Calcium negatively regulates an intramolecular interaction between the N-terminal recoverin homology and EF-hand motif domains and the C-terminal C1 and catalytic domains of diacylglycerol kinase α

Biochemical and Biophysical Research Communications

Volumn 423, Issue 3, 2012, Pages 571-576

  Takahashi, Masato ^a   Yamamoto, Tatsuya ^a   Sakai, Hiromichi ^a   Sakane, Fumio ^a  

^a CHIBA UNIVERSITY   (Japan)

Author keywords

Helix; Calcium; Circular dichroism spectroscopy; Diacylglycerol kinase; EF hand; Intramolecular interaction

Indexed keywords

CALCIUM; DIACYLGLYCEROL KINASE; DIACYLGLYCEROL KINASE ALPHA; GREEN FLUORESCENT PROTEIN; RECOVERIN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION;

AMINO ACID MOTIFS; ANIMALS; CALCIUM; CATALYTIC DOMAIN; CERCOPITHECUS AETHIOPS; COS CELLS; DIACYLGLYCEROL KINASE; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MUTATION; SWINE;

EID: 84863332129     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.06.006     Document Type: Article

References (35)

1. Goto K., Hozumi Y., Kondo H. Diacylglycerol, phosphatidic acid, and the converting enzyme, diacylglycerol kinase, in the nucleus. Biochim. Biophys. Acta 2006, 1761:535-541.
2. Merida I., Avila-Flores A., Merino E. Diacylglycerol kinases: at the hub of cell signalling. Biochem. J. 2008, 409:1-18.
3. Sakane F., Imai S., Kai M., Yasuda S., Kanoh H. Diacylglycerol kinases: why so many of them?. Biochim. Biophys. Acta 2007, 1771:793-806.
4. Shulga Y.V., Topham M.K., Epand R.M. Regulation and functions of diacylglycerol kinases. Chem. Rev. 2011, 111:6186-6208.
5. van Blitterswijk W.J., Houssa B. Properties and functions of diacylglycerol kinases. Cell. Signal. 2000, 12:595-605.
6. Sakane F., Yamada K., Kanoh H., Yokoyama C., Tanabe T. Porcine diacylglycerol kinase sequence has zinc finger and E-F hand motifs. Nature 1990, 344:345-348.
7. Yamada K., Sakane F., Kanoh H. Immunoquantitation of 80 kDa diacylglycerol kinase in pig and human lymphocytes and several other cells. FEBS Lett. 1989, 244:402-406.
8. Goto K., Watanabe M., Kondo H., Yuasa H., Sakane F., Kanoh H. Gene cloning, sequence, expression and in situ localization of 80 kDa diacylglycerol kinase specific to oligodendrocyte of rat brain. Mol. Brain Res. 1992, 16:75-87.
9. Yanagisawa K., Yasuda S., Kai M., Imai S., Yamada K., Yamashita T., Jimbow K., Kanoh H., Sakane F. Diacylglycerol kinase α suppresses tumor necrosis factor-α-induced apoptosis of human melanoma cells through NF-κB activation. Biochim. Biophys. Acta 2007, 1771:462-474.
10. Flores I., Jones D.R., Cipres A., Diaz-Flores E., Sanjuan M.A., Merida I. Diacylglycerol kinase inhibition prevents IL-2-induced G1 to S transition through a phosphatidylinositol-3 kinase-independent mechanism. J. Immunol. 1999, 163:708-714.
11. Olenchock B.A., Guo R., Carpenter J.H., Jordan M., Topham M.K., Koretzky G.A., Zhong X.P. Disruption of diacylglycerol metabolism impairs the induction of T cell anergy. Nat. Immunol. 2006, 7:1174-1181.
12. Zha Y., Marks R., Ho A.W., Peterson A.C., Janardhan S., Brown I., Praveen K., Stang S., Stone J.C., Gajewski T.F. T cell anergy is reversed by active Ras and is regulated by diacylglycerol kinase-α. Nat. Immunol. 2006, 7:1166-1173.
13. Cutrupi S., Baldanzi G., Gramaglia D., Maffe A., Schaap D., Giraudo E., van Blitterswijk W., Bussolino F., Comoglio P.M., Graziani A. Src-mediated activation of α-diacylglycerol kinase is required for hepatocyte growth factor-induced cell motility. EMBO J. 2000, 19:4614-4622.
14. K. Takeishi, A. Taketomi, K. Shirabe, T. Toshima, T. Motomura, T. Ikegami, T. Yoshizumi, F. Sakane, Y. Maehara, Diacylglycerol kinase α enhances hepatocellular carcinoma progression by activation of Ras-Raf-MEK-ERK pathway, Journal of hepatology, in press (2012). (DOI: 10.1016/j.jhep.2012.02.026).
15. Kretsinger R.H. The informational role of calcium in the cytosol. Adv. Cyclic Nucl. Res. 1979, 11:1-26.
16. Moncrief N.D., Kretsinger R.H., Goodman M. Evolution of EF-hand calcium-modulated proteins. I. Relationships based on amino acid sequences. J. Mol. Evol. 1990, 30:522-562.
17. Ohno S., Emori Y., Imajoh S., Kawasaki H., Kisaragi M., Suzuki K. Evolutionary origin of a calcium-dependent protease by fusion of genes for a thiol protease and a calcium-binding protein?. Nature 1984, 312:566-570.
18. Murachi T. Calcium-dependent proteinases and specific inhibitors: calpain and calpastatin. Biochem. Soc. Symp. 1984, 49:149-167.
19. Bairoch A., Cox J.A. EF-hand motifs in inositol phospholipid-specific phospholipase C. FEBS Lett. 1990, 269:454-456.
20. Sakane F., Yamada K., Imai S., Kanoh H. Porcine 80-kDa diacylglycerol kinase is a calcium-binding and calcium/phospholipid-dependent enzyme and undergoes calcium-dependent translocation. J. Biol. Chem. 1991, 266:7096-7100.
21. Yamada K., Sakane F., Matsushima N., Kanoh H. EF-hand motifs of α, β and γ isoforms of diacylglycerol kinase bind calcium with different affinities and conformational changes. Biochem. J. 1997, 321:59-64.
22. Merino E., Sanjuan M.A., Moraga I., Cipres A., Merida I. Role of the diacylglycerol kinase α-conserved domains in membrane targeting in intact T cells. J. Biol. Chem. 2007, 282:35396-35404.
23. Sakane F., Imai S., Yamada K., Kanoh H. The regulatory role of EF-hand motifs of pig 80K diacylglycerol kinase as assessed using truncation and deletion mutants. Biochem. Biophys. Res. Commun. 1991, 181:1015-1021.
24. Jiang Y., Qian W., Hawes J.W., Walsh J.P. A domain with homology to neuronal calcium sensors is required for calcium-dependent activation of diacylglycerol kinase α. J. Biol. Chem. 2000, 275:34092-34099.
25. Tsushima S., Kai M., Yamada K., Imai S., Houkin K., Kanoh H., Sakane F. Diacylglycerol kinase γ serves as an upstream suppressor of Rac1 and lamellipodium formation. J. Biol. Chem. 2004, 279:28603-28613.
26. Fabiato A., Fabiato F. Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells. J. Physiol. (Paris) 1979, 75:463-505.
27. Greenfield N., Fasman G.D. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 1969, 8:4108-4116.
28. 2+-binding, conformational changes, and phosphodiesterase activity. J. Biol. Chem. 1977, 252:8415-8422.
29. 2+-dependent regulator protein. J. Biol. Chem. 1977, 252:4108-4117.
30. 2+ switch in muscular contraction. J. Biol. Chem. 1993, 268:19232-19238.
31. Li J., Jia Z., Zhou W., Wei Q. Calcineurin regulatory subunit B is a unique calcium sensor that regulates calcineurin in both calcium-dependent and calcium-independent manner. Proteins 2009, 77:612-623.
32. 2+-binding site: metal-binding properties, localization in tissues and cells, and effect on calcineurin. Biochemistry 2003, 42:14553-14565.
33. Suzuki K., Ishiura S. Effect of metal ions on the structure and activity of calcium-activated neutral protease (CANP). J. Biochem. 1983, 93:1463-1471.
34. Tanaka T., Hidaka H. Hydrophobic regions function in calmodulin-enzyme(s) interactions. J. Biol. Chem. 1980, 255:11078-11080.
35. Gagne S.M., Tsuda S., Li M.X., Chandra M., Smillie L.B., Sykes B.D. Quantification of the calcium-induced secondary structural changes in the regulatory domain of troponin-C. Protein Sci. 1994, 3:1961-1974.