ReviewBiology2026
The Biological Significance of Calmodulin Binding to Lipids.
Review in Biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
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0 citing papers in PubMed.
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Authors and funding
1 author.
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Abstract
In addition to binding to and regulating over 400 different proteins, calmodulin (CaM) also binds to lipids. Binding occurs to the prenylated tails of various small GTPases, to specific lipids in biological membranes and to free lipids in the cytoplasm. Here, CaM binding to Rac1, RalA, and KRAS4b is covered, emphasizing its importance in protein translocation from the cell membrane to the cytosol and its resultant impact on cell signaling. Binding phosphatidylserine and phosphatidylethanolamine in membranes not only leads to the tethering of CaM, but also to the disruption of lipid bilayers. Binding to sphingolipids also occurs, an event that acts as a competitive inhibitor of CaM function. The mechanism through which CaM binds to lipids is also examined. In total, the current state of affairs regarding calcium-dependent CaM-lipid binding is reviewed, including potential therapeutic uses, setting the stage for future work on this important biological event.
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