ArticleThe Journal of biological chemistry2022
Purine biosynthetic enzymes assemble into liquid-like condensates dependent on the activity of chaperone protein HSP90.
Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 44 citations in OpenAlex.
- Review
- Microcephaly-associated protein WDR62 supports purine metabolism by interacting with co-chaperone BAG2.The EMBO journal · 2026Article
- Kinase KEY1 controls pyrenoid condensate size throughout the cell cycle by disrupting phase separation interactions.Nature cell biology · 2026Article
- IMP metabolic mechanisms and IMPDH targeting strategies in tumor metabolic reprogramming and therapy (Review).International journal of molecular medicine · 2026Review
- Spatiotemporal organization of membrane protein controls bacterial extracellular electron transfer.Nature communications · 2026Article
- Coordination of cell organelles to promote metabolon formation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Enzyme Assemblies in Nucleotide Metabolism: Structure, Regulation, and Disease Implications.Advances in experimental medicine and biology · 2026Review
- Metabolic functions for molecular chaperones and stress proteins in microcephaly.Cellular and molecular life sciences : CMLS · 2025Review
- Kinase KEY1 controls pyrenoid condensate size throughout the cell cycle by disrupting phase separation interactions.bioRxiv : the preprint server for biology · 2025Article
- Expanding clinical spectrum of PAICS deficiency: Comprehensive analysis of two sibling cases.European journal of human genetics : EJHG · 2025Article
- Dynamic Cytoplasm: A Physical Regulator of Enzymatic Function.Biochemistry · 2025Review
- Purinosomes as a therapeutic target in hepatocellular carcinoma: insights and opportunities.Discover oncology · 2025Article
- Purinosomes and Purine Metabolism in Mammalian Neural Development: A Review.Acta histochemica et cytochemica · 2024Review
- Interplay between mTOR and Purine Metabolism Enzymes and Its Relevant Role in Cancer.International journal of molecular sciences · 2024Review
- Light-sensitive phosphorylation regulates retinal IMPDH1 activity and filament assembly.The Journal of cell biology · 2024Article
- Chaperone regulation of biomolecular condensates.Frontiers in biophysics · 2024Article
- Regulatory mechanisms of one-carbon metabolism enzymes.The Journal of biological chemistry · 2023Review
- Article
- Stress-related biomolecular condensates in plants.The Plant cell · 2023Article
- Paradoxes of Cellular SUMOylation Regulation: A Role of Biomolecular Condensates?Pharmacological reviews · 2023Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Enzymes within the de novo purine biosynthetic pathway spatially organize into dynamic intracellular assemblies called purinosomes. The formation of purinosomes has been correlated with growth conditions resulting in high purine demand, and therefore, the cellular advantage of complexation has been hypothesized to enhance metabolite flux through the pathway. However, the properties of this cellular structure are unclear. Here, we define the purinosome in a transient expression system as a biomolecular condensate using fluorescence microscopy. We show that purinosomes, as denoted by formylglycinamidine ribonucleotide synthase granules in purine-depleted HeLa cells, are spherical and appear to coalesce when two come into contact, all liquid-like characteristics that are consistent with previously reported condensates. We further explored the biophysical and biochemical means that drive the liquid-liquid phase separation of these structures. We found that the process of enzyme condensation into purinosomes is likely driven by the oligomeric state of the pathway enzymes and not a result of intrinsic disorder, the presence of low-complexity domains, the assistance of RNA scaffolds, or changes in intracellular pH. Finally, we demonstrate that the heat shock protein 90 KDa helps to regulate the physical properties of the condensate and maintain their liquid-like state inside HeLa cells. We show that disruption of heat shock protein 90 KDa activity induced the transformation of formylglycinamidine ribonucleotide synthase clusters into more irregularly shaped condensates, suggesting that its chaperone activity is essential for purinosomes to retain their liquid-like properties. This refined view of the purinosome offers new insight into how metabolic enzymes spatially organize into dynamic condensates within human cells.
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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.