Plant and animal type 2B Ca2+-ATPases: Evidence for a common auto-inhibitory mechanism

FEBS Letters

Volumn 584, Issue 23, 2010, Pages 4783-4788

  Bonza, Maria Cristina ^a   Luoni, Laura ^a  

^a UNIVERSITY OF MILAN   (Italy)

Author keywords

Auto inhibition; Ca2+ ATPases; Chimeric protein; P type ATPases

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATASE (CALCIUM) 8; PLASMA MEMBRANE CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE 4B; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHIMERA; ENZYME INHIBITION; MUTANT; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; SACCHAROMYCES CEREVISIAE; YEAST;

ANIMALS; ARABIDOPSIS; ARABIDOPSIS PROTEINS; CALCIUM-TRANSPORTING ATPASES; ENZYME INHIBITORS; HUMANS; PLASMA MEMBRANE CALCIUM-TRANSPORTING ATPASES; PROTEIN STRUCTURE, TERTIARY; SPECIES SPECIFICITY;

ANIMALIA;

EID: 78649655549     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.11.008     Document Type: Article

References (28)

1. McAinsh M.R., Pittman J.K. Shaping the calcium signature. New Phytol. 2009, 181:275-294.
2. Dodd A.N., Kudla J., Sanders D. The language of calcium signaling. Annu. Rev. Plant Biol. 2010, 61:593-620.
3. Møller J.V., Juul B., le Maire M. Structural organization ion transport energy transduction of P-type ATPases. Biochim. Biophys. Acta 1996, 1286:1-51.
4. Geisler M., Axelsen K.B., Harper J.F., Palmgren M.G. Molecular aspects of higher plant P-type Ca2+ -ATPases. Biochim. Biophys. Acta 2000, 65:52-78.
5. Axelsen K.B., Palmgren M.G. Inventory of the superfamily of P-type ion pumps in Arabidopsis. Plant Physiol. 2001, 126:696-706.
6. 2+-ATPases. Physiol. Plant 2005, 27:559-5740.
7. 2+ ATPase of animal cells: structure, function and regulation. Arch. Biochem. Biophys. 2008, 476(1):65-74.
8. 2+-ATPases by terminal domains. J. Bioenerg. Biomembr. 2005, 37:369-374.
9. 2+ antiporters in plant development. Transporters and pumps in plant signalling 2010, 133-164. Springer-Verlag, Berlin, Heidelberg, D. M. Geisler, K. Venema (Eds.).
10. 2+-ATPase activity by acidic phospholipids. Physiol. Plant 2001, 112:315-320.
11. 2+-ATPase by acidic phospholipids: evidence for a phospholipid binding site which overlaps the calmodulin-binding site. Mol. Membr. Biol. 2008, 25:539-546.
12. Brini M., Carafoli E. Calcium pumps in health and disease. Physiol. Rev. 2009, 89(4):1341-1378.
13. 2+-ATPase of Arabidopsis thaliana with a calmodulin binding domain at the N-terminus. Plant Physiol. 2000, 123:1495-1505.
14. 2+-ATPase of radish seedlings. I. Biochemical characteristics using ITP as a substrate. Plant Physiol. 1992, 98:1196-1201.
15. 2+-ATPase of Arabidopsis thaliana, and characterization of a hyperactive mutant. Planta 2004, 218:814-823.
16. 2+ pump contains a site that interacts with its calmodulin-binding domain. J. Biol. Chem. 1991, 266:2930-2936.
17. 2+ pump interacts with the transduction domain of the enzyme. Protein Sci. 1992, 1:1613-1621.
18. 2+-ATPase involves an interaction of the N-terminus with the small cytoplasmic loop. FEBS Lett. 2004, 574:20-24.
19. 2+-ATPase of Arabidopsis thaliana, generate partially deregulated pumps. J. Biol. Chem. 2009, 284:30881-30888.
20. 2+ pump near the N-terminus. Biochem. J. 1998, 331:763-766.
21. 2+ ATPases. J. Cell Biol. 1994, 124:351-363.
22. 2+ pump of the plasma membrane of Arabidopsis thaliana: characteristics and sensitivity to fluorescein derivatives. Botanica Acta 1993, 106:20-25.
23. 2+ pump ACA8 contains overlapping as well as physically separated autoinhibitory and calmodulin-binding domains. J. Biol. Chem. 2006, 281:1058-1065.
24. 2+ dependencies. Physiol. Plant. 2006, 126:175-186.
25. 2+ pump. J. Biol. Chem. 1994, 269:1687-1691.
26. 2+ pump involved in the activation. J. Biol. Chem. 2007, 282:35440-35448.
27. 2+-pumping ATPase?. Biochemistry 1991, 30:7978-7983.
28. Hwang I., Harper J.F., Liang F., Sze H. Calmodulin activation of an endoplasmic reticulum-located calcium pump involves an interaction with the N-terminal autoinhibitory domain. Plant Physiol. 2000, 122:157-167.