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Super-Resolution Imaging Reveals Dynamic Reticular Cytoophidia.

Yi-Fan Fang1, Yi-Lan Li1, Xiao-Ming Li1

  • 1School of Life Science and Technology, Shanghai Tech University, Shanghai 201210, China.

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Cytidine triphosphate (CTP) synthase (CTPS) forms dynamic, filamentous cytoophidia in human cells. These structures are reticular, suggesting they may compartmentalize cellular components.

Keywords:
CTP synthasecytoophidiumfluorescence recovery after photobleaching (FRAP)stimulated emission depletion (STED)

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Area of Science:

  • Cell Biology
  • Biophysics
  • Molecular Biology

Background:

  • Cytidine triphosphate (CTP) synthase (CTPS) is an essential enzyme involved in nucleotide biosynthesis.
  • CTPS forms filamentous structures known as cytoophidia, observed across all domains of life.
  • The mesoscale organization and physical properties of cytoophidia remain incompletely understood.

Purpose of the Study:

  • To investigate the mesoscale structure and dynamics of CTPS cytoophidia in human cells.
  • To characterize the physical properties of cytoophidia using advanced microscopy techniques.
  • To explore the potential functional implications of cytoophidia's reticular organization.

Main Methods:

  • Fluorescence Recovery After Photobleaching (FRAP) microscopy to assess cytoophidia dynamics.
  • Stimulated Emission Depletion (STED) microscopy for high-resolution imaging of cytoophidia structure.
  • Utilized an EGFP dimeric tag to probe the physical characteristics of CTPS filaments.

Main Results:

  • CTPS cytoophidia exhibit dynamic behavior within the cell.
  • The cytoophidia display a reticular, interconnected network structure.
  • Evidence suggests that the reticular network may facilitate the co-localization of other proteins, such as IMPDH.
  • Observed novel structures termed CTPS granules with associated 'tentacles'.

Conclusions:

  • CTPS cytoophidia are dynamic and possess a reticular architecture.
  • The mesoscale organization of CTPS cytoophidia likely plays a role in cellular compartmentalization and protein interactions.
  • Further research into CTPS granules and their functions is warranted.