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Related Concept Videos

Anaphase Promoting Complex00:50

Anaphase Promoting Complex

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...
Anaphase Promoting Complex00:50

Anaphase Promoting Complex

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...
Separation of Sister Chromatids02:17

Separation of Sister Chromatids

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...
Anaphase A and B01:39

Anaphase A and B

Microtubules form through the end-to-end polymerization of tubulin heterodimers. Kinetochore microtubules originate from the spindle poles, and their plus-ends connect with the kinetochores on sister-chromatids. Ndc80 protein complexes, present on the kinetochore, form low-affinity links with the plus end of these kinetochore microtubules.
Plus-end depolymerization releases tubulin heterodimers from the terminal region of the microtubule. As tubulin subunits are lost, the Ndc80 complexes detach...
Anaphase A and B01:39

Anaphase A and B

Microtubules form through the end-to-end polymerization of tubulin heterodimers. Kinetochore microtubules originate from the spindle poles, and their plus-ends connect with the kinetochores on sister-chromatids. Ndc80 protein complexes, present on the kinetochore, form low-affinity links with the plus end of these kinetochore microtubules.
Plus-end depolymerization releases tubulin heterodimers from the terminal region of the microtubule. As tubulin subunits are lost, the Ndc80 complexes detach...
The Spindle Assembly Checkpoint02:19

The Spindle Assembly Checkpoint

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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Related Experiment Video

Updated: May 27, 2026

Immunofluorescence Analysis of Endogenous and Exogenous Centromere-kinetochore Proteins
05:35

Immunofluorescence Analysis of Endogenous and Exogenous Centromere-kinetochore Proteins

Published on: March 3, 2016

Structural insights into anaphase-promoting complex function and mechanism.

David Barford1

  • 1Division of Structural Biology, Institute of Cancer Research, Chester Beatty Laboratories, 237 Fulham Road, London SW3 6JB, UK. david.barford@icr.ac.uk

Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
|November 16, 2011
PubMed
Summary
This summary is machine-generated.

The anaphase-promoting complex (APC/C) regulates cell division by marking proteins for destruction. Structural studies reveal how APC/C subunits and co-activators control target recognition for cell cycle progression.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The anaphase-promoting complex or cyclosome (APC/C) is a large E3 ubiquitin ligase crucial for cell cycle progression.
  • It controls sister chromatid segregation and mitotic exit by ubiquitinating key regulatory proteins.
  • APC/C activity and substrate specificity are tightly regulated by co-activators, phosphorylation, and inhibitory factors.

Purpose of the Study:

  • To review recent structural and biochemical findings on the APC/C.
  • To elucidate the roles of APC/C subunits and co-activators in substrate recognition.
  • To discuss regulatory mechanisms governing APC/C substrate binding and specificity.

Main Methods:

  • Literature review of recent structural and biochemical studies.
  • Analysis of APC/C subunit interactions and co-activator binding.
  • Examination of regulatory mechanisms influencing APC/C activity.

Main Results:

  • Structural insights reveal how APC/C core subunits and co-activators interact to mediate substrate recognition.
  • Understanding the structural basis of co-activator binding and conformation is key to APC/C regulation.
  • Mechanisms controlling co-activator accessibility and binding modulate APC/C substrate specificity.

Conclusions:

  • Structural and biochemical data are advancing our understanding of APC/C function.
  • The interplay between APC/C subunits and co-activators is critical for precise cell cycle control.
  • Regulation of substrate recognition is central to the APC/C's role in mitosis.