| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2039948 | Cell Reports | 2015 | 12 Pages |
•PI acyl chain composition varies between cancer and normal cell lines•Growth factor removal does not affect PI lipid chain composition•p53 mutation leads to changes in PI acyl chain composition
SummaryPhosphatidylinositol phosphate (PIP) second messengers relay extracellular growth cues through the phosphorylation status of the inositol sugar, a signal transduction system that is deregulated in cancer. In stark contrast to PIP inositol head-group phosphorylation, changes in phosphatidylinositol (PI) lipid acyl chains in cancer have remained ill-defined. Here, we apply a mass-spectrometry-based method capable of unbiased high-throughput identification and quantification of cellular PI acyl chain composition. Using this approach, we find that PI lipid chains represent a cell-specific fingerprint and are unperturbed by serum-mediated signaling in contrast to the inositol head group. We find that mutation of Trp53 results in PIs containing reduced-length fatty acid moieties. Our results suggest that the anchoring tails of lipid second messengers form an additional layer of PIP signaling in cancer that operates independently of PTEN/PI3-kinase activity but is instead linked to p53.
Graphical AbstractFigure optionsDownload full-size imageDownload as PowerPoint slide
