The isoform-specific region of the Na,K-ATpase catalytic subunit: Role in enzyme kinetics and regulation by protein kinase C

Biochemistry

Volumn 43, Issue 51, 2004, Pages 16174-16183

  Duran, Marie Josée ^a   Pierre, Sandrine V ^a,b   Carr, Deborah L ^a   Pressley, Thomas A ^a  

^a TEXAS TECH UNIVERSITY HEALTH SCIENCES CENTER SCHOOL OF MEDICINE   (United States)

^b MEDICAL COLLEGE OF OHIO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CELLS; ENZYME KINETICS; POTASSIUM; PROTEINS;

BINDING SITES; ISOFORM-SPECIFIC REGION (ISR); OPOSSUM KIDNEY (OK); STRUCTURAL DIVERGENCE;

SODIUM;

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ADENOSINE TRIPHOSPHATE; HYDROGEN POTASSIUM ADENOSINE TRIPHOSPHATASE; LITHIUM ION; OUABAIN; PHORBOL ESTER; POTASSIUM ION; PROTEIN KINASE C;

ANIMAL CELL; ARTICLE; BINDING SITE; CATALYSIS; CHIMERA; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME REGULATION; ENZYME SUBUNIT; GENETIC TRANSFECTION; HUMAN; NONHUMAN; ONCOGENE C MYC; OPOSSUM; PRIORITY JOURNAL; PROTEIN EXPRESSION; RAT;

AMINO ACID SEQUENCE; ANIMALS; HUMANS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NA(+)-K(+)-EXCHANGING ATPASE; POTASSIUM; PROTEIN ISOFORMS; PROTEIN KINASE C; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS C-MYC; RATS; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; TEMPERATURE;

ANIMALIA; DIDELPHIDAE; RODENTIA; STROPHANTHUS GRATUS;

EID: 11144281256     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0490183     Document Type: Article

References (27)

1. Blanco, G., and Mercer, R. W. (1998) Isozymes of the Na-K-ATPase: heterogeneity in structure, diversity in function, Am. J. Physiol. 275, F633-F650.
2. +-ATPaSe central isoform-specific region: Involvement in PKC regulation, Am. J. Physiol. 283, F1066-F1074.
3. +-ATPaSe alpha-subunit from rat brain, Biochemistry 25, 8125-8132.
4. +-ATPaSe does not need its amino terminus to maintain cell viability, Am. J. Physiol. 267, C590-C597.
5. Jewell, E. A., and Lingrel, J. B. (1991) Comparison of the substrate dependence properties of the rat Na, K-ATPase α1, α2, α3 isoforms expressed in HeLa cells, J. Biol. Chem. 266, 16925-16930.
6. 3H]ouabain binding to the transport adenosine triphosphatase from outer medulla of canine kidney, J. Biol. Chem. 248, 7197-7200.
7. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951) Protein measurement with the Folin phenol reagent, J. Biol. Chem. 193, 265-275.
8. Petrosian, S. A., Carr, D. L., Guerrero, G., and Pressley, T. A. (1998) Mutagenesis disrupts posttranslational processing of the Na, K-ATPase catalytic subunit, Arch. Biochem. Biophys. 357, 249-258.
9. Toyoshima, C., and Nomura, H. (2002) Structural changes in the calcium pump accompanying the dissociation of calcium, Nature 418, 605-611.
10. Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution, Nature 405, 647-655.
11. Guex, N., and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling, Electrophoresis 18, 2714-2723.
12. Peitsch, M. C. (1996) ProMod and Swiss-Model: Internet-based tools for automated comparative protein modeling, Biochem. Soc. Trans. 24, 274-279.
13. +-ATPase is not an essential residue for active transport of sodium and potassium ions, Biochemistry 32, 13340-13349.
14. Daly, S. E., Lane, L. K., and Blostein, R. (1996) Structure/function analysis of the amino-terminal region of the α1 and α2 subunits of Na, K-ATPase, J. Biol. Chem. 271, 23683-23689.
15. Daly, S. E., Lane, L. K., and Blostein, R. (1994) Functional consequences of amino-terminal diversity of the catalytic subunit of the Na, K-ATPase, J. Biol. Chem. 269, 23944-2394.
16. Pedemonte, C. H., Pressley, T. A., Lokhandwala, M. F., and Cinelli, A. R. (1997) Regulation of Na, K-ATPase transport activity by protein kinase C, J. Membr. Biol. 155, 219-227.
17. +-ATPaSe, Am. J. Physiol. 262, C743-C751.
18. 2+-ATPaSe in E1 and E2 states, Biophys. J. 80, 2187-2197.
19. Huge M., Siegal G., Viuster G. W., Guntert P., Gloor S. M., Abrahams J. P. (2003) ATP-induced conformational changes of the nucleotide-binding domain of Na, K.-ATPase, Nat. Struct. Biol. 10, 468-474.
20. Segall, L., Lane, L. K., and Blostein, R. (2002) New insights into the role of the N terminus in conformational transitions of the Na, K-ATPase, J. Biol. Chem. 277, 35202-35209.
21. +-ATPase molecules to the plasma membrane, Biochemistry 39, 9884-9892.
22. Kirchhausen, T. (1999) Adaptors for clathrin-mediated traffic, Annu. Rev. Cell. Dev. Biol. 15, 705-732.
23. Dietrich, J., Kastrup, J., Nielsen, B. L., Ødum, N., and Geisler, C. (1997) Regulation and function of the CD3γ DxxxLL motif: A binding site for adaptor protein-1 and adaptor protein-2 in vitro, J. Cell. Biol. 138, 271-281.
24. +-ATPase α-subunit is essential for AP-2 binding and clathrin-dependent endocytosis, J. Biol. Chem. 277, 17108-17111.
25. Courtois-Coutry, N., Roush, D., Rajendran, V., McCarthy, J. B., Geibel, J., Kashgarian, M., and Caplan, M. J. (1997) A tyrosine-based signal targets H/K-ATPase to a regulated compartment and is required for the cessation of gastric secretion, Cell 90, 501-510.
26. Beguin, P., Peitsch, M. C., and Geering, K. (1996) α1 but not α2 or α3 isoforms of Na, K-ATPase are efficiently phosphorylated in a novel protein kinase C motif, Biochemistry 35, 14098-14108.
27. Jorgensen, P. L., Hakansson, K. O., and Karlish, S. J. D. (2003) Structure and mechanism of Na, K -ATPase: Functional sites and their interactions, Annu. Rev. Physiol. 65, 817-849.