A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae

Oriol Gallego; Matthew J Betts; Jelena Gvozdenovic-Jeremic; Kenji Maeda; Christian Matetzki; Carmen Aguilar-Gurrieri; Pedro Beltran-Alvarez; Stefan Bonn; Carlos Fernández-Tornero; Lars Juhl Jensen; Michael Kuhn; Jamie Trott; Vladimir Rybin; Christoph W Müller; Peer Bork; Marko Kaksonen; Robert B Russell; Anne-Claude Gavin

doi:10.1038/msb.2010.87

A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae

Oriol Gallego, Matthew J Betts, Jelena Gvozdenovic-Jeremic, Kenji Maeda, Christian Matetzki, Carmen Aguilar-Gurrieri, Pedro Beltran-Alvarez, Stefan Bonn, Carlos Fernández-Tornero, Lars Juhl Jensen, Michael Kuhn, Jamie Trott, Vladimir Rybin, Christoph W Müller, Peer Bork, Marko Kaksonen, Robert B Russell, Anne-Claude Gavin

117 Citations (Scopus)

Abstract

Proteing-metabolite networks are central to biological systems, but are incompletely understood. Here, we report a screen to catalog proteing-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 proteing-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 language	English
Journal	Molecular Systems Biology
Volume	6
Pages (from-to)	430
ISSN	1744-4292
DOIs	https://doi.org/10.1038/msb.2010.87
Publication status	Published - 2010
Externally published	Yes

Keywords

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

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10.1038/msb.2010.87

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Gallego, O., Betts, M. J., Gvozdenovic-Jeremic, J., Maeda, K., Matetzki, C., Aguilar-Gurrieri, C., Beltran-Alvarez, P., Bonn, S., Fernández-Tornero, C., Jensen, L. J., Kuhn, M., Trott, J., Rybin, V., Müller, C. W., Bork, P., Kaksonen, M., Russell, R. B., & Gavin, A-C. (2010). A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae. Molecular Systems Biology, 6, 430. https://doi.org/10.1038/msb.2010.87

Gallego, O, Betts, MJ, Gvozdenovic-Jeremic, J, Maeda, K, Matetzki, C, Aguilar-Gurrieri, C, Beltran-Alvarez, P, Bonn, S, Fernández-Tornero, C, Jensen, LJ, Kuhn, M, Trott, J, Rybin, V, Müller, CW, Bork, P, Kaksonen, M, Russell, RB & Gavin, A-C 2010, 'A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae', Molecular Systems Biology, vol. 6, pp. 430. https://doi.org/10.1038/msb.2010.87

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abstract = "Proteing-metabolite networks are central to biological systems, but are incompletely understood. Here, we report a screen to catalog proteing-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 proteing-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.",

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AU - Gallego, Oriol

AU - Betts, Matthew J

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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

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AB - Proteing-metabolite networks are central to biological systems, but are incompletely understood. Here, we report a screen to catalog proteing-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 proteing-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.

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KW - Fatty Acid-Binding Proteins

KW - High-Throughput Screening Assays

KW - Lipid Metabolism

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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

SN - 1744-4292

VL - 6

SP - 430

JO - Molecular Systems Biology

JF - Molecular Systems Biology

ER -

A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae

Abstract

Keywords

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