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Live-cell lipid biochemistry reveals a role of diacylglycerol side-chain composition for cellular lipid dynamics and protein affinities.

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Schuhmacher,  Milena
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Wagner,  Nicolai
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Schuhmacher,  Jan Simon
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Lohmann,  Annett
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Henry,  Ian
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Shevchenko,  Andrej
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Nadler,  André
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Citation

Schuhmacher, M., Grasskamp, A. T., Barahtjan, P., Wagner, N., Lombardot, B., Schuhmacher, J. S., et al. (2020). Live-cell lipid biochemistry reveals a role of diacylglycerol side-chain composition for cellular lipid dynamics and protein affinities. Proceedings of the National Academy of Sciences of the United States of America, 117(14), 7729-7738. doi:10.1073/pnas.1912684117.


Cite as: https://hdl.handle.net/21.11116/0000-0008-A2E4-F
Abstract
Every cell produces thousands of distinct lipid species, but insight into how lipid chemical diversity contributes to biological signaling is lacking, particularly because of a scarcity of methods for quantitatively studying lipid function in living cells. Using the example of diacylglycerols, prominent second messengers, we here investigate whether lipid chemical diversity can provide a basis for cellular signal specification. We generated photo-caged lipid probes, which allow acute manipulation of distinct diacylglycerol species in the plasma membrane. Combining uncaging experiments with mathematical modeling, we were able to determine binding constants for diacylglycerol-protein interactions, and kinetic parameters for diacylglycerol transbilayer movement and turnover in quantitative live-cell experiments. Strikingly, we find that affinities and kinetics vary by orders of magnitude due to diacylglycerol side-chain composition. These differences are sufficient to explain differential recruitment of diacylglycerol binding proteins and, thus, differing downstream phosphorylation patterns. Our approach represents a generally applicable method for elucidating the biological function of single lipid species on subcellular scales in quantitative live-cell experiments.