Journal
MOLECULAR SYSTEMS BIOLOGY
Volume 6, Issue -, Pages -Publisher
WILEY
DOI: 10.1038/msb.2010.87
Keywords
interactome; lipid-array; network; pleckstrin homology domains; sphingolipids
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Funding
- Federal Ministry of Education and Research (BMBF) [01GS0865]
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Protein-metabolite networks are central to biological systems, but are incompletely understood. Here, we report a screen to catalog protein-lipid interactions in yeast. We used arrays of 56 metabolites to measure lipid-binding fingerprints of 172 proteins, including 91 with predicted lipid-binding domains. We identified 530 protein-lipid associations, the majority of which are novel. To show the data set's biological value, we studied further several novel interactions with sphingolipids, a class of conserved bioactive lipids with an elusive mode of action. Integration of live-cell imaging suggests new cellular targets for these molecules, including several with pleckstrin homology (PH) domains. Validated interactions with Slm1, a regulator of actin polarization, show that PH domains can have unexpected lipid-binding specificities and can act as coincidence sensors for both phosphatidylinositol phosphates and phosphorylated sphingolipids. Molecular Systems Biology 6: 430; published online 30 November 2010; doi:10.1038/msb.2010.87
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