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Title

Bifunctional sphingosine for cell-based analysis of protein-sphingolipid interactions

Authors
Haberkant, Per
Stein, Frank
Höglinger, Doris
Gerl, Mathias J
Brügger, Britta
Van Veldhoven, Paul P
Krijgsveld, Jeroen
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Published in ACS Chemical Biology. 2016, vol. 11, no. 1, p. 222-230
Abstract 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.
Keywords HumansMolecular StructureProtein Array AnalysisProtein BindingProteomics/methodsReproducibility of ResultsSphingolipids/metabolismSphingosine/analogs & derivatives/chemical synthesis/chemistry
Identifiers
PMID: 26555438
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Article (Published version) (5.8 MB) - document accessible for UNIGE members only Limited access to UNIGE
Research group Métabolisme des lipides (1001)
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HABERKANT, Per et al. Bifunctional sphingosine for cell-based analysis of protein-sphingolipid interactions. In: ACS Chemical Biology, 2016, vol. 11, n° 1, p. 222-230. doi: 10.1021/acschembio.5b00810 https://archive-ouverte.unige.ch/unige:124754

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Deposited on : 2019-10-22

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