ArticleExperimental cell research2017
Critical roles of CTP synthase N-terminal in cytoophidium assembly.
Article in Experimental cell research, 2017. 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, 20 citations in OpenAlex.
- Article
- CTPS cytoophidia formation affects cell cycle progression and promotes TSN‑induced apoptosis of MKN45 cells.Molecular medicine reports · 2022Article
- [Interference of CTPS gene promotes toosendanin-induced apoptosis of human gastric cancer MKN-45 cells].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2022Article
- ASNS disruption shortens CTPS cytoophidia in Saccharomyces cerevisiae.G3 (Bethesda, Md.) · 2021Article
- Article
- CTP synthase polymerization in germline cells of the developingBiology open · 2020Article
- The TOR pathway modulates cytoophidium formation inThe Journal of biological chemistry · 2019Article
- The NADPJournal of microbiology (Seoul, Korea) · 2019Article
- mTOR-S6K1 pathway mediates cytoophidium assembly.Journal of genetics and genomics = Yi chuan xue bao · 2019Article
- Characterization of filament-forming CTP synthases from Arabidopsis thaliana.The Plant journal : for cell and molecular biology · 2018Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Several metabolic enzymes assemble into distinct intracellular structures in prokaryotes and eukaryotes suggesting an important functional role in cell physiology. The CTP-generating enzyme CTP synthase forms long filamentous structures termed cytoophidia in bacteria, yeast, fruit flies and human cells independent of its catalytic activity. However, the amino acid determinants for protein-protein interaction necessary for polymerisation remained unknown. In this study, we systematically analysed the role of the conserved N-terminal of Drosophila CTP synthase in cytoophidium assembly. Our mutational analyses identified three key amino acid residues within this region that play an instructive role in organisation of CTP synthase into a filamentous structure. Co-transfection assays demonstrated formation of heteromeric CTP synthase filaments which is disrupted by protein carrying a mutated N-terminal alanine residue thus revealing a dominant-negative activity. Interestingly, the dominant-negative activity is supressed by the CTP synthase inhibitor DON. Furthermore, we found that the amino acids at the corresponding position in the human protein exhibit similar properties suggesting conservation of their function through evolution. Our data suggest that cytoophidium assembly is a multi-step process involving N-terminal-dependent sequential interactions between correctly folded structural units and provide insights into the assembly of these enigmatic structures.
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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.