ArticlePloS one2018
Spatial alterations of De Novo purine biosynthetic enzymes by Akt-independent PDK1 signaling pathways.
Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- Enzyme Assemblies in Nucleotide Metabolism: Structure, Regulation, and Disease Implications.Advances in experimental medicine and biology · 2026Review
- Purinosomes as a therapeutic target in hepatocellular carcinoma: insights and opportunities.Discover oncology · 2025Article
- Activation of the WNT4/ β-catenin/FOXO1 pathway by PDK1 promotes cervical cancer metastasis and EMT process.Journal of molecular histology · 2025Article
- Light-sensitive phosphorylation regulates retinal IMPDH1 activity and filament assembly.The Journal of cell biology · 2024Article
- A journey into the regulatory secrets of theFrontiers in pharmacology · 2024Review
- The Purinosome: A Case Study for a Mammalian Metabolon.Annual review of biochemistry · 2022Review
- From purines to purinergic signalling: molecular functions and human diseases.Signal transduction and targeted therapy · 2021Review
- Human de novo purine biosynthesis.Critical reviews in biochemistry and molecular biology · 2021Review
- The chemical diversity and structure-based discovery of allosteric modulators for the PIF-pocket of protein kinase PDK1.Journal of enzyme inhibition and medicinal chemistry · 2019Review
- Phase-separated condensates of metabolic complexes in living cells: Purinosome and glucosome.Methods in enzymology · 2019Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
A macromolecular complex of the enzymes involved in human de novo purine biosynthesis, the purinosome, has been shown to consist of a core assembly to regulate the metabolic activity of the pathway. However, it remains elusive whether the core assembly itself can be selectively controlled in the cytoplasm without promoting the purinosome. Here, we reveal that pharmacological inhibition of the cytoplasmic activity of 3-phosphoinositide-dependent protein kinase 1 (PDK1) selectively promotes the formation of the core assembly, but not the purinosome, in cancer cells. However, alternative signaling cascades that are associated with the plasma membrane-bound PDK1 activity, including Akt-mediated cascades, regulate neither the core assembly nor the purinosome in our conditions. Along with immunofluorescence microscopy and a knock-down study against PDK1 using small interfering RNAs, we reveal that cytoplasmic PDK1-associated signaling pathways regulate subcellular colocalization of three enzymes that form the core assembly of the purinosome in an Akt-independent manner. Collectively, this study reveals a new mode of compartmentalization of purine biosynthetic enzymes controlled by spatially resolved signaling pathways.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.