CTP synthase forms cytoophidia in the cytoplasm and nucleus

被引:74
作者
Gou, Ke-Miart [1 ,2 ]
Chang, Chia-Chun [3 ]
Shen, Qing-Ji [1 ]
Sung, Li-Ying [3 ]
Liu, Ji-Long [1 ]
机构
[1] Univ Oxford, Dept Physiol Anat & Genet, MRC Funct Genom Unit, Oxford OX1 3PT, England
[2] China Agr Univ, Coll Biol Sci, State Key Lab Agrobiotechnol, Beijing 100193, Peoples R China
[3] Natl Taiwan Univ, Inst Biotechnol, Taipei 10764, Taiwan
基金
英国医学研究理事会;
关键词
CTP synthase; Cytoophidium; Intracellular compartment; INOSINE MONOPHOSPHATE DEHYDROGENASE; OCULOPHARYNGEAL MUSCULAR-DYSTROPHY; DROSOPHILA GERMINAL VESICLE; INCLUSIONS; BODIES; COMPARTMENTALIZATION; IDENTIFICATION; ORGANELLES; BACTERIA; PROTEINS;
D O I
10.1016/j.yexcr.2014.01.029
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
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.
引用
收藏
页码:242 / 253
页数:12
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