3NSU

A Systematic Screen for Protein-Lipid Interactions in Saccharomyces cerevisiae

3NSU の概要

• エントリーDOI: 10.2210/pdb3nsu/pdb
• 関連するPDBエントリー: 1BTK
• 分子名称: Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1, SULFATE ION (3 entities in total)
• 機能のキーワード: pleckstrin homology domain, signaling protein
• 由来する生物種: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast)
• 細胞内の位置: Cell membrane; Peripheral membrane protein; Cytoplasmic side: P40485
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27939.49

構造登録者

Gallego, O.,Fernandez-Tornero, C.,Aguilar-Gurrieri, C.,Muller, C.,Gavin, A.C. (登録日: 2010-07-02, 公開日: 2010-12-15, 最終更新日: 2023-09-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)