Abstract
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.
Highlights
Specialty section: This article was submitted to Signaling, a section of the journal Frontiers in Cell and Developmental
This review focuses on our current understanding of the structure, enzymology, regulation, and physiological roles of this Diacylglycerol kinases (DGKs) and suggests some future areas of research to understand this DGK isoform
Like other DGKs, the C1 domains of DGK-θ is homologous to PKC C1A and C1C domains with an extended region closest to the presumed catalytic domain near the C terminus
Summary
Binds to this domain either and it is unclear as to whether RhoA is a regulator under various physiological conditions (see Regulation below). DGK-θ is very sensitive to the bulk and surface concentration of the DAG substrate This provides a mechanism for regulating the enzyme in response to increases in DAG that accompany many signaling pathways. While the precise RhoA binding regions have not been fully identified, a potential important role for these interactions is given support from the observations that other DGKs may show similar associations. Additional studies are clearly required to define the precise role of DGK-θ phosphorylation in membrane association and catalytic activation. Additional analyses showed that while the acidic phospholipids recruit polybasic cofactors to the surface of artificial membranes, they do not affect the membrane association of DGK-θ suggesting interfacial association and catalytic activity are independently regulated. The polybasic protein that represents the physiological regulator of DGK-θ in various tissues has/have not been identified and represents an important challenge in the field
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