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Related Concept Videos

NF-κB-dependent Signaling Pathway02:26

NF-κB-dependent Signaling Pathway

The transcription factor NF-κB was discovered in 1986 in the lab of Nobel laureate Professor David Baltimore, for its interaction with the immunoglobulin light chain enhancer in B-cells. After more than three decades of study, it is now evident that NF-κB regulates the expression of over 100 genes. Most of these genes play an essential role in the innate and adaptive immune responses as well as the inflammatory responses of animals.
NF-κB-dependent Signaling Mechanism
The heterodimer of NF-κB...
NF-kB-dependent Signaling Pathway02:26

NF-kB-dependent Signaling Pathway

The transcription factor NF-κB was discovered in 1986 in the lab of Nobel laureate Professor David Baltimore, for its interaction with the immunoglobulin light chain enhancer in B-cells. After more than three decades of study, it is now evident that NF-κB regulates the expression of over 100 genes. Most of these genes play an essential role in the innate and adaptive immune responses as well as the inflammatory responses of animals.
NF-κB-dependent Signaling Mechanism
The heterodimer of NF-κB...
Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
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...
Negative Regulator Molecules01:23

Negative Regulator Molecules

Positive regulators allow a cell to advance through cell cycle checkpoints. Negative regulators have an equally important role as they terminate a cell’s progression through the cell cycle—or pause it—until the cell meets specific criteria.
The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...

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Related Experiment Video

Updated: Jun 18, 2026

A Guide to Production, Crystallization, and Structure Determination of Human IKK1/α
11:27

A Guide to Production, Crystallization, and Structure Determination of Human IKK1/α

Published on: November 2, 2018

Pim-1 controls NF-kappaB signalling by stabilizing RelA/p65.

K Nihira1, Y Ando, T Yamaguchi

  • 1Department of Molecular Genetics, Medical Research Institute, Tokyo Medical and Dental University, Yushima 1-5-45, Bunkyo-ku, Tokyo 113-8510, Japan.

Cell Death and Differentiation
|November 14, 2009
PubMed
Summary

The kinase Pim-1 phosphorylates RelA/p65 at Ser276, preventing its degradation and activating the NF-kappaB pathway. This phosphorylation is crucial for cellular responses and gene regulation.

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Last Updated: Jun 18, 2026

A Guide to Production, Crystallization, and Structure Determination of Human IKK1/α
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A Guide to Production, Crystallization, and Structure Determination of Human IKK1/α

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NF-κB-dependent Luciferase Activation and Quantification of Gene Expression in Salmonella Infected Tissue Culture Cells
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NF-κB-dependent Luciferase Activation and Quantification of Gene Expression in Salmonella Infected Tissue Culture Cells

Published on: January 12, 2020

Area of Science:

  • Molecular Biology
  • Cellular Signaling
  • Ubiquitin-Proteasome System

Background:

  • Protein degradation via the ubiquitin-proteasome system regulates cellular responses.
  • The NF-kappaB signaling pathway relies on ubiquitin-mediated proteolysis.
  • The precise mechanism of RelA/p65 ubiquitination and degradation is not fully understood.

Purpose of the Study:

  • To investigate the role of RelA/p65 phosphorylation in its degradation.
  • To identify kinases involved in RelA/p65 phosphorylation at Ser276.
  • To elucidate the function of Pim-1 in NF-kappaB signaling.

Main Methods:

  • Phosphorylation site analysis of RelA/p65.
  • Kinase identification using depletion and knockdown approaches.
  • Assessment of NF-kappaB target gene transactivation and signaling.

Main Results:

  • Phosphorylation of RelA/p65 at Ser276 inhibits its degradation by the ubiquitin-proteasome system.
  • Pim-1 kinase is identified as a key regulator of RelA/p65 Ser276 phosphorylation.
  • Pim-1 depletion impairs RelA/p65 transactivation, IL-6 production, and increases apoptosis.

Conclusions:

  • Pim-1 phosphorylation of RelA/p65 at Ser276 protects it from degradation.
  • This phosphorylation event is essential for NF-kappaB pathway activation and cellular responses.
  • Pim-1 plays a critical role in regulating RelA/p65 stability and function.