The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
Cooperative roles of various membrane phospholipids in the activation of calcium-activated, phospholipid-dependent protein kinase.
Open accessAbstract
Although phosphatidylserine is the sole phospholipid effective for the activation of Ca2+-activated, phospholipid-dependent protein kinase in the presence of a small amount of unsaturated diacylglycerol and micromolar concentrations of Ca2+ (Takai, Y., Kishimoto, A., Kikkawa, U., Mori, T., and Nishizuka, Y. (1979) Biochem. Biophys. Res. Commun. 91, 1218-1224), other species of phospholipids modulate the activation of enzyme considerably. When phosphatidylserine is supplemented with phosphatidylethanolamine, further enhancement of the enzymatic activity is observed. Inversely, the addition of phosphatidylcholine or sphingomyelin markedly diminishes the enzyme activation by phosphatidylserine. Phosphatidylinositol, which serves as the source of unsaturated diacylglycerol, and phosphatidic acid do not show significant effects. Kinetic analysis has indicated that phosphatidylethanolamine enhances the enzyme activation by marked increase in the affinity of enzyme for Ca2+ and also by slight increase in the affinity for phosphatidylserine as well as for unsaturated diacylglycerol without affecting the maximum reaction velocity. Phosphatidylcholine and sphingomyelin diminish the enzyme activation in an uncompetitive manner with respect to Ca2+ and in a competitive manner with respect to both phosphatidylserine and unsaturated diacylglycerol. These results suggest that each species of the various membrane phospholipids plays a specific role with positive or negative cooperativity in the activation of this unique protein kinase.
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“In addition, elevated PS to SM ratio, as in the KO astrocytes, activates protein kinase C by positive co-operativity56.”
From An iPSC-derived astrocyte model of fragile X syndrome exhibits dysregulated cholesterol homeostasis (2023) · cites this paper as [56]
Citations
Cites
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Inositol phospholipids and cell surface receptor function
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A simple method for the preparation of 32P-labelled adenosine triphosphate of high specific activity
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Self-citationden Kamp, J. A. F. O. (1979) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.48.070179.000403 · Cited by 1,262
Calcium-dependent activation of a multifunctional protein kinase by membrane phospholipids.
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Self-citationPhospholipid Methylation and Biological Signal Transmission
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Self-citationTakai, Y., Kishimoto, A., Kikkawa, U., Terutoshi, M. O. R. I., & Nishizuka, Y. (1979) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(79)91197-5 · Cited by 731
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The role of protein kinase C in cell surface signal transduction and tumour promotion
Nishizuka, Y. (1984) · Nature · doi:10.1038/308693a0 · Cited by 7,455
Self-citationStudies and Perspectives of Protein Kinase C
Nishizuka, Y. (1986) · Science · doi:10.1126/science.3014651 · Cited by 5,068
Self-citationCastagna, M., Takai, Y., Kaibuchi, K., Sano, K., Kikkawa, U., & Nishizuka, Y. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34459-4 · Cited by 4,725
Self-citationTurnover of Inositol Phospholipids and Signal Transduction
Nishizuka, Y. (1984) · Science · doi:10.1126/science.6147898 · Cited by 1,614
Self-citationHannun, Y. A., Loomis, C. R., Merrill, A. H., & Bell, R. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)67133-9 · Cited by 1,156
Metadata
- Authors
- Kaibuchi, K., Takai, Y., & Nishizuka, Y.
- Affiliations
- National Institute for Basic Biology (JP)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1981-07
- Volume
- 256
- Issue
- 14
- Pages
- 7146-7149
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W191339276
- Cited by
- 367
- References
- 25
- Citations by year
- 2026: 1 · 2023: 1 · 2021: 1 · 2020: 1 · 2019: 1 · 2018: 1 · 2016: 2 · 2015: 2 · 2014: 1 · 2013: 1 · 2012: 2
- FWCI
- 9.78
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sphingolipid Metabolism and Signaling
- Keywords
- phospholipid-dependent protein kinase, phosphatidylserine, phosphatidylethanolamine, phosphatidylcholine, sphingomyelin, phosphatidylinositol, phosphatidic acid, enzyme activation, calcium affinity, cooperative enzyme kinetics, membrane phospholipids
- MeSH terms
- Animals, Brain, Calcium, Cell Membrane, Enzyme Activation, Kinetics, Membrane Lipids, Phospholipids, Protein Kinases, Structure-Activity Relationship, Rats
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