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Updated: Feb 7, 2026

Bottom-Up In Vitro Methods to Assay the Ultrastructural Organization, Membrane Reshaping, and Curvature Sensitivity Behavior of Septins
Published on: August 17, 2022
Mechanically-induced Septin Networks Protect Nuclear Integrity.
Margaret E Utgaard1, Alexia Caillier1, Shreya Chandrasekar1
1Dept. Cell & Molecular Physiology, Loyola University Chicago, Stritch School of Medicine, Maywood, IL 60153.
Septins, a cytoskeletal component, protect cells from mechanical stress by reinforcing the nuclear membrane. These proteins accumulate under force, preventing nuclear rupture during cellular confinement.
Area of Science:
- Cell biology
- Biophysics
- Cytoskeletal dynamics
Background:
- The cytoskeleton mediates cellular mechanical interactions.
- The specific role of septins in these processes is not well understood.
- Septins are known to interact with actin filaments.
Purpose of the Study:
- To investigate the role of septins in cellular mechanotransduction.
- To determine how septins respond to mechanical forces, particularly those involving the nucleus.
- To elucidate the protective function of septins against nuclear damage.
Main Methods:
- Cell culture and manipulation (nucleus removal).
- Microscopy to observe septin and actin localization.
- Mechanical stimulation via cell confinement and bead indentation.
- Gene knockdown (SEPT7) to assess functional consequences.
Main Results:
- Septins localize to subnuclear actin stress fibers.
- Loss of the nucleus disrupts these septin-decorated fibers, but they can be rescued by a nucleus-mimicking bead.
- Mechanical compression increases septin accumulation at the nucleus-cortex interface.
- SEPT7 knockdown elevates the risk of nuclear membrane rupture under confinement.
Conclusions:
- Septins function as a mechanosensitive element in cells.
- They dynamically accumulate in response to mechanical stress, particularly at the nuclear envelope.
- Septins provide a protective mechanism, buffering forces to prevent nuclear membrane rupture.
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