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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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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.
Cellular Functions of Septins
Recent studies have revealed the multifaceted roles of septins in various cellular processes such as cytokinesis, ciliogenesis, and neurogenesis. Septins act as scaffolds and...
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The double-stranded structure of DNA has two major advantages. First, it serves as a safe repository of genetic information where one strand serves as the back-up in case the other strand is damaged. Second, the double-helical structure can be wrapped around proteins called histones to form nucleosomes, which can then be tightly wound to form chromosomes. This way, DNA chains up to 2 inches long can be contained within microscopic structures in a cell. A double-stranded break not only damages...
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Comparative Excretory Systems02:24

Comparative Excretory Systems

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Animals have evolved different strategies for excretion, the removal of waste from the body. Most waste must be dissolved in water to be excreted, so an animal’s excretory strategy directly affects its water balance.
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The Fossil Record02:56

The Fossil Record

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The fossil record documents only a small fraction of all organisms that have ever inhabited Earth. Fossilization is a rare process, and most organisms never become fossils. Moreover, the fossil record only exhibits fossils that have been discovered. Nevertheless, sedimentary rock fossils of long-lived, abundant, hard-bodied organisms dominate the fossil record. These fossils offer valuable information, such as an organism's physical form, behavior, and age. Studying the fossil record helps...
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Euchromatin01:01

Euchromatin

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The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions take up more dye, appearing darker, while the less-compact areas take up less dye and appear lighter. Based on the compaction level, chromatins are classified into two primary forms – euchromatin and heterochromatin.
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Related Experiment Video

Updated: Feb 10, 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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The Mammalian Septin Interactome.

Katharina Neubauer1, Barbara Zieger1

  • 1Division of Pediatric Hematology and Oncology, Department of Pediatrics and Adolescent Medicine, Faculty of Medicine, Medical Center-University of Freiburg Freiburg, Germany.

Frontiers in Cell and Developmental Biology
|February 23, 2017
PubMed
Summary
This summary is machine-generated.

Septins are essential proteins forming complexes that regulate cell structure and function. Understanding mammalian septin interactions is crucial for insights into cellular processes and diseases.

Keywords:
human endothelial cellsplateletsseptin-interacting proteinsseptin-multimersseptins

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Septins are conserved GTP-binding proteins involved in cytoskeleton organization, cytokinesis, and membrane dynamics.
  • Thirteen mammalian septin genes form four subgroups (SEPT2, SEPT3, SEPT6, SEPT7) that assemble into complexes.
  • Septin misregulation is linked to human diseases like neurodegenerative and bleeding disorders.

Purpose of the Study:

  • To elucidate important mammalian septin interactions.
  • To focus on clinically relevant septin interactions.
  • To enhance understanding of septin functions and regulation.

Main Methods:

  • Analysis of septin sequence homology and domain structure.
  • Characterization of septin complex formation (e.g., hetero-trimer SEPT2-6-7).
  • Investigation of septin self-assembly into higher-order structures (filaments, rings).

Main Results:

  • Mammalian septins form apolar tri-, hexa-, or octameric complexes.
  • Complex composition is subgroup-specific, with isoforms influencing function.
  • Septins self-assemble into diverse higher-order structures.
  • Specific septin interactions are highlighted, with clinical relevance.

Conclusions:

  • Septin complex assembly and isoforms are key to their diverse cellular roles.
  • Understanding septin interactions provides insights into cellular functions and disease mechanisms.
  • Further research is needed to fully understand septin roles, particularly in exocytosis and disease.