A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae
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A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae. / 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.
In: Molecular Systems Biology, Vol. 6, 2010, p. 430.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae
AU - Gallego, Oriol
AU - Betts, Matthew J
AU - Gvozdenovic-Jeremic, Jelena
AU - Maeda, Kenji
AU - Matetzki, Christian
AU - Aguilar-Gurrieri, Carmen
AU - Beltran-Alvarez, Pedro
AU - Bonn, Stefan
AU - Fernández-Tornero, Carlos
AU - Jensen, Lars Juhl
AU - Kuhn, Michael
AU - Trott, Jamie
AU - Rybin, Vladimir
AU - Müller, Christoph W
AU - Bork, Peer
AU - Kaksonen, Marko
AU - Russell, Robert B
AU - Gavin, Anne-Claude
PY - 2010
Y1 - 2010
N2 - 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.
AB - 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.
KW - Algorithms
KW - Fatty Acid-Binding Proteins
KW - High-Throughput Screening Assays
KW - Lipid Metabolism
KW - Lipid-Linked Proteins
KW - Lipids
KW - Metabolome
KW - Models, Biological
KW - Protein Array Analysis
KW - Protein Binding
KW - Protein Interaction Domains and Motifs
KW - Saccharomyces cerevisiae
KW - Saccharomyces cerevisiae Proteins
KW - Validation Studies as Topic
U2 - 10.1038/msb.2010.87
DO - 10.1038/msb.2010.87
M3 - Journal article
C2 - 21119626
VL - 6
SP - 430
JO - Molecular Systems Biology
JF - Molecular Systems Biology
SN - 1744-4292
ER -
ID: 40739959