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Related Concept Videos

Positive Regulator Molecules02:39

Positive Regulator Molecules

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.
Positive Regulator Molecules01:45

Positive Regulator Molecules

To consistently produce healthy cells, the cell cycle—the process that generates daughter cells—must be precisely regulated.
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...
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...
Inhibition of Cdk Activity02:34

Inhibition of Cdk Activity

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...
Inhibition of CDK Activity02:34

Inhibition of CDK Activity

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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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

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

Published on: May 3, 2018

Assembly, activation, and substrate specificity of cyclin D1/Cdk2 complexes.

Stephan C Jahn1, Mary E Law, Patrick E Corsino

  • 1Department of Pharmacology and Therapeutics and the ‡Shands Cancer Center, University of Florida , Gainesville, Florida 32610, United States.

Biochemistry
|May 1, 2013
PubMed
Summary

The protein p21 acts as a scaffold, enabling cyclin D1 and cyclin-dependent kinase 2 (Cdk2) to form active complexes. These complexes phosphorylate key cancer-related proteins, influencing cellular activity.

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Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
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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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Last Updated: May 11, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

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Published on: May 3, 2018

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
10:33

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

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Combining Mitotic Cell Synchronization and High Resolution Confocal Microscopy to Study the Role of Multifunctional Cell Cycle Proteins During Mitosis
08:33

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

Published on: December 5, 2017

Area of Science:

  • Molecular Biology
  • Cell Cycle Regulation
  • Cancer Biology

Background:

  • Conflicting data exists on cyclin D1/cyclin-dependent kinase 2 (Cdk2) complex activity.
  • Cyclin D1 is frequently overexpressed in various cancers, highlighting the need to understand its interactions.
  • The role of p21 in regulating cyclin D1/Cdk2 complex formation and function remains unclear.

Purpose of the Study:

  • To investigate the role of p21 in the formation and activity of cyclin D1/Cdk2 complexes.
  • To identify novel substrates phosphorylated by cyclin D1/Cdk2 complexes.
  • To explore the implications of p21-mediated complex formation in cancer.

Main Methods:

  • Utilized a novel p21-PCNA fusion protein and p21 mutant proteins.
  • Assessed the ability of cyclin D1 and Cdk2 to complex in the presence and absence of p21.
  • Investigated the kinase activity of formed complexes and identified their substrates through phosphorylation assays.

Main Results:

  • p21 is essential for cyclin D1 and Cdk2 complex formation; they do not associate without p21.
  • The p21/cyclin D1/Cdk2 complexes are kinase-active and bind to the trimeric PCNA complex.
  • Increased p21 levels enhance cyclin D1/Cdk2 complex formation and activity, leading to phosphorylation of Nucleophosmin, Cdh1, and PSF.

Conclusions:

  • p21 functions as a crucial scaffolding protein for active cyclin D1/Cdk2 complex formation.
  • Cyclin D1/Cdk2 complexes phosphorylate proteins involved in centrosome replication and chromosomal instability, suggesting a role in cancer.
  • PSF is identified as a novel Cdk2 substrate, with potential implications for cellular activity.