%0 Journal Article %1 Gallego2010Systematic %A Gallego, Oriol %A Betts, Matthew J. %A Gvozdenovic-Jeremic, Jelena %A Maeda, Kenji %A Matetzki, Christian %A Aguilar-Gurrieri, Carmen %A Beltran-Alvarez, Pedro %A Bonn, Stefan %A Fernández-Tornero, Carlos %A Jensen, Lars Juhl J. %A Kuhn, Michael %A Trott, Jamie %A Rybin, Vladimir %A Müller, Christoph W. %A Bork, Peer %A Kaksonen, Marko %A Russell, Robert B. %A Gavin, Anne-Claude C. %D 2010 %I Nature Publishing Group %J Molecular systems biology %K interaction-networks protein-lipid %R 10.1038/msb.2010.87 %T A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae. %U http://dx.doi.org/10.1038/msb.2010.87 %V 6 %X 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.

@article{Gallego2010Systematic, abstract = {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.}, added-at = {2018-12-02T16:09:07.000+0100}, author = {Gallego, Oriol and Betts, Matthew J. and Gvozdenovic-Jeremic, Jelena and Maeda, Kenji and Matetzki, Christian and Aguilar-Gurrieri, Carmen and Beltran-Alvarez, Pedro and Bonn, Stefan and Fern\'{a}ndez-Tornero, Carlos and Jensen, Lars Juhl J. and Kuhn, Michael and Trott, Jamie and Rybin, Vladimir and M\"{u}ller, Christoph W. and Bork, Peer and Kaksonen, Marko and Russell, Robert B. and Gavin, Anne-Claude C.}, biburl = {https://www.bibsonomy.org/bibtex/2171976a282895895e118e02ecb460519/karthikraman}, citeulike-article-id = {8334217}, citeulike-linkout-0 = {http://dx.doi.org/10.1038/msb.2010.87}, citeulike-linkout-1 = {http://dx.doi.org/10.1038/msb201087}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/21119626}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=21119626}, day = 30, doi = {10.1038/msb.2010.87}, interhash = {587e6c4517a23eb978782aa815f7f52b}, intrahash = {171976a282895895e118e02ecb460519}, issn = {1744-4292}, journal = {Molecular systems biology}, keywords = {interaction-networks protein-lipid}, month = nov, pmid = {21119626}, posted-at = {2010-12-03 10:24:26}, priority = {2}, publisher = {Nature Publishing Group}, timestamp = {2018-12-02T16:09:07.000+0100}, title = {A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae.}, url = {http://dx.doi.org/10.1038/msb.2010.87}, volume = 6, year = 2010 }