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Related Concept Videos

Role of Septins01:02

Role of Septins

1.7K
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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Septins01:19

Septins

1.8K
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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Cytoskeletal Linker Proteins - Plakins01:09

Cytoskeletal Linker Proteins - Plakins

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Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...
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Depolarizing Blockers: Pharmocokinetics01:19

Depolarizing Blockers: Pharmocokinetics

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Depolarizing blockers are administered through intravenous injection. Succinylcholine is the most common choice of depolarizing blockers in emergency clinical practices. Although they have a rapid onset, they readily diffuse away from the motor end plate into the extracellular fluid. They are metabolized by enzymes such as liver butyrylcholinesterase and plasma pseudocholinesterases. This produces a short duration of action, typically 5-10 minutes long, unlike nondepolarizing blockers, which...
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Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

2.0K
Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
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Related Experiment Video

Updated: Jun 7, 2025

Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution
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Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution

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Protamine 2 deficiency results in Septin 12 abnormalities.

Ondrej Sanovec1,2, Michaela Frolikova1, Veronika Kraus1

  • 1Laboratory of Reproductive Biology, Institute of Biotechnology, Czech Academy of Sciences, BIOCEV, Vestec, Czechia.

Frontiers in Cell and Developmental Biology
|November 11, 2024
PubMed
Summary

Sperm chromatin protein Protamine 2 interacts with motility protein Septin 12. This interaction impacts Septin 12 localization and sperm quality, potentially explaining low sperm motility and abnormalities.

Keywords:
Protamine 2 deficiencySeptin 12annulusasthenozoospermiaspermsperm immotility

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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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Procoagulant Platelet Characterization by Measuring Phosphatidylserine Exposure and Microvesicle Release from Human Purified Platelets
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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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Area of Science:

  • Reproductive biology
  • Spermatozoa
  • Cell biology

Background:

  • Abnormal sperm chromatin is linked to poor sperm motility.
  • The interdependence between sperm chromatin and motility remains unclear.

Purpose of the Study:

  • To investigate the mechanistic link between sperm chromatin packaging and sperm motility.
  • To explore the interaction between Protamine 2 and Septin 12 in sperm.

Main Methods:

  • Investigated Protamine 2 (Prm2) knockout mouse models.
  • Analyzed Septin 12 isoforms' localization in Prm2 deficient sperm.
  • Performed co-immunoprecipitation assays with Protamine 2 and Septin 12.
  • Examined sperm nuclear morphology and acrosome biogenesis.
  • Analyzed human asthenozoospermia patient samples.

Main Results:

  • Protamine 2 interacts with Septin 12, a key motility-associated protein.
  • Septin 12 isoforms show altered localization in Prm2 deficient sperm.
  • Prm2 deficient sperm exhibit smaller nuclei and abnormal acrosome formation.
  • Human asthenozoospermia patients display imbalanced protamine ratios and altered Septin 12 localization.

Conclusions:

  • Findings suggest a novel interaction between Septin 12 and Protamine 2 (or Lamin B2/3).
  • Altered expression and localization of these proteins contribute to sperm motility defects and morphological abnormalities.
  • This study provides mechanistic insights into sperm quality regulation.