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Issue 10, 2010
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Proteome-wide detection of phospholipidprotein interactions in mitochondria by photocrosslinking and click chemistry

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Abstract

Photoactivatable lipid analogues are uniquely suited for the detection of lipidprotein interactions in biological membranes. Based on photocrosslinking, new methodology has been developed for the proteome-wide detection of lipidprotein interactions. Bifunctional lipid analogues containing a tag for click chemistry in addition to the photoactivatable moiety enable the enrichment of the crosslinked proteins that is required for subsequent identification by mass spectrometry. In principle the phospholipid interaction-based membrane protein proteomics approach is applicable to any biomembrane and any lipid. Here, we review the background and the development of the new methodology. Results obtained with photocrosslinking in purified mitochondrial membranes from the yeast Saccharomyces cerevisiae are summarized and future perspectives discussed.

Graphical abstract: Proteome-wide detection of phospholipid–protein interactions in mitochondria by photocrosslinking and click chemistry

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Publication details

The article was received on 12 Feb 2010, accepted on 26 Mar 2010 and first published on 11 Jun 2010


Article type: Review Article
DOI: 10.1039/C003064N
Citation: Mol. BioSyst., 2010,6, 1751-1759
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    Proteome-wide detection of phospholipidprotein interactions in mitochondria by photocrosslinking and click chemistry

    J. Gubbens and A. I. P. M. de Kroon, Mol. BioSyst., 2010, 6, 1751
    DOI: 10.1039/C003064N

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