Cytoophidia in the Molecular Sciences: Structure, Function, and Regulation
A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".
Deadline for manuscript submissions: closed (20 April 2025) | Viewed by 2866
Special Issue Editor
2. Department of Physiology, Anatomy and Genetics, University of Oxford, Oxford OX1 3PT, UK
Interests: metabolic cell biology; cytoophidium
Special Issues, Collections and Topics in MDPI journals
Special Issue Information
Dear Colleagues,
The subcellular sequestration of proteins within membrane-bound compartments is widely acknowledged to be an important mode of enzymatic regulation. In 2010, the essential de novo pyrimidine biosynthesis enzyme CTP synthase (CTPS) was found to assemble to form a filamentous structure termed “the cytoophidium”.Cytoophidia can be formed by metabolic enzymes in all the three domains of life. Many more enzymes have been identified as cytoophidium-assembling proteins. Recent studies have pushed the resolution to near-atomic levels to analyze the filamentation of CTP synthase with all its substrates. In addition, a positive-feedback signaling loop containing both cytoophidia and an integrin adhesion complex couples tissue architecture and metabolism. Therefore, multidisciplinary approaches provide invaluable insights into the structure, function, and regulation of cytoophidia in the molecular sciences.
Prof. Dr. Ji-Long Liu
Guest Editor
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Keywords
- cytoophidium
- filament
- CTP synthase
- IMPDH
- intracellular compartment
- metabolic cell biology
- metabolic filamentation
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