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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...
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...

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Related Experiment Video

Updated: May 31, 2026

Experimental Approaches to Study Mitochondrial Localization and Function of a Nuclear Cell Cycle Kinase, Cdk1
13:15

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

Published on: February 25, 2016

CDK9 interacts with a RanGTP-importin-β complex to regulate erythroid enucleation.

Lucas M Newton1,2,3,4,5, Krystle Y B Lim1,2, Donia Y Abeid1,2

  • 1Department of Biochemistry & Chemistry, La Trobe University, Melbourne, VIC 3073, Australia.

Journal of Cell Science
|February 20, 2026
PubMed
Summary
This summary is machine-generated.

Cyclin-dependent kinase 9 (CDK9) interacts with the importin-beta complex during red blood cell formation. This interaction is crucial for the final nuclear extrusion step in erythroid enucleation.

Keywords:
CDK9EnucleationErythropoiesisImportin-β

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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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A Murine Cell Line Based Model of Chronic CDK9 Inhibition to Study Widespread Non-Genetic Transcriptional Elongation Defects (TEdeff) in Cancers
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A Murine Cell Line Based Model of Chronic CDK9 Inhibition to Study Widespread Non-Genetic Transcriptional Elongation Defects (TEdeff) in Cancers

Published on: September 26, 2019

Related Experiment Videos

Last Updated: May 31, 2026

Experimental Approaches to Study Mitochondrial Localization and Function of a Nuclear Cell Cycle Kinase, Cdk1
13:15

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

Published on: February 25, 2016

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

A Murine Cell Line Based Model of Chronic CDK9 Inhibition to Study Widespread Non-Genetic Transcriptional Elongation Defects (TEdeff) in Cancers
10:49

A Murine Cell Line Based Model of Chronic CDK9 Inhibition to Study Widespread Non-Genetic Transcriptional Elongation Defects (TEdeff) in Cancers

Published on: September 26, 2019

Area of Science:

  • Cell Biology
  • Hematopoiesis
  • Molecular Biology

Background:

  • Erythroid enucleation is the final step in red blood cell development.
  • CDK9 was previously identified as a regulator of this process.
  • CDK9's role appeared independent of its known transcriptional functions.

Purpose of the Study:

  • To identify the interactome of CDK9 in differentiating erythroblasts.
  • To elucidate the novel role of CDK9 in erythroid enucleation.

Main Methods:

  • Co-immunoprecipitation and mass spectrometry to identify CDK9 interactors.
  • Functional assays and imaging analysis of erythroblasts.
  • Inhibition of importin-beta in erythroblasts.

Main Results:

  • CDK9 interacts with a RanGTP-Importin-β complex during erythroid differentiation.
  • Inhibition of importin-beta disrupts erythroid enucleation.
  • CDK9 and importin-β colocalize at the site of nuclear extrusion.
  • A novel physical link between CDK9 and importin-β activity precedes CaM/Ca2+ and F-actin signaling.

Conclusions:

  • CDK9 plays a critical role in erythroid enucleation through interaction with the importin-β complex.
  • This interaction is independent of CDK9's transcriptional role.
  • CDK9 and importin-β represent a novel pathway regulating nuclear extrusion during red blood cell formation.