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Título: | A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae |
Autor: | Gallego, Oriol; Betts, Matthew J.; Gvozdenovic-Jeremic, Jelena; Maeda, Kenji; Matetzki, Christian; Aguilar-Gurrieri, Carmen; Beltrán-Álvarez, Pedro; Bonn, Stefan; Fernández-Tornero, Carlos CSIC ORCID ; Jensen, Lars Juhl; Kuhn, Michael; Trott, Jamie; Rybin, Vladimir; Müller, Christoph W.; Bork, Peer; Kaksonen, Marko; Russell, Robert B.; Gavin, Anne-Claude | Fecha de publicación: | 30-nov-2010 | Editor: | Nature Publishing Group | Citación: | Molecular Systems Biology 6:430(2010) | Resumen: | 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 | Descripción: | 15 páginas, 8 figuras, 1 tabla | Versión del editor: | http://dx.doi.org/10.1038/msb.2010.87 | URI: | http://hdl.handle.net/10261/52402 | DOI: | 10.1038/msb.2010.87 | ISSN: | 1744-4292 | E-ISSN: | 1744-4292 |
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Mol_Syst_Biol_Fdez-Tornero_2010.pdf | 1,64 MB | Adobe PDF | Visualizar/Abrir |
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