Scientific article

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

Published inACS Chemical Biology, vol. 11, no. 1, p. 222-230
Publication date2016

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.

  • Humans
  • Molecular Structure
  • Protein Array Analysis
  • Protein Binding
  • Proteomics/methods
  • Reproducibility of Results
  • Sphingolipids/metabolism
  • Sphingosine/analogs & derivatives/chemical synthesis/chemistry
Affiliation Not a UNIGE publication
Citation (ISO format)
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
Main files (1)
Article (Published version)
ISSN of the journal1554-8929

Technical informations

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