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Cited by 123Lipid metabolism and biosynthesisSphingolipid Metabolism and SignalingCancer, Lipids, and Metabolism

CDP-Diacylglycerol Synthases (CDS): Gateway to Phosphatidylinositol and Cardiolipin Synthesis

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Blunsom, Nicholas J., Cockcroft, Shamshad·2020·Frontiers in Cell and Developmental Biology
DOI 10.3389/fcell.2020.00063PMC PMC7018664
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Abstract

Cytidine diphosphate diacylglycerol (CDP-DAG) is a key intermediate in the synthesis of phosphatidylinositol (PI) and cardiolipin (CL). Both PI and CL have highly specialized roles in cells. PI can be phosphorylated and these phosphorylated derivatives play major roles in signal transduction, membrane traffic, and maintenance of the actin cytoskeletal network. CL is the signature lipid of mitochondria and has a plethora of functions including maintenance of cristae morphology, mitochondrial fission, and fusion and for electron transport chain super complex formation. Both lipids are synthesized in different organelles although they share the common intermediate, CDP-DAG. CDP-DAG is synthesized from phosphatidic acid (PA) and CTP by enzymes that display CDP-DAG synthase activities. Two families of enzymes, CDS and TAMM41, which bear no sequence or structural relationship, have now been identified. TAMM41 is a peripheral membrane protein localized in the inner mitochondrial membrane required for CL synthesis. CDS enzymes are ancient integral membrane proteins found in all three domains of life. In mammals, they provide CDP-DAG for PI synthesis and for phosphatidylglycerol (PG) and CL synthesis in prokaryotes. CDS enzymes are critical for maintaining phosphoinositide levels during phospholipase C (PLC) signaling. Hydrolysis of PI (4,5) bisphosphate by PLC requires the resynthesis of PI and CDS enzymes catalyze the rate-limiting step in the process. In mammals, the protein products of two CDS genes (CDS1 and CDS2) localize to the ER and it is suggested that CDS2 is the major CDS for this process. Expression of CDS enzymes are regulated by transcription factors and CDS enzymes may also contribute to CL synthesis in mitochondria. Studies of CDS enzymes in protozoa reveal spatial segregation of CDS enzymes from the rest of the machinery required for both PI and CL synthesis identifying a key gap in our understanding of how CDP-DAG can cross the different membrane compartments in protozoa and in mammals.

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  • There are two CDS enzymes (CDS1 and CDS2) and one PIS enzyme, all localised at the ER and integral membrane proteins.

    “There are two CDS enzymes, CDS1 and CDS2, and one PIS enzyme, both localised at the ER; all three enzymes are integral membrane proteins [6,22].”

    From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [22]

    The ‘Mammalian CDS1 and CDS2’ section states that both CDS enzymes are integral membrane proteins and localize to ER membranes; it also places PIS at the ER in COS-7 cells. Our copy does not state that PIS is an integral membrane protein or establish that there is only one PIS enzyme, so those parts of the claim are not supported by this source. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

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Research works printed but not linked: 162

  1. Acehan D. Malhotra A. Xu Y. Ren M. Stokes D. L. Schlame M. (2011). Cardiolipin affects the supramolecular organization of ATP synthase in mitochondria. Biophys. J. 100 2184– 2192. 10.1016/j.bpj.2011.03.031 21539786 PMC3150712 · DOI
  2. AhYoung A. P. Jiang J. Zhang J. Khoi Dang X. Loo J. A. Zhou Z. H. (2015). Conserved SMP domains of the ERMES complex bind phospholipids and mediate tether assembly. Proc. Natl. Acad. Sci. U.S.A. 112 E3179– E3188. 10.1073/pnas.1422363112 26056272 PMC4485115 · DOI
  3. Alfonso Pecchio A. R. Cardozo Gizzi A. M. Renner M. L. Molina-Calavita M. Caputto B. L. (2011). c-Fos activates and physically interacts with specific enzymes of the pathway of synthesis of polyphosphoinositides. Mol. Biol. Cell 22 4716– 4725. 10.1091/mbc.E11-03-0259 21998197 PMC3237616 · DOI
  4. Alhouayek M. Masquelier J. Muccioli G. G. (2018). Lysophosphatidylinositols, from cell membrane constituents to GPR55 Ligands. Trends Pharmacol. Sci. 39 586– 604. 10.1016/j.tips.2018.02.011 29588059 · DOI
  5. Anderson K. E. Kielkowska A. Durrant T. N. Juvin V. Clark J. Stephens L. R. (2013). Lysophosphatidylinositol-acyltransferase-1 (LPIAT1) is required to maintain physiological levels of PtdIns and PtdInsP(2) in the mouse. PLoS. One 8: e58425. 10.1371/journal.pone.0058425 23472195 PMC3589398 · DOI
  6. Arimoto T. Takeishi Y. Takahashi H. Shishido T. Niizeki T. Koyama Y. (2006). Cardiac-specific overexpression of diacylglycerol kinase zeta prevents Gq protein-coupled receptor agonist-induced cardiac hypertrophy in transgenic mice. Circulation 113 60– 66. 10.1161/circulationaha.105.560771 16380548 · DOI
  7. Athea Y. Viollet B. Mateo P. Rousseau D. Novotova M. Garnier A. (2007). AMP-activated protein kinase alpha2 deficiency affects cardiac cardiolipin homeostasis and mitochondrial function. Diabetes 56 786– 794. 10.2337/db06-0187 17327449 PMC1955690 · DOI
  8. Baggelaar M. P. Maccarrone M. van der Stelt M. (2018). 2-Arachidonoylglycerol: a signaling lipid with manifold actions in the brain. Prog. Lipid Res. 71 1– 17. 10.1016/j.plipres.2018.05.002 29751000 · DOI · Paper page
  9. Baile M. G. Lu Y. W. Claypool S. M. (2014). The topology and regulation of cardiolipin biosynthesis and remodeling in yeast. Chem. Phys. Lipids 179 25– 31. 10.1016/j.chemphyslip.2013.10.008 24184646 PMC3947685 · DOI
  10. Balla T. (2013). Phosphoinositides: tiny lipids with giant impact on cell regulation. Physiol. Rev. 93 1019– 1137. 10.1152/physrev.00028.2012 23899561 PMC3962547 · DOI · Paper page
  11. Barneda D. Cosulich S. Stephens L. Hawkins P. (2019). How is the acyl chain composition of phosphoinositides created and does it matter? Biochem. Soc. Trans. 47 1291– 1305. 10.1042/BST20190205 31657437 PMC6824679 · DOI · Paper page
  12. Barneda D. Planas-Iglesias J. Gaspar M. L. Mohammadyani D. Prasannan S. Dormann D. (2015). The brown adipocyte protein CIDEA promotes lipid droplet fusion via a phosphatidic acid-binding amphipathic helix. Elife 4: e07485. 10.7554/eLife.07485 26609809 PMC4755750 · DOI
  13. Blunsom N. J. Cockcroft S. (2020). Phosphatidylinositol synthesis at the endoplasmic reticulum. Biochim. Biophys. Acta Mol. Cell Biol. Lipids 1865 158471. 31173893
  14. Blunsom N. J. Gomez-Espinosa E. Ashlin T. G. Cockcroft S. (2017). Mitochondrial CDP-diacylglycerol synthase activity is due to the peripheral protein. TAMM41 and not due to the integral membrane protein, CDP-diacylglycerol synthase 1. Biochim. Biophys. Acta 1863 284– 298. 10.1016/j.bbalip.2017.12.005 29253589 PMC5791848 · DOI
  15. Blunsom N. J. Gomez-Espinosa E. Ashlin T. G. Cockcroft S. (2019). Sustained phospholipase C stimulation of H9c2 cardiomyoblasts by vasopressin induces an increase in CDP-diacylglycerol synthase 1 (CDS1) through protein kinase C and cFos. Biochim. Biophys. Acta Mol. Cell Biol. Lipids 1864 1072– 1082. 10.1016/j.bbalip.2019.03.002 30862571 PMC6495107 · DOI
  16. Bozelli J. C. Jr. Epand R. M. (2019a). Role of membrane shape in regulating the phosphatidylinositol cycle at contact sites. Chem. Phys. Lipids 221 24– 29. 10.1016/j.chemphyslip.2019.03.002 30851248 · DOI
  17. Bozelli J. C. Jr. Epand R. M. (2019b). Specificity of Acyl chain composition of phosphatidylinositols. Proteomics 19: e1900138. 10.1002/pmic.201900138 31381272 · DOI
  18. Broekman M. J. Ward J. W. Marcus A. J. (1981). Fatty acid composition of phosphatidylinositol and phosphatidic acid in stimulated platelets. Persistence of arachidonyl-stearyl structure. J. Biol. Chem. 256 8271– 8274. 6790536
  19. Cardozo Gizzi A. M. Caputto B. L. (2013). Mechanistic insights into the nongenomic regulation of phospholipid synthesizing enzymes. IUBMB Life 65 584– 592. 10.1002/iub.1173 23712998 · DOI
  20. Carman G. M. Kelley M. J. (1992). “ CDPdiacylglycerol synthase from yeast,” in Methods in Enzymology, eds Dennis E. A. Vance e. E., (Cambridge, MA: Academic Press). 209 242– 247. 10.1016/0076-6879(92)09030-7 1323038 · DOI
  21. Chiapparino A. Maeda K. Turei D. Saez-Rodriguez J. Gavin A. C. (2016). The orchestra of lipid-transfer proteins at the crossroads between metabolism and signaling. Prog. Lipid Res. 61 30– 39. 10.1016/j.plipres.2015.10.004 26658141 · DOI
  22. Choy C. H. Han B. K. Botelho R. J. (2017). Phosphoinositide diversity, distribution, and effector function: stepping out of the box. BioEssays 39: 1700121. 10.1002/bies.201700121 28977683 · DOI
  23. Chung J. Torta F. Masai K. Lucast L. Czapla H. Tanner L. B. (2015). Intracellular transport. PI4P/phosphatidylserine countertransport at ORP5- and ORP8-mediated ER-plasma membrane contacts. Science 349 428– 432. 10.1126/science.aab1370 26206935 PMC4638224 · DOI
  24. Cockcroft S. Raghu P. (2016). Topological organisation of the phosphatidylinositol 4,5-bisphosphate-phospholipase C resynthesis cycle: PITPs bridge the ER-PM gap. Biochem. J. 473 4289– 4310. 10.1042/bcj20160514c 27888240 · DOI · Paper page
  25. Comer F. I. Parent C. A. (2007). Phosphoinositides specify polarity during epithelial organ development. Cell 128 239– 240. 10.1016/j.cell.2007.01.010 17254962 · DOI
  26. D’Angelo G. Vicinanza M. Di Campli A. De Matteis M. A. (2008). The multiple roles of PtdIns(4)P – not just the precursor of PtdIns(4,5)P2. J. Cell Sci 121(Pt 12) 1955– 1963. 10.1242/jcs.023630 18525025 · DOI
  27. Dechamps S. Shastri S. Wengelnik K. Vial H. J. (2010). Glycerophospholipid acquisition in Plasmodium – a puzzling assembly of biosynthetic pathways. Int. J. Parasitol. 40 1347– 1365. 10.1016/j.ijpara.2010.05.008 20600072 · DOI
  28. Di W. Lv J. Jiang S. Lu C. Yang Z. Ma Z. (2018). PGC-1: the energetic regulator in cardiac metabolism. Curr. Issues Mol. Biol. 28 29– 46. 10.21775/cimb.028.029 29388552 · DOI
  29. Di Paolo G. de Camilli P. (2006). Phosphoinositides in cell regulation and membrane dynamics. Nature 443 651– 657. 10.1038/nature05185 17035995 · DOI · Paper page
  30. D’Souza K. Epand R. M. (2015). The phosphatidylinositol synthase-catalyzed formation of phosphatidylinositol does not exhibit acyl chain specificity. Biochemistry 54 1151– 1153. 10.1021/bi5015634 25633188 · DOI
  31. D’Souza K. Kim Y. J. Balla T. Epand R. M. (2014). Distinct properties of the two isoforms of CDP-diacylglycerol synthase. Biochemistry 53 7358– 7367. 10.1021/bi501250m 25375833 PMC4255645 · DOI
  32. Dudek J. (2017). Role of cardiolipin in mitochondrial signaling pathways. Front. Cell Dev. Biol. 5: 90. 10.3389/fcell.2017.00090 29034233 PMC5626828 · DOI
  33. Dudek J. Cheng I. F. Balleininger M. Vaz F. M. Streckfuss-Bomeke K. Hubscher D. (2013). Cardiolipin deficiency affects respiratory chain function and organization in an induced pluripotent stem cell model of Barth syndrome. Stem Cell Res. 11 806– 819. 10.1016/j.scr.2013.05.005 23792436 · DOI
  34. Dzugasova V. Obernauerova M. Horvathova K. Vachova M. Zakova M. Subik J. (1998). Phosphatidylglycerolphosphate synthase encoded by the PEL1/PGS1 gene in Saccharomyces cerevisiae is localized in mitochondria and its expression is regulated by phospholipid precursors. Curr. Genet. 34 297– 302. 10.1007/s002940050399 9799363 · DOI
  35. Epand R. M. So V. Jennings W. Khadka B. Gupta R. S. Lemaire M. (2016). Diacylglycerol Kinase-ε: properties and biological roles. Front. Cell Dev. Biol. 4: 112. 10.3389/fcell.2016.00112 27803897 PMC5067486 · DOI
  36. Fei W. Shui G. Zhang Y. Krahmer N. Ferguson C. Kapterian T. S. (2011). A role for phosphatidic acid in the formation of “supersized” lipid droplets. PLoS.Genet. 7: e1002201. 10.1371/journal.pgen.1002201 21829381 PMC3145623 · DOI
  37. Gallas M. R. Dienhart M. K. Stuart R. A. Long R. M. (2006). Characterization of Mmp37p, a Saccharomyces cerevisiae mitochondrial matrix protein with a role in mitochondrial protein import. Mol. Biol. Cell 17 4051– 4062. 10.1091/mbc.e06-04-0366 16790493 PMC1556384 · DOI
  38. Galmes R. Houcine A. van Vliet A. R. Agostinis P. Jackson C. L. Giordano F. (2016). ORP5/ORP8 localize to endoplasmic reticulum-mitochondria contacts and are involved in mitochondrial function. EMBO Rep. 17 800– 810. 10.15252/embr.201541108 27113756 PMC5278607 · DOI
  39. Ganong B. R. Leonard J. M. Raetz C. R. (1980). Phosphatidic acid accumulation in the membranes of Escherichia coli mutants defective in CDP-diglyceride synthetase. J. Biol. Chem. 255 1623– 1629. 6243645
  40. Ganong B. R. Raetz C. R. (1982). Massive accumulation of phosphatidic acid in conditionally lethal CDP-diglyceride synthetase mutants and cytidine auxotrophs of Escherichia coli. J. Biol. Chem. 257 389– 394. 6273438
  41. Garner K. Hunt A. N. Koster G. Somerharju P. Grover E. Li M. (2012). Phosphatidylinositol transfer protein. Cytoplasmic 1 (PITPNC1) binds and transfers phosphatidic acid. J. Biol. Chem. 287 32263– 32276. 10.1074/jbc.M112.375840 22822086 PMC3442557 · DOI
  42. Gemmill R. M. Roche J. Potiron V. A. Nasarre P. Mitas M. Coldren C. D. (2011). ZEB1-responsive genes in non-small cell lung cancer. Cancer Lett. 300 66– 78. 10.1016/j.canlet.2010.09.007 20980099 PMC3337721 · DOI
  43. Gheldof A. Hulpiau P. van Roy F. De Craene B. Berx G. (2012). Evolutionary functional analysis and molecular regulation of the ZEB transcription factors. Cell. Mol. Life Sci. 69 2527– 2541. 10.1007/s00018-012-0935-3 22349261 PMC11115101 · DOI
  44. Giblin W. Skinner M. E. Lombard D. B. (2014). Sirtuins: guardians of mammalian healthspan. Trends Genet. 30 271– 286. 10.1016/j.tig.2014.04.007 24877878 PMC4077918 · DOI
  45. Gong J. Sun Z. Wu L. Xu W. Schieber N. Xu D. (2011). Fsp27 promotes lipid droplet growth by lipid exchange and transfer at lipid droplet contact sites. J. Cell Biol. 195 953– 963. 10.1083/jcb.201104142 22144693 PMC3241734 · DOI
  46. Hagio M. Gombos Z. Varkonyi Z. Masamoto K. Sato N. Tsuzuki M. (2000). Direct evidence for requirement of phosphatidylglycerol in photosystem II of photosynthesis. Plant Physiol. 124 795– 804. 10.1104/pp.124.2.795 11027727 PMC59183 · DOI
  47. Halford S. Dulai K. S. Daw S. C. Fitzgibbon J. Hunt D. M. (1998). Isolation and chromosomal localization of two human CDP-diacylglycerol synthase (CDS) genes. Genomics 54 140– 144. 10.1006/geno.1998.5547 9806839 · DOI
  48. Halford S. Inglis S. Gwilliam R. Spencer P. Mohamed M. Ebenezer N. D. (2002). Genomic organization of human CDS2 and evaluation as a candidate gene for corneal hereditary endothelial dystrophy 2 on chromosome 20p13. Exp. Eye Res. 75 619– 623. 10.1006/exer.2002.2052 12457874 · DOI
  49. Harami G. M. Gyimesi M. Kovacs M. (2013). From keys to bulldozers: expanding roles for winged helix domains in nucleic-acid-binding proteins. Trends Biochem. Sci. 38 364– 371. 10.1016/j.tibs.2013.04.006 23768997 · DOI
  50. Hardie R. C. Liu C. H. Randall A. S. Sengupta S. (2015). In vivo tracking of phosphoinositides in Drosophila photoreceptors. J. Cell Sci. 128 4328– 4340. 10.1242/jcs.180364 26483384 PMC4712823 · DOI
  51. Haselier A. Akbari H. Weth A. Baumgartner W. Frentzen M. (2010). Two closely related genes of Arabidopsis encode plastidial cytidinediphosphate diacylglycerol synthases essential for photoautotrophic growth. Plant Physiol. 153 1372– 1384. 10.1104/pp.110.156422 20442275 PMC2899908 · DOI
  52. He Y. Yam C. Pomraning K. Chin J. S. Yew J. Y. Freitag M. (2014). Increase in cellular triacylglycerol content and emergence of large ER-associated lipid droplets in the absence of CDP-DG synthase function. Mol. Biol. Cell 25 4083– 4095. 10.1091/mbc.E14-03-0832 25318672 PMC4263451 · DOI
  53. Heacock A. M. Uhler M. D. Agranoff B. W. (1996). Cloning of CDP-diacylglycerol synthase from a human neuronal cell line. J. Neurochem. 67 2200– 2203. 10.1046/j.1471-4159.1996.67052200.x 8863531 · DOI
  54. Henry S. A. Kohlwein S. D. Carman G. M. (2012). Metabolism and regulation of glycerolipids in the yeast Saccharomyces cerevisiae. Genetics 190 317– 349. 10.1534/genetics.111.130286 22345606 PMC3276621 · DOI
  55. Hill J. T. Demarest B. L. Bisgrove B. W. Gorsi B. Su Y.-C. Yost H. J. (2013). MMAPPR: mutation mapping analysis pipeline for pooled RNA-seq. Genome Res. 23 687– 697. 10.1101/gr.146936.112 23299975 PMC3613585 · DOI
  56. Hille B. Dickson E. J. Kruse M. Vivas O. Suh B. C. (2015). Phosphoinositides regulate ion channels. Biochim. Biophys. Acta 1851 844– 856. 10.1016/j.bbalip.2014.09.010 25241941 PMC4364932 · DOI · Paper page
  57. Hirabayashi Y. Kwon S. K. Paek H. Pernice W. M. Paul M. A. Lee J. (2017). ER-mitochondria tethering by PDZD8 regulates Ca(2+) dynamics in mammalian neurons. Science 358 623– 630. 10.1126/science.aan6009 29097544 PMC5818999 · DOI
  58. Hishikawa D. Hashidate T. Shimizu T. Shindou H. (2014). Diversity and function of membrane glycerophospholipids generated by the remodeling pathway in mammalian cells. J. Lipid Res. 55 799– 807. 10.1194/jlr.R046094 24646950 PMC3995458 · DOI
  59. Horibata Y. Ando H. Satou M. Shimizu H. Mitsuhashi S. Shimizu Y. (2017). Identification of the N-terminal transmembrane domain of StarD7 and its importance for mitochondrial outer membrane localization and phosphatidylcholine transfer. Sci. Rep. 7: 8793. 10.1038/s41598-017-09205-1 28821867 PMC5562819 · DOI
  60. Horvath S. E. Daum G. (2013). Lipids of mitochondria. Prog. Lipid Res. 52 590– 614. 10.1016/j.plipres.2013.07.002 24007978 · DOI
  61. Hozumi Y. Fujiwara H. Kaneko K. Fujii S. Topham M. K. Watanabe M. (2017). Diacylglycerol kinase ε localizes to subsurface cisterns of cerebellar Purkinje cells. Cell Tissue Res. 368 441– 458. 10.1007/s00441-017-2579-y 28191598 · DOI
  62. Icho T. Sparrow C. P. Raetz C. R. (1985). Molecular cloning and sequencing of the gene for CDP-diglyceride synthetase of Escherichia coli. J. Biol. Chem. 260 12078– 12083. 2995358
  63. Ikon N. Ryan R. O. (2017). Cardiolipin and mitochondrial cristae organization. Biochim. Biophys. Acta Biomembr. 1859 1156– 1163. 10.1016/j.bbamem.2017.03.013 28336315 PMC5426559 · DOI
  64. Imae R. Inoue T. Nakasaki Y. Uchida Y. Ohba Y. Kono N. (2012). LYCAT, a homologue of C. elegans acl-8, acl-9, and acl-10, determines the fatty acid composition of phosphatidylinositol in mice. J. Lipid Res. 53 335– 347. 10.1194/jlr.M018655 22172515 PMC3276457 · DOI
  65. Inglis-Broadgate S. L. Ocaka L. Banerjee R. Gaasenbeek M. Chapple J. P. Cheetham M. E. (2005). Isolation and characterization of murine Cds (CDP-diacylglycerol synthase) 1 and 2. Gene 356 19– 31. 10.1016/j.gene.2005.04.037 16023307 · DOI
  66. Inloes J. M. Jing H. Cravatt B. F. (2018). The spastic paraplegia-associated phospholipase DDHD1 is a primary brain phosphatidylinositol lipase. Biochemistry 57 5759– 5767. 10.1021/acs.biochem.8b00810 30221923 PMC6237197 · DOI
  67. Jain S. Caforio A. Fodran P. Lolkema J. S. Minnaard A. J. Driessen A. J. M. (2014). Identification of CDP-archaeol synthase, a missing link of ether lipid biosynthesis in Archaea. Chem. Biol. 21 1392– 1401. 10.1016/j.chembiol.2014.07.022 25219966 · DOI
  68. Jiao H. Yin Y. Liu Z. (2019). Structures of the mitochondrial CDP-DAG synthase Tam41 suggest a potential lipid substrate pathway from membrane to the active site. Structure 27, 1258– 1269.e4. 10.1016/j.str.2019.04.017 31178220 · DOI
  69. Kawasaki K. Kuge O. Yamakawa Y. Nishijima M. (2001). Purification of phosphatidylglycerophosphate synthase from Chinese hamster ovary cells. Biochem. J. 354(Pt 1) 9– 15. 10.1042/bj3540009 11171073 PMC1221622 · DOI
  70. Kelley M. J. Carman G. M. (1987). Purification and characterization of CDP-diacylglycerol synthase from Saccharomyces cerevisiae. J. Biol. Chem. 262 14563– 14570. 2822695
  71. Kim H. S. Xiao C. Wang R. H. Lahusen T. Xu X. Vassilopoulos A. (2010). Hepatic-specific disruption of SIRT6 in mice results in fatty liver formation due to enhanced glycolysis and triglyceride synthesis. Cell Metab. 12 224– 236. 10.1016/j.cmet.2010.06.009 20816089 PMC2935915 · DOI
  72. Kim Y. J. Guzman-Hernandez M. L. Balla T. (2011). A highly dynamic ER-derived phosphatidylinositol-synthesizing organelle supplies phosphoinositides to cellular membranes. Dev. Cell 21 813– 824. 10.1016/j.devcel.2011.09.005 22075145 PMC3235737 · DOI
  73. Kiyasu J. Y. Pieringer R. A. Paulus H. Kennedy E. P. (1963). The biosynthesis of phosphatidylglycerol. J. Biol. Chem. 238 2293– 2298. 14033231
  74. Kong P. Lehmann M. J. Helms J. B. Brouwers J. F. Gupta N. (2018). Lipid analysis of Eimeria sporozoites reveals exclusive phospholipids, a phylogenetic mosaic of endogenous synthesis, and a host-independent lifestyle. Cell Discov. 4: 24. 10.1038/s41421-018-0023-4 29844921 PMC5964319 · DOI
  75. Kong P. Ufermann C. M. Zimmermann D. L. M. Yin Q. Suo X. Helms J. B. (2017). Two phylogenetically and compartmentally distinct CDP-diacylglycerol synthases cooperate for lipid biogenesis in Toxoplasma gondii. J. Biol. Chem. 292 7145– 7159. 10.1074/jbc.M116.765487 28314772 PMC5409480 · DOI
  76. Kuchta K. Knizewski L. Wyrwicz L. S. Rychlewski L. Ginalski K. (2009). Comprehensive classification of nucleotidyltransferase fold proteins: identification of novel families and their representatives in human. Nucleic Acids Res. 37 7701– 7714. 10.1093/nar/gkp854 19833706 PMC2794190 · DOI
  77. Kutik S. Rissler M. Guan X. L. Guiard B. Shui G. Gebert N. (2008). The translocator maintenance protein Tam41 is required for mitochondrial cardiolipin biosynthesis. J. Cell Biol. 183 1213– 1221. 10.1083/jcb.200806048 19114592 PMC2606970 · DOI
  78. Lai L. Wang M. Martin O. J. Leone T. C. Vega R. B. Han X. (2014). A role for peroxisome proliferator-activated receptor gamma coactivator 1 (PGC-1) in the regulation of cardiac mitochondrial phospholipid biosynthesis. J. Biol. Chem. 289 2250– 2259. 10.1074/jbc.M113.523654 24337569 PMC3900969 · DOI
  79. Laurinyecz B. Peter M. Vedelek V. Kovacs A. L. Juhasz G. Maroy P. (2016). Reduced expression of CDP-DAG synthase changes lipid composition and leads to male sterility in Drosophila. Open Biol. 6: 50169. 10.1098/rsob.150169 26791243 PMC4736822 · DOI
  80. Lee H. C. Inoue T. Sasaki J. Kubo T. Matsuda S. Nakasaki Y. (2012). LPIAT1 regulates arachidonic acid content in phosphatidylinositol and is required for cortical lamination in mice. Mol. Biol. Cell 23 4689– 4700. 10.1091/mbc.E12-09-0673 23097495 PMC3521678 · DOI
  81. Li M. Hou T. Gao T. Lu X. Yang Q. Zhu Q. (2018). p53 cooperates with SIRT6 to regulate cardiolipin de novo biosynthesis. Cell Death Dis. 9: 941. 10.1038/s41419-018-0984-0 30237540 PMC6148051 · DOI
  82. Lilley A. C. Major L. Young S. Stark M. J. Smith T. K. (2014). The essential roles of cytidine diphosphate-diacylglycerol synthase in bloodstream form Trypanosoma brucei. Mol. Microbiol. 92 453– 470. 10.1111/mmi.12553 24533860 PMC4114554 · DOI
  83. Liu C. H. Bollepalli M. K. Long S. V. Asteriti S. Tan J. Brill J. A. (2018). Genetic dissection of the phosphoinositide cycle in Drosophila photoreceptors. J. Cell Sci. 131: jcs214478. 10.1242/jcs.214478 29567856 PMC5963847 · DOI
  84. Liu X. Yin Y. Wu J. Liu Z. (2014). Structure and mechanism of an intramembrane liponucleotide synthetase central for phospholipid biosynthesis. Nat. Commun. 5: 4244. 10.1038/ncomms5244 24968740 PMC4083444 · DOI
  85. Liu Y. Ji Y. Li X. Shui G. Huang X. (2019). Lipid storage regulator CdsA is essential for Drosophila metamorphosis. J. Genet. Genomics 46 231– 234. 10.1016/j.jgg.2019.02.008 31072795 · DOI
  86. Liu Y. Wang W. Shui G. Huang X. (2014). CDP-diacylglycerol synthetase coordinates cell growth and fat storage through phosphatidylinositol metabolism and the insulin pathway. PLoS Genet. 10: e1004172. 10.1371/journal.pgen.1004172 24603715 PMC3945474 · DOI
  87. López-Lara I. M. Geiger O. (2017). Bacterial lipid diversity. Biochim. Biophys. Acta Mol. Cell Biol. Lipids 1862 1287– 1299. 27760387
  88. Lung M. Shulga Y. V. Ivanova P. T. Myers D. S. Milne S. B. Brown H. A. (2009). Diacylglycerol kinase epsilon is selective for both acyl chains of phosphatidic acid or diacylglycerol. J. Biol. Chem. 284 31062– 31073. 10.1074/jbc.M109.050617 19744926 PMC2781506 · DOI
  89. Lykidis A. (2007). Comparative genomics and evolution of eukaryotic phospholipid biosynthesis. Prog. Lipid Res. 46 171– 199. 10.1016/j.plipres.2007.03.003 17512056 · DOI
  90. Lykidis A. Jackson P. D. Rock C. O. Jackowski S. (1997). The role of CDP-diacylglycerol synthase and phosphatidylinositol synthase activity levels in the regulation of cellular phosphatidylinositol content. J. Biol. Chem. 272 33402– 33409. 10.1074/jbc.272.52.33402 9407135 · DOI
  91. MacDonald G. Baker R. R. Thompson W. (1975). Selective synthesis of molecular classes of phosphatidic acid, diacylglycerol and phosphatidylinositol in rat brain. J. Neurochem. 24 655– 661. 10.1111/j.1471-4159.1975.tb11658.x 1123618 · DOI
  92. Maguire J. J. Tyurina Y. Y. Mohammadyani D. Kapralov A. A. Anthonymuthu T. S. Qu F. (2017). Known unknowns of cardiolipin signaling: the best is yet to come. Biochim. Biophys. Acta Mol. Cell Biol. Lipids 1862 8– 24. 10.1016/j.bbalip.2016.08.001 27498292 PMC5323096 · DOI
  93. Maillet M. van Berlo J. H. Molkentin J. D. (2013). Molecular basis of physiological heart growth: fundamental concepts and new players. Nat. Rev. Mol. Cell Biol. 14 38– 48. 10.1038/nrm3495 23258295 PMC4416212 · DOI · Paper page
  94. Martin D. Gannoun-Zaki L. Bonnefoy S. Eldin P. Wengelnik K. Vial H. (2000). Characterization of Plasmodium falciparum CDP-diacylglycerol synthase, a proteolytically cleaved enzyme. Mol. Biochem. Parasitol. 110 93– 105. 10.1016/s0166-6851(00)00260-7 10989148 · DOI
  95. Martin-Belmonte F. Mostov K. (2007). Phosphoinsositides cotrol epithelial development. Cell Cycle 6 1957– 1961. 17712229
  96. Mejia E. M. Nguyen H. Hatch G. M. (2014). Mammalian cardiolipin biosynthesis. Chem. Phys. Lipids 179 11– 16. 10.1016/j.chemphyslip.2013.10.001 24144810 · DOI
  97. Mercade A. Sanchez A. Folch J. M. (2007). Characterization and physical mapping of the porcine CDS1 and CDS2 genes. Anim. Biotechnol. 18 23– 35. 17364441
  98. Mérida I. Andrada E. Gharbi S. I. Ávila-Flores A. (2015). Redundant and specialized roles for diacylglycerol kinases α and ζ in the control of T cell functions. Sci. Signal. 8 re6. 10.1126/scisignal.aaa0974 25921290 · DOI
  99. Michell R. H. (1975). Inositol phospholipids in cell surface receptor function. Biochim. Biophys. Acta 415 81– 147. 10.1016/0304-4157(75)90017-9 164246 · DOI
  100. Michell R. H. (2018). Do inositol supplements enhance phosphatidylinositol supply and thus support endoplasmic reticulum function? Br. J. Nutr. 120 301– 316. 10.1017/S0007114518000946 29859544 · DOI
  101. Mishra N. N. Tran T. T. Seepersaud R. Garcia-de-la-Maria C. Faull K. Yoon A. (2017). Perturbations of phosphatidate cytidylyltransferase (CdsA) mediate daptomycin resistance in Streptococcus mitis/oralis by a novel mechanism. Antimicrob. Agents Chemother. 61: e02435-16. 10.1128/AAC.02435-16 28115347 PMC5365703 · DOI
  102. Mok A. Y. McDougall G. E. McMurray W. C. (1992). CDP-diacylglycerol synthesis in rat liver mitochondria. FEBS Lett. 312 236– 240. 10.1016/0014-5793(92)80942-a 1330695 · DOI
  103. Mok A. Y. McDougall G. E. McMurray W. C. (1993). Comparative studies of CDP-diacylglycerol synthase in rat liver mitochondria and microsomes. Biochem. Cell Biol. 71 183– 189. 10.1139/o93-029 8398077 · DOI
  104. Moser von Filseck J. Vanni S. Mesmin B. Antonny B. Drin G. (2015). A phosphatidylinositol-4-phosphate powered exchange mechanism to create a lipid gradient between membranes. Nat. Commun. 6: 6671. 10.1038/ncomms7671 25849868 · DOI
  105. Motrich R. D. Castro G. M. Caputto B. L. (2013). Old players with a newly defined function: Fra-1 and c-Fos support growth of human malignant breast tumors by activating membrane biogenesis at the cytoplasm. PLoS One 8: e53211. 10.1371/journal.pone.0053211 23301044 PMC3534677 · DOI
  106. Mujalli A. Chicanne G. Bertrand-Michel J. Viars F. Stephens L. Hawkins P. (2018). Profiling of phosphoinositide molecular species in human and mouse platelets identifies new species increasing following stimulation. Biochim. Biophys. Acta 1863 1121– 1131. 10.1016/j.bbalip.2018.06.009 29902570 · DOI
  107. Müller A. Wenzel M. Strahl H. Grein F. Saaki T. N. V. Kohl B. (2016). Daptomycin inhibits cell envelope synthesis by interfering with fluid membrane microdomains. Proc. Natl. Acad. Sci. U.S.A. 113 E7077– E7086. 10.1073/pnas.1611173113 27791134 PMC5111643 · DOI
  108. Murley A. Sarsam R. D. Toulmay A. Yamada J. Prinz W. A. Nunnari J. (2015). Ltc1 is an ER-localized sterol transporter and a component of ER-mitochondria and ER-vacuole contacts. J. Cell Biol. 209 539– 548. 10.1083/jcb.201502033 25987606 PMC4442815 · DOI
  109. Murley A. Yamada J. Niles B. J. Toulmay A. Prinz W. A. Powers T. (2017). Sterol transporters at membrane contact sites regulate TORC1 and TORC2 signaling. J. Cell Biol. 216 2679– 2689. 10.1083/jcb.201610032 28774891 PMC5584152 · DOI
  110. Naguib A. Bencze G. Engle D. D. Chio I. I. Herzka T. Watrud K. (2015). p53 mutations change phosphatidylinositol acyl chain composition. Cell Rep. 10 8– 19. 10.1016/j.celrep.2014.12.010 25543136 PMC4287966 · DOI
  111. Nakagawa Y. Rustow B. Rabe H. Kunze D. Waku K. (1989). The de novo synthesis of molecular species of phosphatidylinositol from endogenously labeled CDP diacylglycerol in alveolar macrophage microsomes. Arch. Biochem. Biophys. 268 559– 566. 10.1016/0003-9861(89)90323-8 2913948 · DOI
  112. Nakano T. Matsui H. Tanaka T. Hozumi Y. Iseki K. Kawamae K. (2016). Arachidonoyl-specific diacylglycerol kinase ε and the endoplasmic reticulum. Front. Cell Dev. Biol. 4: 132 10.3389/fcell.2016.00132 PMC5114243 27917381 · DOI
  113. Niizeki T. Takeishi Y. Kitahara T. Arimoto T. Koyama Y. Goto K. (2008). Diacylglycerol kinase zeta rescues G alpha q-induced heart failure in transgenic mice. Circ. J. 72 309– 317. 10.1253/circj.72.309 18219172 · DOI
  114. Nishiyama K. Maeda M. Yanagisawa K. Nagase R. Komura H. Iwashita T. (2012). MPIase is a glycolipozyme essential for membrane protein integration. Nat. Commun. 3: 1260. 10.1038/ncomms2267 23232390 PMC3535364 · DOI
  115. Osman C. Haag M. Wieland F. T. Brugger B. Langer T. (2010). A mitochondrial phosphatase required for cardiolipin biosynthesis: the PGP phosphatase Gep4. EMBO J. 29 1976– 1987. 10.1038/emboj.2010.98 20485265 PMC2892375 · DOI
  116. Pan W. Pham V. N. Stratman A. N. Castranova D. Kamei M. Kidd K. R. (2012). CDP-diacylglycerol synthetase-controlled phosphoinositide availability limits VEGFA signaling and vascular morphogenesis. Blood 120 489– 498. 10.1182/blood-2012-02-408328 22649102 PMC3398756 · DOI
  117. Parsons J. B. Rock C. O. (2013). Bacterial lipids: metabolism and membrane homeostasis. Prog. Lipid Res. 52 249– 276. 10.1016/j.plipres.2013.02.002 23500459 PMC3665635 · DOI
  118. Patten I. S. Arany Z. (2012). PGC-1 coactivators in the cardiovascular system. Trends Endocrinol. Metab. 23 90– 97. 10.1016/j.tem.2011.09.007 22047951 · DOI
  119. Pekarsky Y. Croce C. M. (2019). Noncoding RNA genes in cancer pathogenesis. Adv. Biol. Regul. 71 219– 223. 10.1016/j.jbior.2018.12.002 30611710 PMC6800108 · DOI
  120. Pettitt T. R. Martin A. Horton T. Liossis C. Lord J. M. Wakelam M. J. (1997). Diacylglycerol and phosphatidate generated by phospholipases C and D, respectively, have distinct fatty acid compositions and functions. Phospholipase D-derived diacylglycerol does not activate protein kinase C in porcine aortic endothelial cells. J. Biol. Chem. 272 17354– 17359. 10.1074/jbc.272.28.17354 9211874 · DOI
  121. Prescott S. M. Majerus P. W. (1981). The fatty acid composition of phosphatidylinositol from thrombin- stimulated human platelets. J. Biol. Chem. 256 579– 582. 7451460
  122. Qi Y. Kapterian T. S. Du X. Ma Q. Fei W. Zhang Y. (2016). CDP-diacylglycerol synthases regulate the growth of lipid droplets and adipocyte development. J. Lipid Res. 57 767– 780. 10.1194/jlr.M060574 26946540 PMC4847625 · DOI
  123. Racca A. C. Prucca C. G. Caputto B. L. (2019). Fra-1 and c-Fos N-terminal deletion mutants impair breast tumor cell proliferation by blocking lipid synthesis activation. Front. Oncol. 9: 544. 10.3389/fonc.2019.00544 31275861 PMC6593343 · DOI
  124. Raghu P. Coessens E. Manifava M. Georgiev P. Pettitt T. Wood E. (2009). Rhabdomere biogenesis in Drosophila photoreceptors is acutely sensitive to phosphatidic acid levels. J. Cell Biol. 185 129– 145. 10.1083/jcb.200807027 19349583 PMC2700502 · DOI
  125. Raghu P. Joseph A. Krishnan H. Singh P. Saha S. (2019). Phosphoinositides: regulators of nervous system function in health and disease. Front. Mol. Neurosci. 12: 208. 10.3389/fnmol.2019.00208 31507376 PMC6716428 · DOI
  126. Ren S. Caforio A. Yang Q. Sun B. Yu F. Zhu X. (2017). Structural and mechanistic insights into the biosynthesis of CDP-archaeol in membranes. Cell Res. 27 1378– 1391. 10.1038/cr.2017.122 28961231 PMC5674157 · DOI
  127. Robinson C. V. Rohacs T. Hansen S. B. (2019). Tools for understanding nanoscale lipid regulation of ion channels. Trends Biochem. Sci. 44 795– 806. 10.1016/j.tibs.2019.04.001 31060927 PMC6729126 · DOI · Paper page
  128. Rohit S. Aniruddha P. Padinjat R. Sandeep K. (2018). Evidence of sinks and sources in the phospholipase C−activated PIP2 cycle. FEBS Lett. 592 962– 972. 10.1002/1873-3468.12998 29427502 · DOI
  129. Romanauska A. Kohler A. (2018). The inner nuclear membrane is a metabolically active territory that generates nuclear lipid droplets. Cell 174 700– 715.e18. 10.1016/j.cell.2018.05.047 29937227 PMC6371920 · DOI
  130. Saito S. Goto K. Tonosaki A. Kondo H. (1997). Gene cloning and characterization of CDP-diacylglycerol synthase from rat brain. J. Biol. Chem. 272 9503– 9509. 10.1074/jbc.272.14.9503 9083091 · DOI
  131. Sakane F. Mizuno S. Takahashi D. Sakai H. (2018). Where do substrates of diacylglycerol kinases come from? Diacylglycerol kinases utilize diacylglycerol species supplied from phosphatidylinositol turnover-independent pathways. Adv. Biol. Regul. 67 101– 108. 10.1016/j.jbior.2017.09.003 28918129 · DOI
  132. Sanjuan M. A. Jones D. R. Izquierdo M. Merida I. (2001). Role of diacylglycerol kinase alpha in the attenuation of receptor signaling. J. Cell Biol. 153 207– 220. 10.1083/jcb.153.1.207 11285286 PMC2185527 · DOI
  133. Sato N. Hagio M. Wada H. Tsuzuki M. (2000). Requirement of phosphatidylglycerol for photosynthetic function in thylakoid membranes. Proc. Natl. Acad. Sci. U.S.A. 97 10655– 10660. 10.1073/pnas.97.19.10655 10984546 PMC27080 · DOI
  134. Sato R. Sawasato K. Nishiyama K. I. (2019). YnbB is a CdsA paralogue dedicated to biosynthesis of glycolipid MPIase involved in membrane protein integration. Biochem. Biophys. Res. Commun. 510 636– 642. 10.1016/j.bbrc.2019.01.145 30739787 · DOI
  135. Sawasato K. Sato R. Nishikawa H. Iimura N. Kamemoto Y. Fujikawa K. (2019). CdsA is involved in biosynthesis of glycolipid MPIase essential for membrane protein integration in vivo. Sci. Rep. 9: 1372. 10.1038/s41598-018-37809-8 30718729 PMC6362211 · DOI
  136. Schlame M. Greenberg M. L. (2017). Biosynthesis, remodeling and turnover of mitochondrial cardiolipin. Biochim. Biophys. Acta Mol. Cell Biol. Lipids 1862 3– 7. 10.1016/j.bbalip.2016.08.010 27556952 PMC5125896 · DOI
  137. Serricchio M. Vissa A. Kim P. K. Yip C. M. McQuibban G. A. (2018). Cardiolipin synthesizing enzymes form a complex that interacts with cardiolipin-dependent membrane organizing proteins. Biochim. Biophys. Acta Mol. Cell Biol. Lipids 1863 447– 457. 10.1016/j.bbalip.2018.01.007 29343430 · DOI
  138. Shastri S. Zeeman A. M. Berry L. Verburgh R. J. Braun-Breton C. Thomas A. W. (2010). Plasmodium CDP-DAG synthase: an atypical gene with an essential N-terminal extension. Int. J. Parasitol. 40 1257– 1268. 10.1016/j.ijpara.2010.03.006 20385136 · DOI
  139. Shen H. Dowhan W. (1997). Regulation of phospholipid biosynthetic enzymes by the level of CDP-diacylglycerol synthase activity. J. Biol. Chem. 272 11215– 11220. 10.1074/jbc.272.17.11215 9111022 · DOI
  140. Shen H. Heacock P. N. Clancey C. J. Dowhan W. (1996). The CDS1 gene encoding CDP-diacylglycerol synthase in Saccharomyces cerevisiae is essential for cell growth. J. Biol. Chem. 271 789– 795. 10.1074/jbc.271.2.789 8557688 · DOI
  141. Shewan A. Eastburn D. J. Mostov K. (2011). Phosphoinositides in cell architecture. Cold Spring Harb. Perspect. Biol. 3: a004796. 10.1101/cshperspect.a004796 21576256 PMC3140688 · DOI
  142. Shulga Y. V. Topham M. K. Epand R. M. (2011). Regulation and functions of diacylglycerol kinases. Chem. Rev. 111 6186– 6208. 10.1021/cr1004106 21800853 · DOI
  143. Singal T. Dhalla N. S. Tappia P. S. (2009). Regulation of c-Fos and c-Jun gene expression by phospholipase C activity in adult cardiomyocytes. Mol. Cell. Biochem. 327 229– 239. 10.1007/s11010-009-0061-1 19225867 · DOI
  144. Sparrow C. P. Raetz C. R. (1985). Purification and properties of the membrane-bound CDP-diglyceride synthetase from Escherichia coli. J. Biol. Chem. 260 12084– 12091. 2995359
  145. Takeishi Y. Goto K. Kubota I. (2007). Role of diacylglycerol kinase in cellular regulatory processes: a new regulator for cardiomyocyte hypertrophy. Pharmacol. Ther. 115 352– 359. 10.1016/j.pharmthera.2007.04.010 17659347 · DOI
  146. Tamura Y. Harada Y. Nishikawa S. I. Yamano K. Kamiya M. Shiota T. (2013). Tam41 is a CDP-diacylglycerol synthase required for cardiolipin biosynthesis in mitochondria. Cell Metab. 17 1– 10. 23623749 PMC3654088
  147. Tamura Y. Harada Y. Yamano K. Watanabe K. Ishikawa D. Ohshima C. (2006). Identification of Tam41 maintaining integrity of the TIM23 protein translocator complex in mitochondria. J. Cell Biol. 174 631– 637. 10.1083/jcb.200603087 16943180 PMC2064306 · DOI
  148. Tomova C. Humbel B. M. Geerts W. J. Entzeroth R. Holthuis J. C. Verkleij A. J. (2009). Membrane contact sites between apicoplast and ER in Toxoplasma gondii revealed by electron tomography. Traffic 10 1471– 1480. 10.1111/j.1600-0854.2009.00954.x 19602198 · DOI
  149. Traynor-Kaplan A. Kruse M. Dickson E. J. Dai G. Vivas O. Yu H. (2017). Fatty-acyl chain profiles of cellular phosphoinositides. Biochim. Biophys. Acta Mol. Cell Biol. Lipids 1862 513– 522. 10.1016/j.bbalip.2017.02.002 28189644 PMC5392126 · DOI
  150. Vanhaesebroeck B. Stephens L. Hawkins P. (2012). PI3K signalling: the path to discovery and understanding. Nat. Rev. Mol. Cell Biol. 13 195– 203. 10.1038/nrm3290 22358332 · DOI
  151. Volta M. Bulfone A. Gattuso C. Rossi E. Mariani M. Consalez G. G. (1999). Identification and characterization of CDS2, a mammalian homolog of the Drosophila CDP-diacylglycerol synthase gene. Genomics 55 68– 77. 10.1006/geno.1998.5610 9889000 · DOI
  152. Weeks R. Dowhan W. Shen H. Balantac N. Meengs B. Nudelman E. (1997). Isolation and expression of an isoform of human CDP-diacylglycerol synthase cDNA. DNA Cell Biol. 16 281– 289. 10.1089/dna.1997.16.281 9115637 · DOI
  153. Wong L. H. Gatta A. T. Levine T. P. (2019). Lipid transfer proteins: the lipid commute via shuttles, bridges and tubes. Nat. Rev. Mol. Cell Biol. 20 85– 101. 10.1038/s41580-018-0071-5 30337668 · DOI
  154. Wu L. Niemeyer B. Colley N. Socolich M. Zuker C. S. (1995). Regulation of PLC-mediated signalling in vivo by CDP-diacylglycerol synthase. Nature 373 216– 222. 10.1038/373216a0 7816135 · DOI
  155. Xu Y. Mak H. Y. Lukmantara I. Li Y. E. Hoehn K. L. Huang X. (2019). CDP-DAG Synthase 1 and 2 regulate lipid droplet growth through distinct mechanisms. J. Biol. Chem. 294 16740– 16755. 10.1074/jbc.RA119.009992 31548309 PMC6851299 · DOI
  156. Yan X. Liang H. Deng T. Zhu K. Zhang S. Wang N. (2013). The identification of novel targets of miR-16 and characterization of their biological functions in cancer cells. Mol. Cancer 12: 92. 10.1186/1476-4598-12-92 23941513 PMC3751425 · DOI
  157. Yang R. M. Tao J. Zhan M. Yuan H. Wang H. H. Chen S. J. (2019). TAMM41 is required for heart valve differentiation via regulation of PINK-PARK2 dependent mitophagy. Cell Death Differ. 26 2430– 2446. 10.1038/s41418-019-0311-z 30824836 PMC6888875 · DOI
  158. Yang Y. Lee M. Fairn G. D. (2018). Phospholipid subcellular localization and dynamics. J. Biol. Chem. 293 6230– 6240. 10.1074/jbc.r117.000582 29588369 PMC5925819 · DOI
  159. Yen H. Y. Hoi K. K. Liko I. Hedger G. Horrell M. R. Song W. (2018). PtdIns(4,5)P2 stabilizes active states of GPCRs and enhances selectivity of G-protein coupling. Nature 559 423– 427. 10.1038/s41586-018-0325-6 29995853 PMC6059376 · DOI · Paper page
  160. Zhang J. Guan Z. Murphy A. N. Wiley S. E. Perkins G. A. Worby C. A. (2011). Mitochondrial phosphatase PTPMT1 is essential for cardiolipin biosynthesis. Cell Metab. 13 690– 700. 10.1016/j.cmet.2011.04.007 21641550 PMC3119201 · DOI
  161. Zhao W. Cao L. Ying H. Zhang W. Li D. Zhu X. (2019). Endothelial CDS2 deficiency causes VEGFA-mediated vascular regression and tumor inhibition. Cell Res. 29 895– 910. 10.1038/s41422-019-0229-5 31501519 PMC6889172 · DOI
  162. Zhou Y. Peisker H. Weth A. Baumgartner W. Dormann P. Frentzen M. (2013). Extraplastidial cytidinediphosphate diacylglycerol synthase activity is required for vegetative development in Arabidopsis thaliana. Plant J. 75 867– 879. 10.1111/tpj.12248 23711240 · DOI

Cited by

Sorted by citations

Authors
Blunsom, N. J., & Cockcroft, S.
Affiliations
University College London (GB)
Corresponding author
Cockcroft, Shamshad
ORCID
Cockcroft, Shamshad
Venue
Frontiers in Cell and Developmental Biology
Publisher
Frontiers Media SA
Published
2020-02-07
Volume
8
Pages
63-63
ISSN
2296-634X (ISSN-L)
DOI
10.3389/fcell.2020.00063
PMC
PMC7018664
OpenAlex
W3004557677
Cited by
123
References
4
Citations by year
2026: 21 · 2025: 24 · 2024: 22 · 2023: 23 · 2022: 11 · 2021: 14 · 2020: 8
FWCI
1.37
Type
journal article
Language
en
Open access
Licence
Locations
  • Frontiers in Cell and Developmental Biology (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • UCL Discovery (University College London) (submittedVersion)
Funders
British Heart Foundation
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sphingolipid Metabolism and Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
Keywords
CDP-diacylglycerol synthase, phosphatidylinositol synthesis, cardiolipin synthesis, phosphatidic acid, phosphatidylglycerol synthesis, phospholipase C signaling, endoplasmic reticulum, mitochondrial cardiolipin

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