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Related Concept Videos

M-Cdk Drives Transition Into Mitosis02:15

M-Cdk Drives Transition Into Mitosis

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Checkpoints throughout the cell cycle serve as safeguards and gatekeepers, allowing the cell cycle to progress in favorable conditions and slow or halt it in problematic ones. This regulation is known as the cell cycle control system.
Cyclin-dependent kinases, or Cdks, work in concert with cyclins to control cell cycle transitions. M-Cdk, a complex of Cdk1 bound to M cyclin, is a well-known example of this coordinated control that drives the transition from the G2 to the M phase.
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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.
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The orderly progression of the cell cycle depends on the activation of Cdk protein by binding to its cyclin partner. However, the cell cycle must be restricted when undergoing abnormal changes. Most cancers correlate to the deregulated cell cycle, and since Cdks are a central component of the cell cycle, Cdk inhibitors are extensively studied to develop anticancer agents. For instance, cyclin D associates with several Cdks, such as Cdk 4/6, to form an active complex. The cyclin D-Cdk4/6 complex...
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Mitotic cell division results in daughter cells that exactly resemble the parent cell. However, errors in the DNA replication or distribution of genetic material may lead to genetic mutations that may be passed down to every new cell formed from the resulting abnormal cell. Propagation of such mutant cells is restricted through checkpoint mechanisms present at different stages of the cell cycle. These checkpoints involve regulator molecules that either promote or demote cell cycle events.
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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.
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Related Experiment Video

Updated: Oct 27, 2025

Combining Mitotic Cell Synchronization and High Resolution Confocal Microscopy to Study the Role of Multifunctional Cell Cycle Proteins During Mitosis
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Combining Mitotic Cell Synchronization and High Resolution Confocal Microscopy to Study the Role of Multifunctional Cell Cycle Proteins During Mitosis

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CDK1 controls CHMP7-dependent nuclear envelope reformation.

Alberto T Gatta1,2, Yolanda Olmos1,2, Caroline L Stoten1,2

  • 1School of Cancer and Pharmaceutical Sciences, King's College, London, United Kingdom.

Elife
|July 21, 2021
PubMed
Summary
This summary is machine-generated.

The Endosomal Sorting Complex Required for Transport-III (ESCRT-III) machinery aids nuclear envelope sealing. CDK1 phosphorylation of CHMP7 prevents its inappropriate assembly during mitosis, ensuring proper nuclear regeneration.

Keywords:
CDK1CHMPESCRTcell biocell biologyhumannuclear envelope

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Experimental Approaches to Study Mitochondrial Localization and Function of a Nuclear Cell Cycle Kinase, Cdk1
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Experimental Approaches to Study Mitochondrial Localization and Function of a Nuclear Cell Cycle Kinase, Cdk1
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Experimental Approaches to Study Mitochondrial Localization and Function of a Nuclear Cell Cycle Kinase, Cdk1

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The Endosomal Sorting Complex Required for Transport-III (ESCRT-III) machinery is crucial for nuclear envelope (NE) sealing during mitotic exit and repair during interphase rupture.
  • ESCRT-III assembly at the NE is initiated by the interaction of CHMP7 with LEM2, but its regulation during mitosis remains unclear.

Purpose of the Study:

  • To investigate the regulation of ESCRT-III assembly at the nuclear envelope during mitotic exit.
  • To elucidate the role of CHMP7 phosphorylation in controlling ESCRT-III localization and function.

Main Methods:

  • Live cell imaging
  • Protein biochemistry
  • Analysis of protein-protein interactions
  • Phosphorylation site mapping

Main Results:

  • CHMP7 is essential for dissolving LEM2 clusters at the NE during mitotic exit.
  • CDK1 phosphorylates CHMP7 at Ser3 and Ser441 upon mitotic entry, reducing its interaction with LEM2 and limiting assembly during M-phase.
  • Spatiotemporal dephosphorylation of CHMP7 allows its assembly at the NE during telophase but restricts it from the ER.
  • Loss of CDK1 phosphorylation leads to aberrant CHMP7 assembly in the ER during mitotic exit.

Conclusions:

  • CDK1-mediated phosphorylation of CHMP7 acts as a cell-cycle control mechanism to prevent inappropriate ESCRT-III assembly during mitosis.
  • This regulation ensures timely and spatially controlled nuclear envelope regeneration.
  • Microtubules are not required for ESCRT-III assembly at the reforming nuclear envelope.