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Research Article

Academia Journal of Biotechnology 5(3): 044-050, March 2017
DOI: 10.15413/ajb.2017.0102
ISSN: 2315-7747
2017 Academia Publishing

Abstract


The cytoophidium: A novel intracellular compartmentation formed by metabolic enzymes
 

Accepted 20th March, 2017

Hui Wang and Qi-Xiang Shao*
 

Department of Immunology, and the Key Laboratory of Laboratory Medicine of Jiangsu Province, School of Medicine, Jiangsu University, Zhen Jiang, Jiangsu 212013.

*Corresponding author. E-mail: shao_qx@ujs.edu.cn.


Many enzymes are found to self-assemble into foci or fiber structure and these structures may play a complementary role except enzyme modification. Cytidine triphosphate synthase (CTPS), a vital metabolic enzyme that catalyses the rate limiting reaction of CTP synthesis, can form a filamentous structure termed cytoophidium. Although this structure is widespread and universally conserved across different organisms, the cytoophidium is heterogeneous. Also, it is still controversial whether they are enzymatic active and represent a functional assembly. Here, we briefly characterized the recent findings about the structure and potential function of cytoophidium. Furthermore, the regulatory mechanism of cytoophidium assembly/disassembly and the possible signaling pathway involved in CTPS synthesis were discussed. These findings might provide biomarkers prediction for tumors chemotherapeutic drugs and promote new translational medicine development.

Key words: Filament, CTPS, IMPDH, mTOR, metabolism
.
 

This is an open access article published under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Cite this article as:
Wang H, Shao QX
(2017). The cytoophidium: A novel intracellular compartmentation formed by metabolic enzymes. Acad. J. Biotechnol. 5(3): 044-050.

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