Journal
EXPERIMENTAL CELL RESEARCH
Volume 323, Issue 1, Pages 242-253Publisher
ELSEVIER INC
DOI: 10.1016/j.yexcr.2014.01.029
Keywords
CTP synthase; Cytoophidium; Intracellular compartment
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Funding
- Medical Research Council [MC_U137788471, MC_UU_12021/3] Funding Source: researchfish
- Medical Research Council [MC_U137788471, MC_UU_12021/3] Funding Source: Medline
- MRC [MC_UU_12021/3, MC_U137788471] Funding Source: UKRI
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CTP synthase is an essential metabolic enzyme responsible for the de novo synthesis of CTP. Multiple studies have recently showed that CTP synthase protein molecules form filamentous structures termed cytoophidia or CTP synthase filaments in the cytoplasm of eukaryotic cells, as well as in bacteria. Here we report that CTP synthase can form cytoophidia not only in the cytoplasm, but also in the nucleus of eukaryotic cells. Both glutamine deprivation and glutamine analog treatment promote formation of cytoplasmic cytoophidia (C-cytoophidia) and nuclear cytoophidia (N-cytoophidia). N-cytoophidia are generally shorter and thinner than their cytoplasmic counterparts. In mammalian cells, both CTP synthase 1 and CTP synthase 2 can form cytoophidia. Using live imaging, we have observed that both C-cytoophidia and N-cytoophidia undergo multiple rounds of fusion upon glutamine analog treatment. Our study reveals the coexistence of cytoophidia in the cytoplasm and nucleus, therefore providing a good opportunity to investigate the intracellular compartmentation of CTP synthase. (C) 2014 Published by Elsevier Inc.
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