A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae

Research output: Contribution to journalJournal articleResearchpeer-review

  • Oriol Gallego
  • Matthew J Betts
  • Jelena Gvozdenovic-Jeremic
  • Kenji Maeda
  • Christian Matetzki
  • Carmen Aguilar-Gurrieri
  • Pedro Beltran-Alvarez
  • Stefan Bonn
  • Carlos Fernández-Tornero
  • Jensen, Lars Juhl
  • Michael Kuhn
  • Jamie Trott
  • Vladimir Rybin
  • Christoph W Müller
  • Peer Bork
  • Marko Kaksonen
  • Robert B Russell
  • Anne-Claude Gavin
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.
Original languageEnglish
JournalMolecular Systems Biology
Pages (from-to)430
Publication statusPublished - 2010
Externally publishedYes

    Research areas

  • Algorithms, Fatty Acid-Binding Proteins, High-Throughput Screening Assays, Lipid Metabolism, Lipid-Linked Proteins, Lipids, Metabolome, Models, Biological, Protein Array Analysis, Protein Binding, Protein Interaction Domains and Motifs, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Validation Studies as Topic

ID: 40739959