ArticleNature communications2025
The role of gene duplication and paralog specialisation in the evolution of the mammalian PRPS complex.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed.
- Copper transport to mitochondria by SLC25A3 contributes to skeletal myoblast differentiation and is required for survival of differentiated myotubes.bioRxiv : the preprint server for biology · 2026Article
- Divergent evolution of the PRPS enzymes across the tree of life.bioRxiv : the preprint server for biology · 2026Article
- The oncogenic control of nucleotide synthesis.Oncogenesis · 2026Review
- Scaffolding-dependent CASP1 constrains excessive cell-intrinsic inflammatory signaling in leukemia.Cell chemical biology · 2026Article
- Rate-limiting enzymes in nucleotide metabolism synchronize nucleotide biosynthesis and chromatin formation.Molecular cell · 2025Article
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6 authors.
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Abstract
The phosphoribosyl pyrophosphate synthetase (PRPS) enzyme catalyzes a chokepoint reaction in nucleotide production, making it essential for life. Here, we show that the presence of multiple PRPS-encoding genes is a hallmark trait of eukaryotes, and we find that gains or losses of paralogs are associated with major branching events in the eukaryotic tree. We pinpoint the evolutionary origins and define the individual roles for each of the mammalian PRPS paralogs, which we demonstrate work together as a heterogeneous multicomponent complex. Employing isogenic cells representing all viable individual or combinatorial assembly states, we dissect the basic organizational principles of the enzyme complex and characterize the emergent properties responsible for paralog specialization, including new modes of regulation that govern complex assembly and activity in vivo. Collectively, our study demonstrates how evolution has transformed a single PRPS enzyme into a biochemical complex endowed with novel functional and regulatory features that fine-tune mammalian metabolism.
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