Structural basis for α1 versus α2 isoform-distinct behavior of the Na,K-ATPase

Journal of Biological Chemistry

Volumn 278, Issue 11, 2003, Pages 9027-9034

  Segall, Laura ^a   Javaid, Zahid Z ^b   Carl, Stephanie L ^b   Lane, Lois K ^b   Blostein, Rhoda ^a,c  

^a MCGILL UNIVERSITY   (Canada)

^b UNIVERSITY OF CINCINNATI COLLEGE OF MEDICINE   (United States)

^c MONTREAL GENERAL HOSPITAL   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; ENZYME KINETICS; PHASE EQUILIBRIA; RATE CONSTANTS;

PREDILECTION;

BIOCHEMISTRY;

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); AMINO ACID; ISOENZYME; POTASSIUM ION; VANADIC ACID; ADENOSINE TRIPHOSPHATE; HYBRID PROTEIN; ISOPROTEIN; POTASSIUM CHLORIDE; TRYPSIN;

ALPHA CHAIN; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CHIMERA; CONFORMATIONAL TRANSITION; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME STRUCTURE; HELA CELL; HUMAN; HUMAN CELL; MUTAGENESIS; PRIORITY JOURNAL; PROTEIN DOMAIN; AMINO ACID SEQUENCE; ANIMAL; CELL LINE; CELL MEMBRANE; CHEMICAL MODEL; CHEMISTRY; CYTOPLASM; DOSE RESPONSE; GENETIC TRANSFECTION; KINETICS; METABOLISM; MICROSOME; MOLECULAR GENETICS; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; RAT; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; TIME;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ANIMALS; CELL LINE; CELL MEMBRANE; CYTOPLASM; DOSE-RESPONSE RELATIONSHIP, DRUG; HELA CELLS; HUMANS; KINETICS; MICROSOMES; MODELS, CHEMICAL; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; NA(+)-K(+)-EXCHANGING ATPASE; POTASSIUM CHLORIDE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN ISOFORMS; PROTEIN STRUCTURE, TERTIARY; RATS; RECOMBINANT FUSION PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; TIME FACTORS; TRANSFECTION; TRYPSIN; VANADATES;

EID: 0038526240     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M211636200     Document Type: Article

References (33)

1. Jorgensen, P. L. (1975) Biochim. Biophys. Acta 401, 399-415
2. Daly, S. E., Lane, L. K., and Blostein, R. (1994) J. Biol. Chem. 269, 23944-23948
3. Daly, S. E., Lane, L. K., and Blostein, R. (1996) J. Biol. Chem. 271, 23683-23689
4. Boxenbaum, N., Daly, S. E., Javaid, Z. Z., Lane, L. K., and Blostein, R. (1998) J. Biol. Chem. 273, 23086-23092
5. Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Nature 405, 647-655
6. Jewell, E. A., and Lingrel, J. B. (1991) J. Biol. Chem. 266, 16925-16930
7. Kunkel, T. A. (1985) Proc. Natl. Acad. Sci. U. S. A. 82, 488-492
8. Chen, C., and Okayama, H. (1987) Mol. Cell. Biol. 7, 2745-2752
9. Lane, L. K., Feldmann, J. M., Flarsheim, C. E., and Rybczynski, C. L. (1993) J. Biol. Chem. 268, 17930-17934
10. Markwell, M. A., Haas, S. M., Tolbert, N. E., and Bieber, L. L. (1981) Methods Enzymol. 72, 296-303
11. Blostein, R. (1988) Methods Enzymol. 156, 171-178
12. Munzer, J. S., Daly, S. E., Jewell-Motz, E. A., Lingrel, J. B., and Blostein, R. (1994) J. Biol. Chem. 269, 16668-16676
13. DeLean, A., Munson, P. J., and Rodbard, D. (1978) Am. J. Physiol. 235, E97-E102
14. Klodos, I., Post, R. L., and Forbush, B., III (1994) J. Biol. Chem. 269, 1734-1743
15. Vilsen, B. (1997) Biochemistry 36, 13312-13324
16. Arguello, J. M., and Lingrel, J. B. (1995) J. Biol. Chem. 270, 22764-22771
17. Post, R. L., Hegyvary, C., and Kume, S. (1972) J. Biol. Chem. 247, 6530-6540
18. Wierzbicki, W., and Blostein, R. (1993) Proc. Natl. Acad. Sci. U. S. A. 90, 70-74
19. Cantley, L. C., Jr., Cantley, L. G., and Josephson, L. (1978) J. Biol. Chem. 253, 7361-7368
20. Toyoshima, C., and Nomura, H. (2002) Nature 418, 605-611
21. Segall, L., Daly, S. E., and Blostein, R. (2001) J. Biol. Chem. 276, 31535-31541
22. Segall, L., Lane, L. K., and Blostein, R. (2002) J. Biol. Chem. 277, 35202-35209
23. Blanco, G., Sanchez, G., and Mercer, R. W. (1998) Arch. Biochem. Biophys. 359, 139-150
24. Efendiev, R., Bertorello, A. M., Pressley, T. A., Rousselot, M., Feraille, E., and Pedemonte, C. H. (2000) Biochemistry 39, 9884-9892
25. Feraille, E., Carranza, M. L., Gonin, S., Beguin, P., Pedemonte, C., Rousselot, M., Caverzasio, J., Geering, K., Martin, P. Y., and Favre, H. (1999) Mol. Biol. Cell 10, 2847-2859
26. Feraille, E., Carranza, M. L., Rousselot, M., and Favre, H. (1994) Am. J. Physiol. 267, F55-F62
27. Lavoie, L., Roy, D., Ramlal, T., Dombrowski, L., Martn-Vasallo, P., Marette, A., Carpentier, J. L., and Klip, A. (1996) Am. J. Physiol. 270, C1421-C1429
28. Sampson, S. R., Brodie, C., and Alboim, S. V. (1994) Am. J. Physiol. 266, C751-C758
29. Pierre, S. V., Duran, M.-J., Carr, D. L., and Pressley, T. A. (2002) Am. J. Physiol. 283, F1066-F1074
30. Daly, S. E., Blostein, R., and Lane, L. K. (1997) J. Biol. Chem. 272, 6341-6347
31. Coppi, M. V., Compton, L. A., and Guidotti, G. (1999) Biochemistry 38, 2494-2505
32. Patchornik, G., Munson, K., Goldshleger, R., Shainskaya, A., Sachs, G., and Karlish, S. J. D. (2002) Biochemistry 41, 11740-11749
33. Xu, C., Rice, W. J., HE, W., and Stokes, D. L. (2002) J. Mol. Biol. 316, 201-211