:6433-6435. Arachidonic acid reduces transport by EAAT1, activates transport by EAAT2, and has no effect on transport by EAAT3.