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Mammalian DGK consists of ten isozymes (\u03b1\u2013\u03ba) and governs a wide range of physiological and pathological events, including immune responses, neuronal networking, bipolar disorder, obsessive-compulsive disorder, fragile X syndrome, cancer, and type 2 diabetes. DG and PA comprise diverse molecular species that have different acyl chains at the sn-1 and sn-2 positions. Because the DGK activity is essential for phosphatidylinositol turnover, which exclusively produces 1-stearoyl-2-arachidonoyl-DG, it has been generally thought that all DGK isozymes utilize the DG species derived from the turnover. However, it was recently revealed that DGK isozymes, except for DGK\u03b5, phosphorylate diverse DG species, which are not derived from phosphatidylinositol turnover. In addition, various PA-binding proteins (PABPs), which have different selectivities for PA species, were recently found. These results suggest that DGK\u2013PA\u2013PABP axes can potentially construct a large and complex signaling network and play physiologically and pathologically important roles in addition to DGK-dependent attenuation of DG\u2013DG-binding protein axes. For example, 1-stearoyl-2-docosahexaenoyl-PA produced by DGK\u03b4 interacts with and activates Praja-1, the E3 ubiquitin ligase acting on the serotonin transporter, which is a target of drugs for obsessive-compulsive and major depressive disorders, in the brain. This article reviews recent research progress on PA species produced by DGK isozymes, the selective binding of PABPs to PA species and a phosphatidylinositol turnover-independent DG supply pathway.<\/jats:p>","DOI":"10.3390\/ijms21186794","type":"journal-article","created":{"date-parts":[[2020,9,16]],"date-time":"2020-09-16T10:30:12Z","timestamp":1600252212000},"page":"6794","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":68,"title":["New Era of Diacylglycerol Kinase, Phosphatidic Acid and Phosphatidic Acid-Binding Protein"],"prefix":"10.3390","volume":"21","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0857-0377","authenticated-orcid":false,"given":"Fumio","family":"Sakane","sequence":"first","affiliation":[{"name":"Department of Chemistry, Graduate School of Science, Chiba University, Chiba 263-8522, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4213-0631","authenticated-orcid":false,"given":"Fumi","family":"Hoshino","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Graduate School of Science, Chiba University, Chiba 263-8522, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3645-8382","authenticated-orcid":false,"given":"Chiaki","family":"Murakami","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Graduate School of Science, Chiba University, Chiba 263-8522, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,9,16]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1016\/j.bbalip.2006.04.001","article-title":"Diacylglycerol, phosphatidic acid, and the converting enzyme, diacylglycerol kinase, in the nucleus","volume":"1761","author":"Goto","year":"2006","journal-title":"Biochim. 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