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Related Concept Videos

Separation of Sister Chromatids02:17

Separation of Sister Chromatids

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At the transition from prophase to metaphase, there is a reduction in cohesion along the chromosomal arms, resulting in the resolution of sister chromatids. However, residual cohesin connections remain to hold the sister chromatids together until the transition from metaphase to anaphase. The residual connection prevents any premature separation of sister chromatids, blocking the risks of aneuploidy within the daughter cells.
At the onset of anaphase, separase, a proteolytic enzyme, is...
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The Spindle Assembly Checkpoint02:19

The Spindle Assembly Checkpoint

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The spindle assembly checkpoint is a molecular surveillance mechanism ensuring the fidelity of chromosome segregation during anaphase. The checkpoint monitors the completion of all the prerequisite steps before chromosome segregation to determine whether the segregation process should proceed or be delayed.
Many proteins function together to control the spindle assembly checkpoint. Mutations affecting these proteins may allow cells to proceed into anaphase prematurely, resulting in the...
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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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Cohesins02:20

Cohesins

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Cohesin protein complexes are a molecular glue that holds two sister chromatids together. They play an important role both in mitosis and meiosis. In mitosis, all cohesin complexes present on the chromosomes are removed before the start of the anaphase stage.
Cohesin complexes in Meiotic Division
Meiosis involves two distinct rounds of chromosomal segregation and cell divisions— Meiosis I followed by Meiosis II – producing four daughter cells. Meiosis I includes the separation of...
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Role of Septins01:02

Role of Septins

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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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Anaphase Promoting Complex00:50

Anaphase Promoting Complex

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The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
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Related Experiment Video

Updated: Nov 28, 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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Structure and Function of the Separase-Securin Complex.

Shukun Luo1,2, Liang Tong3

  • 1Department of Biological Sciences, Columbia University, New York, NY, 10027, USA.

Sub-Cellular Biochemistry
|November 30, 2020
PubMed
Summary
This summary is machine-generated.

Separase, a key enzyme in cell division, is inhibited by securin. Recent structural studies reveal how securin binds to separase, blocking its active site and controlling cell cycle progression.

Keywords:
CancerCohesinDNA damage repairMeiosisMitosisSister chromatids

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Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions
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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Separase is a crucial cysteine protease regulating chromosome segregation, apoptosis, and DNA repair.
  • Its activity is tightly controlled by inhibitory proteins and posttranslational modifications.
  • Dysregulated separase activity is implicated in cancer and genome instability, making it a drug discovery target.

Purpose of the Study:

  • To elucidate the molecular mechanism of securin-mediated inhibition of separase.
  • To understand how securin binding affects separase's catalytic activity and substrate interaction.

Main Methods:

  • Structural analysis of the separase-securin complex.
  • Biochemical assays to assess catalytic activity and binding interactions.

Main Results:

  • Securin binds to separase, with a key segment occupying the enzyme's active site.
  • This binding physically blocks substrate access, inhibiting separase's protease activity.
  • Securin also engages in extensive interactions outside the active site, stabilizing separase.

Conclusions:

  • Securin acts as a potent inhibitor of separase by blocking its active site.
  • The structural insights provide a molecular basis for separase regulation by securin.
  • Understanding this interaction is vital for developing targeted therapies for cancer and genome instability.