Diacylglycerol Kinases

Topham, Matthew K.; Prescott, Stephen M.

doi:10.1002/0471203076.emm0852

Cited by 1 publication

(1 citation statement)

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“…Since DGKa is associated with DGKc, the former may contribute to the functionality of the catalytic domain. Whereas mammalian DGK enzymes can be classified into five groups according to sequence homology ( Topham and Prescott, 2010 ), plant DGKs only form three phylogenetic clusters, and exhibit a simpler domain organization. Though less varied and complex, plant DGKs included in Cluster I resemble the closest sequence orthologous of metazoan enzymes with proteins that display one or two DAG-binding domains (C1), an upstream basic region and an extended CRD in their N-terminus ( Gómez-Merino et al, 2004 ; Vaultier et al, 2008 ; Cacas et al, 2016 ).…”

Section: Discussionmentioning

confidence: 99%

Diacylglycerol Kinases Are Widespread in Higher Plants and Display Inducible Gene Expression in Response to Beneficial Elements, Metal, and Metalloid Ions

et al. 2017

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Diacylglycerol kinases (DGKs) are pivotal signaling enzymes that phosphorylate diacylglycerol (DAG) to yield phosphatidic acid (PA). The biosynthesis of PA from phospholipase D (PLD) and the coupled phospholipase C (PLC)/DGK route is a crucial signaling process in eukaryotic cells. Next to PLD, the PLC/DGK pathway is the second most important generator of PA in response to biotic and abiotic stresses. In eukaryotic cells, DGK, DAG, and PA are implicated in vital processes such as growth, development, and responses to environmental cues. A plethora of DGK isoforms have been identified so far, making this a rather large family of enzymes in plants. Herein we performed a comprehensive phylogenetic analysis of DGK isoforms in model and crop plants in order to gain insight into the evolution of higher plant DGKs. Furthermore, we explored the expression profiling data available in public data bases concerning the regulation of plant DGK genes in response to beneficial elements and other metal and metalloid ions, including silver (Ag), aluminum (Al), arsenic (As), cadmium (Cd), chromium (Cr), mercury (Hg), and sodium (Na). In all plant genomes explored, we were able to find DGK representatives, though in different numbers. The phylogenetic analysis revealed that these enzymes fall into three major clusters, whose distribution depends on the composition of structural domains. The catalytic domain conserves the consensus sequence GXGXXG/A where ATP binds. The expression profiling data demonstrated that DGK genes are rapidly but transiently regulated in response to certain concentrations and time exposures of beneficial elements and other ions in different plant tissues analyzed, suggesting that DGKs may mediate signals triggered by these elements. Though this evidence is conclusive, further signaling cascades that such elements may stimulate during hormesis, involving the phosphoinositide signaling pathway and DGK genes and enzymes, remain to be elucidated.

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