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Related Concept Videos

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.
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.
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...
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...
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...
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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Related Experiment Video

Updated: Jul 1, 2026

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

Published on: October 26, 2015

The cyclin-dependent kinase 11 interacts with NOT2.

Jiaqi Shi1, Mark A Nelson

  • 1Department of Pathology, Arizona Cancer Center, University of Arizona, Tucson, AZ 85724, USA. sjq@email.arizona.edu

Biochemical and Biophysical Research Communications
|July 26, 2005
PubMed
Summary

Cyclin-dependent kinase 11 (CDK11) interacts with NOT2, a protein involved in apoptosis. This interaction suggests CDK11 regulates NOT2 activity, potentially independent of its kinase function, to influence cell death.

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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

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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

Published on: October 26, 2015

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

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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

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Cyclin-dependent kinase 11 (CDK11), a caspase-processed kinase, plays a role in apoptosis.
  • The precise mechanisms of apoptotic signaling mediated by CDK11(p46) remain largely unknown.

Purpose of the Study:

  • To elucidate the molecular mechanisms underlying CDK11(p46)-mediated apoptotic signaling.
  • To identify novel interacting partners of CDK11(p46) involved in apoptosis.

Main Methods:

  • Yeast two-hybrid screening to identify CDK11(p46) interacting proteins.
  • In vitro and in vivo co-immunoprecipitation assays to confirm protein interactions.
  • Subcellular localization studies using immunofluorescence microscopy.
  • Luciferase mRNA assays and apoptosis assays to assess functional consequences.

Main Results:

  • NOT2 was identified as a novel interacting partner of CDK11(p46).
  • Direct interaction between CDK11(p46) and NOT2 was confirmed in vitro and in human cells, mediated by the NOT domain of NOT2.
  • Both proteins predominantly co-localized in the nucleus.
  • NOT2 overexpression reduced luciferase mRNA levels and induced apoptosis, but NOT2 was not phosphorylated by CDK11(p46).

Conclusions:

  • CDK11(p46) interacts with NOT2, suggesting a role in regulating NOT2 function during apoptosis.
  • The findings indicate that CDK11 may influence apoptosis through mechanisms independent of its kinase activity, possibly by modulating NOT2 activity.