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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

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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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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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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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Disorders of Hemostasis01:24

Disorders of Hemostasis

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Hemostasis, the process that stops bleeding after a blood vessel injury, is crucial for maintaining the integrity of the circulatory system. However, disorders of hemostasis can disrupt this delicate balance, leading to either excessive clotting or bleeding. These disorders can be broadly classified into thromboembolic disorders and bleeding disorders.
Thromboembolic Disorders
Two factors primarily cause thromboembolic conditions.
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Anticoagulant Drugs: Low-Molecular-Weight Heparins01:30

Anticoagulant Drugs: Low-Molecular-Weight Heparins

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Hemostasis is a crucial process that prevents excessive blood loss from damaged blood vessels. It involves various mechanisms such as vasoconstriction, platelet adhesion and activation, and fibrin formation. The importance of each mechanism depends on the type of vessel injury. In contrast, thrombosis is the abnormal formation of a blood clot within the blood vessels, leading to potential complications if the clot obstructs blood flow. Thrombosis can be caused by increased coagulability of the...
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Related Experiment Video

Updated: Jun 24, 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 Sanovec, Michaela Frolikova, Veronika Kraus

    Biorxiv : the Preprint Server for Biology
    |June 10, 2024
    PubMed
    Summary

    Abnormal sperm Protamine 2 impacts Septin 12 localization, affecting sperm motility and morphology. This study reveals a key mechanism linking chromatin packaging defects to reduced sperm function.

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    Area of Science:

    • Reproductive Biology
    • Sperm Biology
    • Molecular Cell Biology

    Background:

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

    Purpose of the Study:

    • To investigate the mechanistic link between Protamine 2 (Prm2) and Septin 12 in sperm.
    • To understand how Prm2 defects affect Septin 12 localization and sperm function.

    Main Methods:

    • Co-immunoprecipitation assays in mouse testicular lysates and HEK cells.
    • Analysis of Septin 12 isoforms in Prm2-deficient sperm.
    • Assessment of sperm nucleus size and acrosome biogenesis.
    • Examination of protein fractions in human asthenozoospermic and normozoospermic sperm.

    Main Results:

    • Protamine 2 directly interacts with Septin 12.
    • Prm2 deficiency causes mislocalization of short Septin 12 and loss of long isoforms from chromatin.
    • Prm2-deficient sperm exhibit smaller nuclei and aberrant acrosome formation.
    • Retained Septin 12 isoforms are found in human asthenozoospermic sperm fractions.

    Conclusions:

    • Findings reveal a novel connection between Protamine 2 and Septin 12.
    • Altered Septin 12 expression/localization due to Prm2 defects contributes to low sperm motility and morphological abnormalities.