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Related Concept Videos

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...
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.
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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Related Experiment Video

Updated: Jul 4, 2026

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

Nuclear HuR accumulation through phosphorylation by Cdk1.

Hyeon Ho Kim1, Kotb Abdelmohsen, Ashish Lal

  • 1Laboratory of Cellular and Molecular Biology, National Institute on Aging-Intramural Research Program, National Institutes of Health, Baltimore, Maryland 21224, USA.

Genes & Development
|July 3, 2008
PubMed
Summary
This summary is machine-generated.

The cell cycle kinase Cdk1 phosphorylates HuR protein during the G2 phase, influencing its location and function. This phosphorylation retains HuR in the nucleus, impacting mRNA translation and cell survival.

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Oligopeptide Competition Assay for Phosphorylation Site Determination
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Oligopeptide Competition Assay for Phosphorylation Site Determination

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Related Experiment Videos

Last Updated: Jul 4, 2026

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

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

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • HuR (Human antigen R) is a nuclear RNA-binding protein.
  • HuR translocates to the cytoplasm under stress and proliferative signals.
  • In the cytoplasm, HuR stabilizes or modulates target mRNA translation.

Purpose of the Study:

  • To investigate the role of HuR phosphorylation at S202 by Cdk1.
  • To determine how Cdk1-mediated phosphorylation affects HuR's subcellular distribution.
  • To understand the impact of HuR phosphorylation on its interaction with 14-3-3 and target mRNAs.

Main Methods:

  • Synchronous G2-phase cell cultures were used.
  • Cdk1 activity was modulated using inhibitory and activating interventions.
  • A novel anti-phospho-HuR(S202) antibody was employed.
  • Subcellular localization of HuR and its interaction with 14-3-3 were analyzed.

Main Results:

  • HuR phosphorylation at S202 by Cdk1 was specific to the G2 phase.
  • Inhibition of Cdk1 increased cytoplasmic HuR levels; activation decreased them.
  • Phospho-HuR(S202) was predominantly nuclear, while the nonphosphorylatable mutant HuR(S202A) was cytoplasmic.
  • Unphosphorylated HuR showed decreased association with 14-3-3 and increased binding to target mRNAs.

Conclusions:

  • Cdk1 phosphorylates HuR during G2 phase, retaining it in the nucleus via 14-3-3 association.
  • This phosphorylation hinders HuR's post-transcriptional function and anti-apoptotic effects.
  • The study elucidates a mechanism controlling HuR's nucleocytoplasmic shuttling and function.