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| 1 | CTP Synthase Is Required for Optic Lobe Homeostasis in Drosophila显示文摘CTP synthase(CTPsyn) is a metabolic enzyme responsible for the de novo synthesis of the nucleotide CTP. Several recent studies have shown that CTPsyn forms filamentous subcellular structures known as cytoophidia in bacteria, yeast, fruit flies and humans. However, it remains elusive whether and how CTPsyn and cytoophidia play a role during development. Here, we show that cytoophidia are abundant in the neuroepithelial stem cells in Drosophila optic lobes. Optic lobes are underdeveloped in CTPsyn mutants as well as in CTPsyn RNAi. Moreover, overexpressing CTPsyn impairs the development of optic lobes, specifically by blocking the transition from neuroepithelium to neuroblast. Taken together, our results indicate that CTPsyn is critical for optic lobe homeostasis in Drosophila. | ?mür Y.Tastan Ji-Long Liu | 2015 | Journal of Genetics and Genomics2015，42，5： | 6 |
| 2 | Temperature-sensitive cytoophidium assembly in Schizosaccharomyces pombe显示文摘The metabolic enzyme CTP synthase(CTPS) is able to compartmentalize into filaments,termed cytoophidia,in a variety of organisms including bacteria,budding yeast,fission yeast,fruit flies and mammals.A previous study in budding yeast shows that the filament-forming process of CTPS is not sensitive to temperature shift.Here we study CTPS filamentation in the fission yeast Schizosaccharomyces pombe.To our surprise,we find that both the length and the occurrence of cytoophidia in S.pombe decrease upon cold shock or heat shock.The temperature-dependent changes of cytoophidia are fast and reversible.Taking advantage of yeast genetics,we demonstrate that heat-shock proteins are required for cytoophidium assembly in S.pombe.Temperature sensitivity of cytoophidia makes S.pombe an attractive model system for future investigations of this novel membraneless organelle. | Jing Zhang Ji-Long Liu | 2019 | Journal of Genetics and Genomics2019，46，9： | 5 |
| 3 | mTOR-S6K1 pathway mediates cytoophidium assembly显示文摘CTP synthase(CTPS), the rate-limiting enzyme in de novo CTP biosynthesis, has been demonstrated to assemble into evolutionarily conserved filamentous structures, termed cytoophidia, in Drosophila, bacteria, yeast and mammalian cells. However, the regulation and function of the cytoophidium remain elusive. Here, we provide evidence that the mechanistic target of rapamycin(mTOR) pathway controls cytoophidium assembly in mammalian and Drosophila cells. In mammalian cells, we find that inhibition of mTOR pathway attenuates cytoophidium formation. Moreover, CTPS cytoophidium assembly appears to be dependent on the mTOR complex 1(mTORC1) mainly. In addition, knockdown of the mTORC1 downstream target S6 K1 can inhibit cytoophidium formation, while overexpression of the constitutively active S6 K1 reverses mTOR knockdown-induced cytoophidium disassembly. Finally, reducing m TOR protein expression results in a decrease of the length of cytoophidium in Drosophila follicle cells.Therefore, our study connects CTPS cytoophidium formation with the mTOR signaling pathway. | Zhe Sun Ji-Long Liu | 2019 | Journal of Genetics and Genomics2019，46，2： | 3 |
| 4 | The atlas of cytoophidia in Drosophila larvae显示文摘In 2010,cytidine 50-triphosphate synthase(CTPS)was reported to form the filamentous or serpentine structure in Drosophila,which we termed the cytoophidium.In the last decade,CTPS filaments/cytoophidia have been found in bacteria,budding yeast,human cells,mice,fission yeast,plants,and archaea,indicating that this mechanism is highly conserved in evolution.In addition to CTPS,other metabolic enzymes have been identified to have the characteristics of forming cytoophidia or similar advanced structures,demonstrating that this is a basic strategy of cells.Nevertheless,our understanding of the physiological function of the cytoophidium remains incomplete and elusive.Here,we took the larva of Drosophila melanogaster as a model to systematically describe the localization and distribution of cytoophidia in different tissues during larval development.We found that the distribution pattern of CTPS cytoophidia is dynamic and heterogenic in larval tissues.Our study provides a road map for further understanding of the function and regulatory mechanism of cytoophidia. | Yuanbing Zhang Jingnan Liu Ji-Long Liu | 2020 | Journal of Genetics and Genomics2020，47，6： | 2 |
| 5 | CTP synthase forms cytoophidia in archaea显示文摘CTP synthase(CTPS)is an important metabolic enzyme that catalyzes the rate-Iimiting reaction of nucleotide CrP de novo synthesis.Since 2010,a series of studies have demonstrated that CTPS can form filamentous structures in bacteria and eukaryotes,which are termed cytoophidia.However,it is unknown whether cytoophidia exist in the third domain of life,archaea.Using Haloarcula hispanica as a model system,here we demonstrate that CTPS forms distinct intracellular compartments in archaea.Under stimulated emission depletion microscopy,we find that the structures of H.hispanica CTPS are elongated,similar to cytoophidia in bacteria and eukaryotes.When Haloarcula cells are cultured in lowsalt medium,the occurrence of cytoophidia increases dramatically.In addition,treatment of H.hispanica with a glutamine analog or overexpression of CTPS can promote cytoophidium assembly.Our study reveals that CTPS can fo rm cytoophidia in all three domains of life,suggesting that forming cytoophidia is an ancient property of CTPS. | Shuang Zhou Hua Xiang Ji-Long Liu | 2020 | Journal of Genetics and Genomics2020，47，4： | 2 |
| 6 | Filamentation of Metabolic Enzymes in Saccharomyces cerevisiae显示文摘Compartmentation via filamentation has recently emerged as a novel mechanism for metabolic regulation. In order to identify filamentforming metabolic enzymes systematically, we performed a genome-wide screening of all strains available from an open reading frameGFP collection in Saccharomyces cerevisiae. We discovered nine novel filament-forming proteins and also confirmed those identified previously. From the 4159 strains, we found 23 proteins, mostly metabolic enzymes, which are capable of forming filaments in vivo. In silico protein-protein interaction analysis suggests that these filament-forming proteins can be clustered into several groups, including translational initiation machinery and glucose and nitrogen metabolic pathways. Using glutamine-utilising enzymes as examples, we found that the culture conditions affect the occurrence and length of the metabolic filaments. Furthermore, we found that two CTP synthases(Ura7p and Ura8p) and two asparagine synthetases(Asn1p and Asn2p) form filaments both in the cytoplasm and in the nucleus.Live imaging analyses suggest that metabolic filaments undergo sub-diffusion. Taken together, our genome-wide screening identifies additional filament-forming proteins in S. cerevisiae and suggests that filamentation of metabolic enzymes is more general than currently appreciated. | Qing-Ji Shen Hakimi Kassim Yong Huang Hui Li Jing Zhang Guang Li Peng-Ye Wang Jun Yan Fangfu Ye Ji-Long Liu | 2016 | Journal of Genetics and Genomics2016，43，6： | 2 |
| 7 | The proline synthesis enzyme P5CS forms cytoophidia in Drosophila显示文摘Compartmentation of enzymes via filamentation has arisen as a mechanism for the regulation of metabolism.In 2010,three groups independently reported that CTP synthase(CTPS)can assemble into a filamentous structure termed the cytoophidium.In searching for CTPS-interacting proteins,here we perform a yeast two-hybrid screening of Drosophila proteins and identify a putative CTPS-interacting protein,△~1-pyrroline-5-carboxylate synthase(P5CS).Using the Drosophila follicle cell as the in vivo model,we confirm that P5CS forms cytoophidia,which are associated with CTPS cytoophidia.Overexpression of P5CS increases the length of CTPS cytoophidia.Conversely,filamentation of CTPS affects the morphology of P5CS cytoophid ia.Finally,in vitro analyses confirm the filament-fo rming property of P5CS.Our work links CTPS with P5CS,two enzymes involved in the rate-limiting steps in pyrimidine and proline biosynthesis,respectively. | Bo Zhang Omür Y.Tastan Xian Zhou Chen-Jun Guo Xuyang Liu Aaron Thind Huan-Huan Hu Suwen Zhao Ji-Long Liu | 2020 | Journal of Genetics and Genomics2020，47，3： | 1 |
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