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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...
M-Cdk Drives Transition Into Mitosis02:15

M-Cdk Drives Transition Into Mitosis

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.
M cyclin...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Abnormal Proliferation02:23

Abnormal Proliferation

Under normal conditions, most adult cells remain in a non-proliferative state unless stimulated by internal or external factors to replace lost cells. Abnormal cell proliferation is a condition in which the cell's growth exceeds and is uncoordinated with normal cells. In such situations, cell division persists in the same excessive manner even after cessation of the stimuli, leading to persistent tumors. The tumor arises from the damaged cells that replicate to pass the damage to the daughter...

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Updated: May 29, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

Boosting and suppressing mitotic phosphorylation.

René H Medema1, Arne Lindqvist

  • 1Department of Medical Oncology and Cancer Genomics Center, UMC Utrecht, The Netherlands. r.h.medema@umcutrecht.nl

Trends in Biochemical Sciences
|October 1, 2011
PubMed
Summary
This summary is machine-generated.

Protein phosphorylation is key to mitosis, driving events like nuclear envelope breakdown. This review explores how cells manage widespread and localized protein dephosphorylation during mitotic exit.

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Last Updated: May 29, 2026

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

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Reversible protein phosphorylation is crucial for mitosis, regulating key events like nuclear envelope breakdown, chromosome condensation, and spindle assembly.
  • Global phosphoproteomic analysis reveals peak protein phosphorylation and phosphosite occupancy during mitosis.
  • Mitotic exit necessitates rapid and extensive protein dephosphorylation to reverse these modifications.

Purpose of the Study:

  • To review the mechanisms governing the global shift in protein phosphorylation during mitosis.
  • To discuss the mechanisms enabling precise spatial control of protein dephosphorylation for mitotic events.
  • To elucidate how cells manage both global and localized phosphorylation dynamics in mitosis.

Main Methods:

  • Global phosphoproteomic analysis to assess phosphorylation levels.
  • Review of existing literature on mitotic regulation.
  • Analysis of mechanisms controlling protein kinase and phosphatase activity.

Main Results:

  • Protein phosphorylation is globally elevated during mitosis.
  • Rapid and massive dephosphorylation occurs during mitotic exit.
  • Spatial control of protein (de)phosphorylation is critical for spindle assembly, chromosome disjunction, and alignment.

Conclusions:

  • Cells employ complex mechanisms to manage the dramatic global increase and subsequent reversal of protein phosphorylation during mitosis.
  • Localized regulation of protein phosphorylation/dephosphorylation is essential for accurate chromosome segregation and spindle function.
  • Understanding these dynamic phosphorylation events is key to comprehending mitotic progression.