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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...

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Autori principali: Haberkant, Per (Autore) , Stein, Frank (Autore) , Höglinger, Doris (Autore) , Gerl, Mathias (Autore) , Brügger, Britta (Autore) , Van Veldhoven, Paul P. (Autore) , Krijgsveld, Jeroen (Autore) , Gavin, Anne-Claude (Autore) , Schultz, Carsten (Autore)
Natura: Article (Journal)
Lingua:inglese
Pubblicazione: 2016
In: ACS chemical biology
Year: 2015, Volume: 11, Fascicolo: 1, Pages: 222-230
ISSN:1554-8937
DOI:10.1021/acschembio.5b00810
Accesso online:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1021/acschembio.5b00810
Testo
Note sull'autore: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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Riassunto: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.
Descrizione del documento:Published: November 11, 2015
Gesehen am 02.09.2020
Descrizione fisica:Online Resource
ISSN:1554-8937
DOI:10.1021/acschembio.5b00810

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