The residues determining differences in ion affinities among the alternative splice variants F, A, and B of the mammalian renal Na-K-Cl cotransporter (NKCC2)

Journal of Biological Chemistry

Volumn 282, Issue 9, 2007, Pages 6540-6547

  Giménez, Ignacio ^a,b   Forbush, Biff ^a  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF ZARAGOZA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

CHLORINE; DISEASES; MUTAGENESIS; NEGATIVE IONS; POSITIVE IONS; POTASSIUM;

COTRANSPORTERS; FUNCTIONAL EXPRESSION; ION AFFINITIES; XENOPUS OOCYTES;

SODIUM;

RNA; SODIUM POTASSIUM CHLORIDE COTRANSPORTER; CHLORINE; ISOPROTEIN; MEMBRANE PROTEIN; SODIUM POTASSIUM CHLORIDE COTRANSPORTER 2 PROTEIN; SODIUM-POTASSIUM CHLORIDE COTRANSPORTER 2 PROTEIN; UNCLASSIFIED DRUG;

ALTERNATIVE RNA SPLICING; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; BARTTER SYNDROME; CHLORIDE CONDUCTANCE; CONTROLLED STUDY; GENE EXPRESSION; GENETIC VARIABILITY; INTRACELLULAR MEMBRANE; ION EXCHANGE; KIDNEY INTERSTITIUM; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; RECEPTOR AFFINITY; SITE DIRECTED MUTAGENESIS; XENOPUS LAEVIS; ANIMAL; C57BL MOUSE; CHEMISTRY; GENETICS; KIDNEY; METABOLISM; MOUSE; PROTEIN TERTIARY STRUCTURE; TRANSGENIC MOUSE; TRANSPORT AT THE CELLULAR LEVEL;

MAMMALIA;

AMINO ACID SUBSTITUTION; ANIMALS; BIOLOGICAL TRANSPORT; CHLORINE; KIDNEY; MEMBRANE PROTEINS; MICE; MICE, INBRED C57BL; MICE, TRANSGENIC; PROTEIN ISOFORMS; PROTEIN STRUCTURE, TERTIARY; SODIUM-POTASSIUM-CHLORIDE SYMPORTERS;

EID: 34250305147     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M610780200     Document Type: Article

References (35)

1. Simon, D. B., Karet, F. E., Hamdan, J. M., DiPietro, A., Sanjad, S. A., and Lifton, R. P. (1996) Nat. Genet. 13, 183-188
2. Isenring, P., Jacoby, S. C., and Forbush, B., III (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 7179-7184
3. Darman, R. B., and Forbush, B. (2002) J. Biol. Chem. 277, 37542-37550
4. Dowd, B. F., and Forbush, B. (2003) J. Biol. Chem. 278, 27347-27353
5. Piechotta, K., Lu, J., and Delpire, E. (2002) J. Biol. Chem. 277, 50812-50819
6. Darman, R. B., Flemmer, A., and Forbush, B. (2001) J. Biol. Chem. 276, 34359-34362
7. Isenring, P., Jacoby, S. C., Chang, J., and Forbush, B. (1998) J. Gen. Physiol. 112, 549-558
8. Isenring, P., and Forbush, B., III (1997) J. Biol. Chem. 272, 24556-24562
9. Igarashi, P., Vanden Heuvel, G. B., Payne, J. A., and Forbush, B., III (1995) Am. J. Physiol. 269, F405-F418
10. Castrop, H., Lorenz, J. N., Hansen, P. B., Friis, U., Mizel, D., Oppermann, M., Jensen, B. L., Briggs, J., Skott, O., and Schnermann, J. (2005) Am. J. Physiol. Renal Physiol. 289, F1185-F1192
11. Gimenez, I., Isenring, P., and Forbush, B. (2002) J. Biol. Chem. 277, 8767-8770
12. Plata, C., Meade, P., Vazquez, N., Hebert, S. C., and Gamba, G. (2002) J. Biol. Chem. 277, 11004-11012
13. Gagnon, E., Forbush, B., Caron, L., and Isenring, P. (2003) Am. J. Physiol. Cell Physiol. 284, C365-C370
14. Payne, J. A., and Forbush, B., III (1994) Proc. Natl. Acad. Sci. U. S. A. 91, 4544-4548
15. Gimenez, I., and Forbush, B., III (2002) FASEB J. 16, 26a
16. Gagnon, E., Bergeron, M. J., Brunet, G. M., Daigle, N. D., Simard, C. F., and Isenring, P. (2004) J. Biol. Chem. 279, 5648-5654
17. Gagnon, E., Bergeron, M. J., Daigle, N. D., Lefoll, M. H., and Isenring, P. (2005) J. Biol. Chem. 280, 32555-32563
18. Lytle, C., Xu, J. C., Biemesderfer, D., and Forbush, B., III (1995) Am. J. Physiol. 269, C1496-C1505
19. Lytle, C., McManus, T. J., and Haas, M. (1998) Am. J. Physiol. 274, C299-C309
20. Vargas-Poussou, R., Feldmann, D., Vollmer, M., Konrad, M., Kelly, L., van den Heuvel, L. P., Tebourbi, L., Brandis, M., Karolyi, L., Hebert, S. C., Lemmink, H. H., Deschenes, G., Hildebrandt, F., Seyberth, H. W., Guay-Woodford, L. M., Knoers, N. V., and Antignac, C. (1998) Am. J. Hum. Genet. 62, 1332-1340
21. Dawson, J. P., Weinger, J. S., and Engelman, D. M. (2002) J. Mol. Biol. 316, 799-805
22. Kolbe, M., Besir, H., Essen, L. O., and Oesterhelt, D. (2000) Science 288, 1390-1396
23. Dutzler, R., Campbell, E. B., Cadene, M., Chait, B. T., and MacKinnon, R. (2002) Nature 415, 287-294
24. Yamashita, A., Singh, S. K., Kawate, T., Jin, Y., and Gouaux, E. (2005) Nature 437, 215-223
25. Russ, W. P., and Engelman, D. M. (2000) J. Mol. Biol. 296, 911-919
26. Kim, S., Jeon, T. J., Oberai, A., Yang, D., Schmidt, J. J., and Bowie, J. U. (2005) Proc. Natl. Acad. Sci. U. S. A. 102, 14278-14283
27. Vila, R., Ponte, I., Jimenez, M. A., Rico, M., and Suau, P. (2002) Prot. Sci. 11, 214-220
28. Grant, G. A., Xu, X. L., and Hu, Z. (2000) Biochemistry 39, 7316-7319
29. Gerelsaikhan, T., Parvin, M. N., and Turner, R. J. (2006) Biochemistry 45, 12060-12067
30. Doyle, D. A., Morais Cabral, J., Pfuetzner, R. A., Kuo, A., Gulbis, J. M., Cohen, S. L., Chait, B. T., and MacKinnon, R. (1998) Science 280, 69-77
31. Sui, H., Han, B. G., Lee, J. K., Walian, P., and Jap, B. K. (2001) Nature 414, 872-878
32. Grunewald, M., Bendahan, A., and Kanner, B. I. (1998) Neuron 21, 623-632
33. Yernool, D., Boudker, O., Jin, Y., and Gouaux, E. (2004) Nature 431, 811-818
34. Jung, J. S., Preston, G. M., Smith, B. L., Guggino, W. B., and Agre, P. (1994) J. Biol. Chem. 269, 14648-14654
35. Gasol, E., Jimenez-Vidal, M., Chillaron, J., Zorzano, A., and Palacin, M. (2004) J. Biol. Chem. 279, 31228-31236