Bifunctional sphingosine for cell-based analysis of protein-sphingolipid interactions
Sphingolipids are essential structural components of cellular membranes and are crucial regulators of cellular processes. While current high-throughput approaches allow for the systematic mapping of interactions of soluble proteins with their lipid-binding partners, photo-cross-linking is the only t...
Gespeichert in:
| Hauptverfasser: | , , , , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
2016
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| In: |
ACS chemical biology
Year: 2015, Jahrgang: 11, Heft: 1, Pages: 222-230 |
| ISSN: | 1554-8937 |
| DOI: | 10.1021/acschembio.5b00810 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1021/acschembio.5b00810
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| Verfasserangaben: | Per Haberkant, Frank Stein, Doris Höglinger, Mathias J. Gerl, Britta Brügger, Paul P. Van Veldhoven, Jeroen Krijgsveld, Anne-Claude Gavin, and Carsten Schultz |
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| 520 | |a Sphingolipids are essential structural components of cellular membranes and are crucial regulators of cellular processes. While current high-throughput approaches allow for the systematic mapping of interactions of soluble proteins with their lipid-binding partners, photo-cross-linking is the only technique that enables for the proteome-wide mapping of integral membrane proteins with their direct lipid environment. Here, we report the synthesis of a photoactivatable and clickable analog of sphingosine (pacSph). When administered to sphingosine-1-phosphate lyase deficient cells, pacSph allows its metabolic fate and the subcellular flux of de novo synthesized sphingolipids to be followed in a time-resolved manner. The chemoproteomic profiling yielded over 180 novel sphingolipid-binding proteins, of which we validated a number, demonstrating the unique value of this technique as a discovery tool. This work provides an important resource for the understanding of the global cellular interplay between sphingolipids and their interacting proteins. | ||
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