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Septins are protein filaments forming the cytoskeleton along with the microtubules, microfilaments, intermediate filaments, and other accessory proteins. In 1971 while studying the cell division cycle in mutant Saccharomyces cerevisiae Harwell et al. first identified the septin-related genes playing a crucial role in yeast cytokinesis. Fluorescence microscopy revealed that these proteins localize at the budding neck as rings. These ring-like proteins were then named Septins by John Pringle, and...
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Local RhoA activation induces septin recruitment.

Shreya Chandrasekar1, Margaret E Utgaard1, Bradley Somerfield1

  • 1Dept. Cell & Molecular Physiology, Loyola University Chicago, Stritch School of Medicine, Maywood, IL 60153.

Biorxiv : the Preprint Server for Biology
|November 19, 2025
PubMed
Summary
This summary is machine-generated.

RhoA signaling influences the septin cytoskeleton, a key component of cell structure. Local RhoA activation, but not myosin changes, increases septin accumulation, revealing new roles for septins in cell remodeling.

Keywords:
CytoskeletonMyosin 2OptogeneticsRhoASeptin

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Area of Science:

  • Cell Biology
  • Cytoskeletal Dynamics
  • Molecular Cell Biology

Background:

  • The actin cytoskeleton is crucial for cell shape and structure.
  • RhoA GTPase regulates the actomyosin cytoskeleton, but its role in septin cytoskeleton regulation is unclear.
  • Traditional assays struggle to resolve spatial and temporal RhoA interactions.

Purpose of the Study:

  • To investigate how RhoA and myosin impact the septin cytoskeleton.
  • To explore the spatial and temporal effects of RhoA signaling on septin organization.
  • To elucidate the mechanism by which RhoA influences septin structure.

Main Methods:

  • Utilized optogenetic tools for spatial and temporal control of cellular processes.
  • Manipulated myosin localization and contractile force.
  • Activated RhoA locally within cells.
  • Assessed changes in septin cytoskeleton architecture and accumulation.

Main Results:

  • Local accumulation or increased activity of myosin did not alter septin architecture.
  • Local activation of RhoA led to a significant local increase in septin accumulation.
  • This RhoA-induced septin increase was independent of the scaffolding protein anillin.

Conclusions:

  • RhoA signaling directly impacts septin cytoskeleton organization.
  • Myosin activity alone is insufficient to remodel the septin cytoskeleton.
  • Septins may play a broader role in mediating RhoA signaling through cytoskeletal remodeling.