Diacylglycerol kinases as sources of phosphatidic acid.
作者： Jinjin Cai , Hanan Abramovici , Stephen H. Gee , Matthew K. Topham
DOI: 10.1016/J.BBALIP.2009.02.010
关键词: Biochemistry 、 Cell biology 、 Signal transduction 、 Lipid signaling 、 Kinase 、 Phosphatidic acid 、 Phosphatidylinositol 、 Plasma protein binding 、 Biology 、 Diacylglycerol kinase
摘要: There are ten mammalian diacylglycerol kinases (DGKs) whose primary role is to terminate (DAG) signaling. However, it becoming increasingly apparent that DGKs also influence signaling events through their product, phosphatidic acid (PA). They do so in some cases by associating with proteins and then modifying activity generating PA. In other cases, broadly regulate virtue of ability provide PA for the synthesis phosphatidylinositols (PtdIns).
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sci-hub.se 参考文章(94)
Keiko YAMADA, Fumio SAKANE, Norio MATSUSHIMA, Hideo KANOH, EF-hand motifs of alpha, beta and gamma isoforms of diacylglycerol kinase bind calcium with different affinities and conformational changes. Biochemical Journal. ,vol. 321, pp. 59- 64 ,(1997) , 10.1042/BJ3210059
R. Guo, C.-K. Wan, J. H. Carpenter, T. Mousallem, R.-M. N. Boustany, C.-T. Kuan, A. W. Burks, X.-P. Zhong, Synergistic control of T cell development and tumor suppression by diacylglycerol kinase α and ζ Proceedings of the National Academy of Sciences of the United States of America. ,vol. 105, pp. 11909- 11914 ,(2008) , 10.1073/PNAS.0711856105
H Inoue, T Yoshioka, Y Hotta, Diacylglycerol kinase defect in a Drosophila retinal degeneration mutant rdgA. Journal of Biological Chemistry. ,vol. 264, pp. 5996- 6000 ,(1989) , 10.1016/S0021-9258(18)83648-1
S.M. Prescott, P.W. Majerus, The fatty acid composition of phosphatidylinositol from thrombin-stimulated human platelets. Journal of Biological Chemistry. ,vol. 256, pp. 579- 582 ,(1981) , 10.1016/S0021-9258(19)70010-6
T H Chuang, B P Bohl, G M Bokoch, Biologically active lipids are regulators of Rac.GDI complexation. Journal of Biological Chemistry. ,vol. 268, pp. 26206- 26211 ,(1993) , 10.1016/S0021-9258(19)74301-4
Fumio Sakane, Hideo Kanoh, Shin-Ichi Imai, Ikuo Wada, Masahiro Kai, Molecular cloning of a diacylglycerol kinase isozyme predominantly expressed in human retina with a truncated and inactive enzyme expression in most other human cells Journal of Biological Chemistry. ,vol. 269, pp. 18492- 18498 ,(1994) , 10.1016/S0021-9258(17)32336-0
H Kanoh, H Kondoh, T Ono, Diacylglycerol kinase from pig brain. Purification and phospholipid dependencies. Journal of Biological Chemistry. ,vol. 258, pp. 1767- 1774 ,(1983) , 10.1016/S0021-9258(18)33053-9
Matthew K. Topham, Michaeline Bunting, Guy A. Zimmerman, Thomas M. McIntyre, Perry J. Blackshear, Stephen M. Prescott, Protein kinase C regulates the nuclear localization of diacylglycerol kinase-ζ Nature. ,vol. 394, pp. 697- 700 ,(1998) , 10.1038/29337
Fumio SAKANE, Masahiro KAI, Ikuo WADA, Shin-ichi IMAI, Hideo KANOH, The C-terminal part of diacylglycerol kinase alpha lacking zinc fingers serves as a catalytic domain. Biochemical Journal. ,vol. 318, pp. 583- 590 ,(1996) , 10.1042/BJ3180583
N Harden, S F Yap, M A Chiam, L Lim, A Drosophila gene encoding a protein with similarity to diacylglycerol kinase is expressed in specific neurons. Biochemical Journal. ,vol. 289, pp. 439- 444 ,(1993) , 10.1042/BJ2890439