Ca2+ binding to site I of the cardiac Ca2+ pump is sufficient to dissociate phospholamban

Journal of Biological Chemistry

Volumn 285, Issue 5, 2010, Pages 3253-3260

  Chen, Zhenhui ^a   Akin, Brandy L ^a   Jones, Larry R ^a  

^a INDIANA UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SUBSTITUTION; ATP HYDROLYSIS; DYNAMIC EQUILIBRIA; HIGH AFFINITY; PHOSPHOLAMBAN; SARCOPLASMIC RETICULUM; SKELETAL MUSCLE; THAPSIGARGINS;

AMINO ACIDS; BINDING ENERGY; BINDING SITES; HYDROLYSIS; ORGANIC ACIDS; PUMPS;

CALCIUM;

ADENOSINE TRIPHOSPHATASE (CALCIUM); ADENOSINE TRIPHOSPHATE; PHOSPHOLAMBAN; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE 2A; THAPSIGARGIN; UNCLASSIFIED DRUG; CALCIUM; CALCIUM BINDING PROTEIN; CROSS LINKING REAGENT;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; BINDING SITE; CALCIUM BINDING; CONTROLLED STUDY; PRIORITY JOURNAL; PROTEIN CROSS LINKING; PROTEIN EXPRESSION; PROTEIN HYDROLYSIS; PROTEIN PROTEIN INTERACTION; SKELETAL MUSCLE; ANIMAL; CHEMICAL MODEL; CHEMISTRY; DOG; HYDROLYSIS; INSECT; KINETICS; METABOLISM; MUTATION; PHOSPHORYLATION; PROTEIN BINDING;

ADENOSINE TRIPHOSPHATE; ANIMALS; BINDING SITES; CALCIUM; CALCIUM-BINDING PROTEINS; CROSS-LINKING REAGENTS; DOGS; HYDROLYSIS; INSECTS; KINETICS; MODELS, CHEMICAL; MUTATION; PHOSPHORYLATION; PROTEIN BINDING; SARCOPLASMIC RETICULUM CALCIUM-TRANSPORTING ATPASES;

EID: 77449089784     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.080820     Document Type: Article

References (26)

1. Simmerman, H. K., and Jones, L. R. (1998) Physiol. Rev. 78, 921-947
2. Frank, K., and Kranias, E. G. (2000) Ann. Med. 32, 572-578
3. Autry, J. M., and Jones, L. R. (1997) J. Biol. Chem. 272, 15872-15880
4. Kimura, Y., Kurzydlowski, K., Tada, M., and MacLennan, D. H. (1997) J. Biol. Chem. 272, 15061-15064
5. Vinge, L. E., Raake, P. W., and Koch, W. J. (2008) Circ. Res. 102, 1458-1470
6. Toyoshima, C., and Inesi, G. (2004) Annu. Rev. Biochem. 73, 269-292
7. Olesen, C., Picard, M., Winther, A. M., Gyrup, C., Morth, J. P., Oxvig, C., Møller, J. V., and Nissen, P. (2007) Nature 450, 1036-1042
8. Toyoshima, C. (2008) Arch. Biochem. Biophys. 476, 3-11
9. Clarke, D. M., Loo, T. W., Inesi, G., and MacLennan, D. H. (1989) Nature 339, 476-478
10. Andersen, J. P., and Vilsen, B. (1992) J. Biol. Chem. 267, 19383-19387
11. Andersen, J. P., and Vilsen, B. (1994) J. Biol. Chem. 269, 15931-15936
12. Andersen, J. P. (1995) Biosci. Rep. 15, 243-261
13. Zhang, Z., Lewis, D., Strock, C., Inesi, G., Nakasako, M., Nomura, H., and Toyoshima, C. (2000) Biochemistry 39, 8758-8767
14. Inesi, G., Kurzmack, M., Coan, C., and Lewis, D. E. (1980) J. Biol. Chem. 255, 3025-3031
15. Strock, C., Cavagna, M., Peiffer, W. E., Sumbilla, C., Lewis, D., and Inesi, G. (1998) J. Biol. Chem. 273, 15104-15109
16. Liu, Y., Pilankatta, R., Lewis, D., Inesi, G., Tadini-Buoninsegni, F., Bartolommei, G., and Moncelli, M. R. (2009) J. Mol. Biol. 391, 858-871
17. MacLennan, D. H., Brandl, C. J., Korczak, B., and Green, N. M. (1985) Nature 316, 696-700
18. Cantilina, T., Sagara, Y., Inesi, G., and Jones, L. R. (1993) J. Biol. Chem. 268, 17018-17025
19. Jones, L. R., Cornea, R. L., and Chen, Z. (2002) J. Biol. Chem. 277, 28319-28329
20. Chen, Z., Stokes, D. L., Rice, W. J., and Jones, L. R. (2003) J. Biol. Chem. 278, 48348-48356
21. Chen, Z., Stokes, D. L., and Jones, L. R. (2005) J. Biol.Chem.280,10530- 10539
22. Chen, Z., Akin, B. L., Stokes, D. L., and Jones, L. R. (2006) J. Biol. Chem. 281, 14163-14172
23. Chen, Z., Akin, B. L., and Jones, L. R. (2007) J. Biol. Chem. 282, 20968-20976
24. Cornea, R. L., Autry, J. M., Chen, Z., and Jones, L. R. (2000) J. Biol. Chem. 275, 41487-41494
25. Clarke, D. M., Loo, T. W., and MacLennan, D. H. (1990) J. Biol. Chem. 265, 6262-6267
26. Toyoshima, C., Asahi, M., Sugita, Y., Khanna, R., Tsuda, T., and Mac- Lennan, D. H. (2003) Proc. Natl. Acad. Sci. U.S.A. 100, 467-472