ArticleThe Biochemical journal1996
The C-terminal part of diacylglycerol kinase alpha lacking zinc fingers serves as a catalytic domain.
Article in The Biochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 69 citations in OpenAlex.
- Elusive structure of mammalian DGKs.Advances in biological regulation · 2022Review
- Review
- Subcellular Localization Relevance and Cancer-Associated Mechanisms of Diacylglycerol Kinases.International journal of molecular sciences · 2020Review
- DGKα in Neutrophil Biology and Its Implications for Respiratory Diseases.International journal of molecular sciences · 2019Review
- Diacylglycerol kinases: Relationship to other lipid kinases.Advances in biological regulation · 2019Review
- Article
- The Ligand Binding Landscape of Diacylglycerol Kinases.Cell chemical biology · 2017Article
- A novel diacylglycerol kinase α-selective inhibitor, CU-3, induces cancer cell apoptosis and enhances immune response.Journal of lipid research · 2016Article
- Diacylglycerol Kinase-ε: Properties and Biological Roles.Frontiers in cell and developmental biology · 2016Review
- The ζ isoform of diacylglycerol kinase plays a predominant role in regulatory T cell development and TCR-mediated ras signaling.Science signaling · 2013Article
- Bacterial expression strategies for several Sus scrofa diacylglycerol kinase alpha constructs: solubility challenges.Scientific reports · 2013Article
- Biosynthesis of alkyl lysophosphatidic acid by diacylglycerol kinases.Biochemical and biophysical research communications · 2012Article
- Diacylglycerol kinases as sources of phosphatidic acid.Biochimica et biophysica acta · 2009Review
- Mammalian diacylglycerol kinases: molecular interactions and biological functions of selected isoforms.Biochimica et biophysica acta · 2009Review
- Molecular determinants for interfacial binding and conformational change in a soluble diacylglycerol kinase.The Journal of biological chemistry · 2009Article
- Diacylglycerol kinases in immune cell function and self-tolerance.Immunological reviews · 2008Review
- Cloning and characterization of mr-s, a novel SAM domain protein, predominantly expressed in retinal photoreceptor cells.BMC developmental biology · 2006Article
- Domains, amino acid residues, and new isoforms of Caenorhabditis elegans diacylglycerol kinase 1 (DGK-1) important for terminating diacylglycerol signaling in vivo.The Journal of biological chemistry · 2005Article
- Mutations in the SAM domain of the ETV6-NTRK3 chimeric tyrosine kinase block polymerization and transformation activity.Molecular and cellular biology · 2004Article
- Site-directed mutagenesis of the active site of diacylglycerol kinase alpha: calcium and phosphatidylserine stimulate enzyme activity via distinct mechanisms.The Biochemical journal · 2003Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
All mammalian diacylglycerol kinase (DGK) isoenzymes so far cloned consist of four conserved regions, namely, C1, C2 (tandem EF-hand structures), C3 (tandem cysteine-rich zinc finger sequences) and the C-terminal C4 domains. To determine the catalytic domain we expressed in COS-7 cells various truncation mutants of pig DGK alpha and assessed their enzyme activities. We found that the C4 domain lacking the whole N-terminal region including the zinc fingers possessed DGK activity that was dependent on the concentrations of diacylglycerol and ATP very similarly, as did the wild-type DGK alpha. Furthermore the DGK activity of the wild-type DGK and that expressed by the C4 domain were similarly activated by anionic amphiphiles such as phosphatidylserine, phosphatidylinositol and deoxycholate. It was also shown that a DGK mutant consisting of the zinc fingers and the C4 domain has enzymological properties very similar to those expressed by the C4 domain alone. We also confirmed that the intact DGKs alpha, beta and gamma expressed in COS-7 cells displayed no detectable phorbol ester binding. These results show that the C4 domain of DGK is the catalytic region that is responsible for the enzyme activities sensitive to different activators. We cannot exclude the possibility that the N-terminal portion including the zinc fingers can still interact with diacylglycerol and activators without affecting the enzyme activity measured in vitro. However, it is quite likely that the DGK zinc fingers do not serve as diacylglycerol-binding sites, in contrast with those present in other proteins such as protein kinases C and n-chimaerin. Site-directed mutagenesis of all six putative ATP binding sites (Lys248, Lys383, Lys395, Lys483, Lys492, and Lys554) did not significantly affect the enzyme activity. We therefore suggest that DGK does not contain a typical P-loop of ATP binding sites.
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