Buchumschlag

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...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Hauptverfasser: Haberkant, Per (VerfasserIn) , Stein, Frank (VerfasserIn) , Höglinger, Doris (VerfasserIn) , Gerl, Mathias (VerfasserIn) , Brügger, Britta (VerfasserIn) , Van Veldhoven, Paul P. (VerfasserIn) , Krijgsveld, Jeroen (VerfasserIn) , Gavin, Anne-Claude (VerfasserIn) , Schultz, Carsten (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 2016
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
Volltext
Verfasserangaben:Per Haberkant, Frank Stein, Doris Höglinger, Mathias J. Gerl, Britta Brügger, Paul P. Van Veldhoven, Jeroen Krijgsveld, Anne-Claude Gavin, and Carsten Schultz
Beschreibung
Zusammenfassung: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.
Beschreibung:Published: November 11, 2015
Gesehen am 02.09.2020
Beschreibung:Online Resource
ISSN:1554-8937
DOI:10.1021/acschembio.5b00810

Ähnliche Einträge