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Article summary:

1. ATP Citrate Lyase (ACLY) is a key metabolic enzyme that catalyzes the production of acetyl-CoA and is upregulated in cancer cells, making it essential for their growth.

2. This study shows that phospholipids PIP2 and PIP3, as well as the Src family kinase Lyn, bind to ACLY in acute lymphoblastic leukemia (AML) patient-derived cells but not in normal donor cells.

3. The binding of PIP2/PIP3 and Lyn-mediated phosphorylation of ACLY stimulate pathways related to acetyl-CoA dependent growth and survival metabolism in cancer cells, suggesting that Lyn has a new role as a regulator of acetyl-CoA mediated metabolic pathways.

Article analysis:

The article is generally reliable and trustworthy, providing evidence for its claims through experiments such as immunoprecipitation, western blotting, reporter ion intensities, confocal imaging, etc. The authors also provide detailed methods for each experiment so readers can understand how the data was collected and analyzed. Furthermore, the article does not appear to be biased or one-sided; it presents both sides equally by discussing both AML patient-derived cells and non-malignant marrow CD34+ cells.

However, there are some potential issues with the article's trustworthiness and reliability. For example, while the authors discuss possible risks associated with their findings (e.g., linking ACLY to cancer pathways), they do not explore any counterarguments or alternative explanations for their results. Additionally, while they mention that PI(3,4,5)P3 levels were too low in HL-60 cells to be analyzed by their method, they do not provide any evidence or explanation for why this might be the case. Finally, there is no discussion of potential limitations or weaknesses of their study; this could lead readers to overestimate the strength of their conclusions.