In Vivo Profiling and Visualization of Cellular Protein-Lipid Interactions Using Bifunctional Fatty Acids

Bifunctional lipid technology: Cells convert externally added photoactivatable and “clickable” fatty acids into a variety of bifunctional phospholipids that can be covalently linked to their protein‐binding partners by irradiation with UV light. Derivatization of the clickable group with a reporter...

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Published inAngewandte Chemie (International ed.) Vol. 52; no. 14; pp. 4033 - 4038
Main Authors Haberkant, Per, Raijmakers, Reinout, Wildwater, Marjolein, Sachsenheimer, Timo, Brügger, Britta, Maeda, Kenji, Houweling, Martin, Gavin, Anne-Claude, Schultz, Carsten, van Meer, Gerrit, Heck, Albert J. R., Holthuis, Joost C. M.
Format Journal Article
LanguageEnglish
Published Weinheim WILEY-VCH Verlag 02.04.2013
WILEY‐VCH Verlag
Subjects
Animals
cell imaging
CHO Cells
Click Chemistry
Cricetinae
Cricetulus
Fatty Acids - chemical synthesis
Fatty Acids - chemistry
Fatty Acids - metabolism
HeLa Cells
Humans
lipids
Microscopy, Confocal
Phospholipids - chemistry
Phospholipids - metabolism
photoaffinity labeling
Protein Binding
proteins
Proteins - chemistry
Proteins - metabolism
Ultraviolet Rays
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Summary:Bifunctional lipid technology: Cells convert externally added photoactivatable and “clickable” fatty acids into a variety of bifunctional phospholipids that can be covalently linked to their protein‐binding partners by irradiation with UV light. Derivatization of the clickable group with a reporter molecule makes it possible to identify and image the lipid‐bound proteins in situ (see scheme).
Bibliography:ArticleID:ANIE201210178
This work was supported by the Marie Curie Actions COFUND (EMBL Interdisciplinary Postdoc (EIPOD) stipend to P.H.), the Netherlands Proteomics Center (NPC) within the Netherlands Genomics Initiative and an NPC Valorization Voucher (P.H.), the European Union (7th FP Marie-Curie ITN "SPHINGONET" to C.S., A.J.R.H., J.C.M.H.), and the DFG (TRR83 to B.B., C.S.). K.M. was a fellow of the Danish Natural Science Research Council (09-064986/FNU). We thank Y. Horibata, H. Sugimoto, and S. Cockcroft for providing plasmids, C. Versluis for high-resolution mass spectrometra, and H. Vlieg, H. Dijkstra, and T. Klimeck for technical assistance.
ark:/67375/WNG-W0T80QH7-H
DFG
istex:51A9FC18981DFDF1E982A5C902E699F30DD8B5EC
European Union
This work was supported by the Marie Curie Actions COFUND (EMBL Interdisciplinary Postdoc (EIPOD) stipend to P.H.), the Netherlands Proteomics Center (NPC) within the Netherlands Genomics Initiative and an NPC Valorization Voucher (P.H.), the European Union (7th FP Marie‐Curie ITN “SPHINGONET” to C.S., A.J.R.H., J.C.M.H.), and the DFG (TRR83 to B.B., C.S.). K.M. was a fellow of the Danish Natural Science Research Council (09‐064986/FNU). We thank Y. Horibata, H. Sugimoto, and S. Cockcroft for providing plasmids, C. Versluis for high‐resolution mass spectrometra, and H. Vlieg, H. Dijkstra, and T. Klimeck for technical assistance.
ObjectType-Article-1
SourceType-Scholarly Journals-1
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content type line 23
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201210178