학술논문
A systematic screen for protein–lipid interactions in Saccharomyces cerevisiae.
Document Type
Article
Author
Gallego, Oriol; Betts, Matthew J; Gvozdenovic‐Jeremic, Jelena; Maeda, Kenji; Matetzki, Christian; Aguilar‐Gurrieri, Carmen; Beltran‐Alvarez, Pedro; Bonn, Stefan; Fernández‐Tornero, Carlos; Jensen, Lars Juhl; Kuhn, Michael; Trott, Jamie; Rybin, Vladimir; Müller, Christoph W; Bork, Peer; Kaksonen, Marko; Russell, Robert B; Gavin, Anne‐Claude
Source
Subject
Language
ISSN
1744-4292
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. [ABSTRACT FROM AUTHOR]