DGK-θ: Structure, Enzymology, and Physiological Roles.
Diacylglycerol kinases (DGKs) are a family of enzymes that catalyze the ATP-dependent phosphorylation of diacylglycerol (DAG) to phosphatidic acid (PtdOH). The recognition of the importance of these enzymes has been increasing ever since it was determined that they played a role in the phosphatidylinositol (PtdIns) cycle and a number of excellent reviews have already been written [(see van Blitterswijk and Houssa, 2000; Kanoh et al., 2002; Mérida et al., 2008; Tu-Sekine and Raben, 2009, 2011; Shulga et al., 2011; Tu-Sekine et al., 2013) among others]. We now know there are ten mammalian DGKs that are organized into five classes. DGK-θ is the lone member of the Type V class of DGKs and remains as one of the least studied. This review focuses on our current understanding of the structure, enzymology, regulation, and physiological roles of this DGK and suggests some future areas of research to understand this DGK isoform.
Department of Biological Chemistry, The Johns Hopkins University School of Medicine Baltimore, MD, USA.
Becky
B
Tu-Sekine
Department of Biological Chemistry, The Johns Hopkins University School of Medicine Baltimore, MD, USA.
Hana L
HL
Goldschmidt
Department of Biological Chemistry, The Johns Hopkins University School of Medicine Baltimore, MD, USA.
Daniel M
DM
Raben
diacylglycerol kinase; interfacial enzymology; phosphatidic acid; regulation; synaptic vesicle cycle
Trends Biochem Sci. 2002 Jun;27(6):273-5
12069781
Mol Cell Biol. 1998 Feb;18(2):762-70
9447972
J Biol Chem. 2003 May 16;278(20):18448-54
12621060
Biochemistry. 2007 Jan 23;46(3):924-32
17223715
Adv Enzyme Regul. 2010;50(1):81-94
19914279
Am J Physiol Heart Circ Physiol. 2007 May;292(5):H2248-56
17208990
J Cell Biochem. 2006 Feb 15;97(3):474-84
16288460
J Biol Chem. 1997 Apr 18;272(16):10422-8
9099683
Cell Signal. 2004 Nov;16(11):1263-71
15337525
Neuron. 1999 Sep;24(1):231-42
10677040
Neuron. 1999 Oct;24(2):323-33
10571227
J Mol Biol. 2005 May 6;348(3):759-75
15826669
Cell Death Differ. 2010 Jun;17(6):1059-68
20057501
BMC Dev Biol. 2013 Oct 01;13:35
24079595
Structure. 2008 Mar;16(3):380-7
18334213
Adv Biol Regul. 2013 Jan;53(1):118-26
23266086
Biochem J. 2001 Jan 1;353(Pt 1):129-137
11115406
Adv Enzyme Regul. 2002;42:213-26
12123717
J Biol Chem. 1999 Mar 12;274(11):6820-2
10066731
Cell Rep. 2016 Jan 12;14 (2):200-7
26748701
J Biochem. 2002 May;131(5):629-33
11983067
Mol Cell Biol. 2007 Oct;27(19):6669-85
17664281
Biochim Biophys Acta. 2004 Mar 22;1636(2-3):169-74
15164764
Exp Cell Res. 2003 Jul 1;287(1):143-54
12799190
Mol Cell Biol. 2005 Aug;25(16):7289-302
16055737
Genes Dev. 2006 Jan 1;20(1):65-76
16391233
Structure. 2008 Jul;16(7):1036-46
18611377
Adv Enzyme Regul. 2006;46:12-24
16854454
J Biol Chem. 2001 Jun 29;276(26):23288-95
11309392
J Pharmacol Sci. 2014;124(3):336-43
24599142
Crit Rev Biochem Mol Biol. 2011 Oct;46(5):353-64
21539478
J Hum Hypertens. 2001 Feb;15(2):93-8
11317187
Semin Reprod Med. 2012 Oct;30(5):374-81
23044873
Trends Biochem Sci. 2016 May;41(5):395-409
27021309
Biochim Biophys Acta. 2014 Apr 4;1841(4):552-62
24369117
Chem Rev. 2011 Oct 12;111(10):6186-208
21800853
Protein Sci. 1997 Feb;6(2):477-80
9041654
Cell. 1994 Mar 11;76(5):933-45
7510218
Proteins. 2007 Jul 1;68(1):13-25
17393457
J Lipid Res. 2013 Aug;54(8):2121-32
23610160
Cell Signal. 2000 Oct;12(9-10):595-605
11080611
J Cell Physiol. 2009 Sep;220(3):548-52
19472209
J Biol Chem. 2005 Mar 18;280(11):9870-8
15632189
Biochim Biophys Acta. 2012 Dec;1823(12):2210-6
22974639
J Biol Chem. 2007 Jul 6;282(27):19644-52
17351295
Biochem J. 2008 Jan 1;409(1):1-18
18062770
Annu Rev Biophys. 2012;41:81-101
22224599
Science. 2007 Feb 2;315 (5812):663-6
17272726