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Interfilament interaction between IMPDH and CTPS cytoophidia.

Chia-Chun Chang^1,2, Gerson D Keppeke¹, Li-Ying Sung^2,3

¹Department of Physiology, Anatomy and Genetics, University of Oxford, UK.

The FEBS Journal

|August 8, 2018

Summary

Inosine monophosphate dehydrogenase (IMPDH) and cytidine triphosphate synthase (CTPS) form cellular structures called cytoophidia. This study visualizes their dynamic interactions within these structures, revealing how they coordinate through filament intertwining.

Keywords:

CTP synthase IMP dehydrogenase cytoophidium live-cell imaging super-resolution imaging

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Area of Science:

Cell Biology
Biochemistry
Molecular Biology

Background:

Inosine monophosphate dehydrogenase (IMPDH) and cytidine triphosphate synthase (CTPS) are key enzymes in nucleotide synthesis.
These enzymes can form filamentous structures called cytoophidia, potentially regulating their activity.
The precise association between IMPDH and CTPS within cytoophidia remains unclear.

Purpose of the Study:

To visualize the dynamic assembly, disassembly, and movement of cytoophidia in live cells.
To elucidate the structural organization of IMPDH and CTPS filaments within mixed cytoophidia.
To understand the coordination mechanisms between IMPDH and CTPS cytoophidia.

Main Methods:

Established a HeLa cell line coexpressing OFP-tagged IMPDH2 and GFP-tagged CTPS1.
Utilized live-cell imaging to observe cytoophidium dynamics.
Employed super-resolution confocal microscopy to analyze filament alignment and intertwining.

Main Results:

Successfully visualized the dynamic behavior of cytoophidia in real-time.
Demonstrated the alignment and intertwining of IMPDH- and CTPS-based filaments within mixed cytoophidia.
Provided detailed insights into the structural organization of these enzyme complexes.

Conclusions:

IMPDH and CTPS cytoophidia exhibit dynamic assembly, disassembly, and movement.
IMPDH and CTPS filaments are structurally organized and can intertwine within mixed cytoophidia.
Interfilament interactions likely play a role in coordinating IMPDH and CTPS cytoophidia, suggesting a novel regulatory mechanism.