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Related Concept Videos

Septins01:19

Septins

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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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Nuclear receptors, or NRs, are unique transcription factors that regulate gene transcription and affect the cellular pathways involved in reproduction, development, or metabolism. Their ability to be stimulated by small lipophilic ligands and control vital cellular processes makes them ideal drug targets. Nearly 10-15% of currently prescribed drugs target these receptors.
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Role of Septins01:02

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Septins are the recently discovered fourth major protein component of the cytoskeleton, along with microfilaments, microtubules, and intermediate filaments. These proteins can associate with other cytoskeletal filaments and carry out varied roles or can be free-floating in the cytoplasm.
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Protein Networks02:26

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An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
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Nuclear Fission02:50

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Many heavier elements with smaller binding energies per nucleon can decompose into more stable elements that have intermediate mass numbers and larger binding energies per nucleon—that is, mass numbers and binding energies per nucleon that are closer to the “peak” of the binding energy graph near 56. Sometimes neutrons are also produced. This decomposition of a large nucleus into smaller pieces is called fission. The breaking is rather random with the formation of a large...
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Protons and neutrons, collectively called nucleons, are packed together tightly in a nucleus. With a radius of about 10−15 meters, a nucleus is quite small compared to the radius of the entire atom, which is about 10−10 meters. Nuclei are extremely dense compared to bulk matter, averaging 1.8 × 1014 grams per cubic centimeter. If the earth’s density were equal to the average nuclear density, the earth’s radius would be only about 200 meters.
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Related Experiment Video

Updated: Feb 7, 2026

Bottom-Up In Vitro Methods to Assay the Ultrastructural Organization, Membrane Reshaping, and Curvature Sensitivity Behavior of Septins
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Bottom-Up In Vitro Methods to Assay the Ultrastructural Organization, Membrane Reshaping, and Curvature Sensitivity Behavior of Septins

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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.

Biorxiv : the Preprint Server for Biology
|February 6, 2026
PubMed
Summary
This summary is machine-generated.

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.

Keywords:
mechanicsmechanotransductionnucleusseptin

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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.