Chemical proteomics reveals bolinaquinone as a clathrin-mediated endocytosis inhibitor - PubMed (original) (raw)

doi: 10.1039/c0mb00126k. Epub 2010 Nov 8.

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• PMID: 21060934
• DOI: 10.1039/c0mb00126k

Chemical proteomics reveals bolinaquinone as a clathrin-mediated endocytosis inhibitor

Luigi Margarucci et al. Mol Biosyst. 2011 Feb.

Abstract

The emerging field of mass spectrometry-based chemical proteomics provides a powerful instrument in the target discovery of bioactive small-molecules, such as drugs or natural products. The identification of their macromolecular targets is required for a comprehensive understanding of their bio-pharmacological role and for unraveling their mechanism of action. We report the application of a chemical proteomics approach to the analysis of the cellular interactome of the marine metabolite bolinaquinone (BLQ). BLQ was linked to an opportune α,ω-diamino polyethylene glycol chain and then immobilized on a matrix support. The modified beads were then used as a bait for fishing the potential partners of BLQ in a THP-1 macrophage cell lysate. Surprisingly, we identified clathrin, a protein involved in the cell internalization of proteins, viruses and other biologically relevant macromolecules, as a specific and major BLQ partner. In addition, we verified the biochemical role of BLQ testing its ability to inhibit the clathrin-mediated endocytosis of albumin. This finding indicates BLQ as a new biotechnological tool for cell endocytosis studies and paves the way to further investigation on its potential role in modulating internalization process.

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