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Phosphatidic acid, a key intermediate in lipid metabolism
Open accessAbstract
Phosphatidic acid (PtdOH) is a key intermediate in glycerolipid biosynthesis. Two different pathways are known for de novo formation of this compound, namely (a) the Gro3P (glycerol 3-phosphate) pathway, and (b) the GrnP (dihydroxyacetone phosphate) pathway. Whereas the former route of PtdOH synthesis is present in bacteria and all types of eukaryotes, the GrnP pathway is restricted to yeast and mammalian cells. In this review article, we describe the enzymes catalyzing de novo formation of PtdOH, their properties and their occurrence in different cell types and organelles. Much attention has recently been paid to the subcellular localization of enzymes involved in the biosynthesis of PtdOH. In all eukaryotic cells, microsomes (ER) harbour the complete set of enzymes catalyzing these pathways and are thus the usual organelle for PtdOH formation. In contrast, the contribution of mitochondria to PtdOH synthesis is restricted to certain enzymes and depends on the cell type. In addition, chloroplasts of plants, lipid particles of the yeast, and peroxisomes of mammalian cells are significantly involved in PtdOH biosynthesis. Redundant systems of acyltransferases, the interplay of organelles, regulation of the pathway on the compartmental level, and finally the contribution of alternative pathways (phosphorylation of diacylglycerol and cleavage of phospholipids by phospholipases) to PtdOH biosynthesis appear to be required for the balanced formation of this important lipid intermediate. Dysfunction of enzymes involved in PtdOH synthesis can result in severe defects of various cellular processes. In this context, the possible physiological role(s) of PtdOH and its related metabolites, lysophosphatidic acid and diacylglycerol, will be discussed.
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“Phosphatidic acid (PA) is a precursor for the synthesis of numerous lipids [181].”
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“As such, PA plays a fundamental role in the regulation of cellular metabolism [181].”
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Cites
A novel X-linked gene, G4.5. is responsible for Barth syndrome
Bione, S., D’Adamo, P., Maestrini, E., Gedeon, Á. K., Bolhuis, P. A., & Toniolo, D. (1996) · Nature Genetics · doi:10.1038/ng0496-385 · Cited by 753
Zinser, E., Sperka-Gottlieb, C. D. M., Fasch, E.-V., Kohlwein, S. D., Paltauf, F., & Daum, G. (1991) · Journal of Bacteriology · doi:10.1128/jb.173.6.2026-2034.1991 · Cited by 705
Self-citationBarth, P. G., Scholte, H. R., BERDEN, J. A., Moorsel, J. M. V. D. K., Luyt‐Houwen, I. E. M., Veer-Korthof, E. T. V., van der Harten, J. J., & Sobotka, M. A. (1983) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(83)90209-5 · Cited by 702
Lysophosphatidic Acid, a Multifunctional Phospholipid Messenger
Moolenaar, W. H. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.22.12949 · Cited by 584
Kunau, W. H. (1995) · Progress in Lipid Research · doi:10.1016/0163-7827(95)00011-9 · Cited by 516
Muoio, D. M., Seefeld, K. J., Witters, L. A., & Coleman, R. (1999) · Biochemical Journal · doi:10.1042/bj3380783 · Cited by 429
van den BOSCH, H. (1974) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.43.070174.001331 · Cited by 418
EUKARYOTIC PHOSPHOLIPID BIOSYNTHESIS
Kent, C. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.001531 · Cited by 381
GLYCEROLIPID BIOSYNTHESIS IN PEROXISOMES VIA THE ACYL DIHYDROXYACETONE PHOSPHATE PATHWAY*
Hajra, A. K., & Bishop, J. E. (1982) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1982.tb21415.x · Cited by 340
Zou, J., Katavić, V., Giblin, E. M., Barton, D. L., MacKenzie, S. L., Keller, W. A., Hu, X., & Taylor, D. C. (1997) · The Plant Cell · doi:10.1105/tpc.9.6.909 · Cited by 308
Research works printed but not linked: 5
- Bell R.M., 1983, The Enzymes, 87
- Gurr M.I., 1980, The Biochemistry of Plants, 205
- Lightner V.A., 1980, Membrane phospholipid synthesis in, Escherichia coli. J. Biol. Chem., 255, 9413
- Shiao Y.‐J., 1995, Regulation of mitochondrial and microsomal phospholipid synthesis by liver fatty acid‐binding protein., J. Biol. Chem., 267, 14353
- Schutgens R.B.H., 1996, Emery and Rimoin’s Principals and Practice of Medical Genetics, 2131
Cited by
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Items 301–400 of 403
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Tayeh, C., Randoux, B., Laruelle, F., Facon, N., & Reignault, P. L. (2016) · Functional Plant Biology · doi:10.1071/fp15347 · Cited by 5
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Sadre, R., & Frentzen, M. (2009) · Advances in photosynthesis and respiration · doi:10.1007/978-90-481-2863-1_4 · Cited by 5
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Zhu, K., Zhang, Y., Ma, J., Zhang, T., Lei, H., Zhao, W., Xu, H., & Li, M. (2025) · Planta · doi:10.1007/s00425-025-04751-9 · Cited by 4
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Label free detection of phospholipids by infrared absorption spectroscopy
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Patel, N., Pirani, K. A., Zhu, T., Kit, M. C. S., Lee, S., Chen, D. G., & Zufferey, R. (2016) · Journal of Eukaryotic Microbiology · doi:10.1111/jeu.12309 · Cited by 4
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Lipids and signal transduction in the nucleus.
Dygas, A., & Barańska, J. (2001) · Acta Biochimica Polonica · doi:10.18388/abp.2001_3937 · Cited by 4
Frimmelova, M., Toman, R., Pompach, P., & Škultéty, Ľ. (2016) · Acta Virologica · doi:10.4149/av_2016_01_27 · Cited by 4
Drapal, M., Wheeler, P. R., & Fraser, P. D. (2018) · FEMS Microbiology Letters · doi:10.1093/femsle/fny153 · Cited by 4
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Miyazawa, D., Ikemoto, A., Fujii, Y. R., & Okuyama, H. (2003) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s1388-1981(02)00319-0 · Cited by 3
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Preferential electrostatic interactions of phosphatidic acid with arginines
Thomas, N., Combs, W., Mandadapu, K. K., & Agrawal, A. (2024) · Soft Matter · doi:10.1039/d4sm00088a · Cited by 2
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Steinmetz, T. D., Thomas, J., Reimann, L., Himmelreich, A.-K., Schulz, S. R., Golombek, F., Castiglione, K., Jäck, H., Brodesser, S., Warscheid, B., et al. (2024) · Journal of Proteome Research · doi:10.1021/acs.jproteome.3c00713 · Cited by 2
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Lipid-Dependent Membrane Remodelling in Protein Trafficking
Chandra, P., & Ktistakis, N. T. (2009) · Springer eBooks · doi:10.1007/978-0-387-93877-6_11 · Cited by 2
Identification of Lipid-Binding Effectors
Kale, S. D., & Tyler, B. M. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-501-5_24 · Cited by 2
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Mérida, I., Carrasco, S., & Ávila‐Flores, A. (2010) · Humana Press eBooks · doi:10.1007/978-1-60761-543-9_4 · Cited by 2
Vijayaraj, P., Jayaraja, S., & Nachiappan, V. (2011) · Toxicological & Environmental Chemistry Reviews · doi:10.1080/02772248.2011.556638 · Cited by 2
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So, V., Wu, J., Traynor‐Kaplan, A., Choy, C. H., Epand, R. M., Botelho, R. J., & Lemaire, M. J. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/633867 · Cited by 2
Urbanczyk, S., Baris, O. R., Hofmann, J., Golombek, F., Castiglione, K., Meng, X., Bözec, A., Mougiakakos, D., Schulz, S. R., Schuh, W., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.14.426649 · Cited by 2
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Maxim, R. M., Romanciuc, F., Crişan, N., Andraș, I., & Socaciu, C. (2015) · Bulletin of University of Agricultural Sciences and Veterinary Medicine Cluj-Napoca Animal Science and Biotechnologies · doi:10.15835/buasvmcn-asb:11652 · Cited by 1
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Yang, H., Liu, J., Huangfu, M., Zhao, H., Li, Y., Zhou, Y., Wang, A., Chen, R.-W., & Li, X. (2025) · Marine Environmental Research · doi:10.1016/j.marenvres.2025.107370 · Cited by 1
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Stewart, G. (2007) · ScholarWorks @ The University of New Orleans (The University of New Orleans)
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Inokuchi, H., Mizuno‐Kamiya, M., & Fujita, A. (2001) · Japanese Journal of Oral Biology · doi:10.2330/joralbiosci1965.43.666
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Engmann, T. (2009) · Kölner Universitäts PublikationsServer (Universität zu Köln)
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Jaiswal, S. R. (2010) · CLOK (University of Central Lancashire)
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Tyagi, M. G., Singh, D., Nirmala, J., Amil, M., & Yadav, S. S. (2019) · Journal of Biomedical and Pharmaceutical Research · doi:10.32553/jbpr.v8i1.572
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Rawlins (2018) · Digital Repository Service (Northeastern University) · doi:10.17760/d20292916
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Metadata
- Authors
- Athenstaedt, K., & Daum, G.
- Affiliations
- University of Graz (AT)
- ORCID
- Athenstaedt, Karin
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 1999-11-15
- Volume
- 266
- Issue
- 1
- Pages
- 1-16
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W2001355405
- Cited by
- 403
- References
- 112
- Citations by year
- 2026: 10 · 2025: 14 · 2024: 15 · 2023: 13 · 2022: 10 · 2021: 18 · 2020: 16 · 2019: 31 · 2018: 16 · 2017: 18 · 2016: 25 · 2015: 23 · 2014: 17 · 2013: 22 · 2012: 15
- FWCI
- 1.04
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- European Journal of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
- Keywords
- phosphatidic acid, glycerolipid biosynthesis, subcellular localization, endoplasmic reticulum, mitochondria, chloroplasts, peroxisomes, acyltransferase, lysophosphatidic acid, diacylglycerol, lipid metabolism
- MeSH terms
- Acyltransferases, Animals, Dihydroxyacetone Phosphate, Glycerophosphates, Lysophospholipids, Mammals, Microsomes, Phenotype, Phosphatidic Acids, Prokaryotic Cells, Organelles, Lipid Metabolism
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