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A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

  • 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.
OriginalsprogEngelsk
TidsskriftMolecular Systems Biology
Vol/bind6
Sider (fra-til)430
ISSN1744-4292
DOI
StatusUdgivet - 2010
Eksternt udgivetJa

ID: 40739959