Journal
CELL REPORTS
Volume 10, Issue 1, Pages 8-19Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2014.12.010
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Funding
- Pershing Square Sohn Foundation
- Department of Defense [W81XWH-13-PCRP-IDA]
- ACS [RSG-14-069-01-TBE]
- NIH [CA137050, 1R01CA190092-01, 5P30CA45508-26, 5P50CA101955-07, 5T32CA148056]
- Robertson Research Fund of Cold Spring Harbor Laboratory
- NIH Cancer Center [5P30CA045508]
- Cold Spring Harbor Laboratory Association
- David Rubinstein Center for Pancreatic Cancer Research at MSKCC
- Damon Runyon Cancer Research Foundation [DRG-2165-13]
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Phosphatidylinositol 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.
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