3NSU

A Systematic Screen for Protein-Lipid Interactions in Saccharomyces cerevisiae

Summary for 3NSU

• Entry DOI: 10.2210/pdb3nsu/pdb
• Related: 1BTK
• Descriptor: Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1, SULFATE ION (3 entities in total)
• Functional Keywords: pleckstrin homology domain, signaling protein
• Biological source: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast)
• Cellular location: Cell membrane; Peripheral membrane protein; Cytoplasmic side: P40485
• Total number of polymer chains: 2
• Total formula weight: 27939.49

Authors

Gallego, O.,Fernandez-Tornero, C.,Aguilar-Gurrieri, C.,Muller, C.,Gavin, A.C. (deposition date: 2010-07-02, release date: 2010-12-15, Last modification date: 2023-09-06)

Primary citation

Gallego, O.,Betts, M.J.,Gvozdenovic-Jeremic, J.,Maeda, K.,Matetzki, C.,Aguilar-Gurrieri, C.,Beltran-Alvarez, P.,Bonn, S.,Fernandez-Tornero, C.,Jensen, L.J.,Kuhn, M.,Trott, J.,Rybin, V.,Muller, C.W.,Bork, P.,Kaksonen, M.,Russell, R.B.,Gavin, A.C.
A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae.
Mol. Syst. Biol., 6:430-430, 2010

PubMed 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.

PubMed: 21119626
DOI: 10.1038/msb.2010.87

Experimental method

X-RAY DIFFRACTION (2 Å)